Ex Parte Salfeld et al

Patent Trial and Appeal Board

May 15, 2017

13736931 (P.T.A.B. May. 15, 2017)

UNITED STATES PATENT AND TRADEMARK OFFICE
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/736,931 01/08/2013 Jochen G. SALFELD 3685.001000C/EKS/KRM 6933
135005 7590 05/16/2017
STERNE, KESSLER, GOLDSTEIN & FOX P.L.L.C.
1100 NEW YORK AVENUE, N.W.
WASHINGTON, DC 20005
EXAMINER
ROMEO, DAVID S
ART UNIT PAPER NUMBER
1647
MAIL DATE DELIVERY MODE
05/16/2017 PAPER
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
PTOL-90A (Rev. 04/07)
FF1. UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte JOCHEN G. SALFELD, DEBORAH J. ALLEN,
ZEHRA KAYMAKCALAN, BORIS LABKOVSKY,
JOHN A. MANKOVICH, BRIAN T. MCGUINNESS,
ANDREW J. ROBERTS, PAUL SAKORAFAS,
HENDRICUS R.J.M. HOOGENBOOM, DAVID SCHOENHAUT,
TRISTAN J. VAUGHAN, MICHAEL WHITE, and ALISON J. WILTON1
____________

Appeal 2015-007511
Application 13/736,931
Technology Center 1600
____________

Before FRANCISCO C. PRATS, JEFFREY N. FREDMAN, and
RYAN H. FLAX, Administrative Patent Judges.

FLAX, Administrative Patent Judge.

DECISION ON APPEAL
This is a decision on appeal under 35 U.S.C. § 134(a) involving
claims directed to a liquid pharmaceutical composition for the treatment of a
disorder in which TNFα is detrimental. Claim 20 is on appeal as rejected
under the doctrine of non-statutory obviousness type double patenting. We
have jurisdiction under 35 U.S.C. § 6(b).
We affirm.

1 Appellants identify the Real Party in Interest as AbbVie Biotechnology
Ltd. App. Br. 3.
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STATEMENT OF THE CASE
Antibodies are proteins (also called immunoglobulins) normally
produced by certain white blood cells (plasma cells) in response to entry into
the body of a foreign substance (antigen) in order to render it harmless.2
The Specification states, “[t]umor necrosis factor α (TNFα) is a
cytokine produced by numerous cell types, including monocytes and
macrophages, that was originally identified based on its capacity to induce
the necrosis of certain mouse tumors.” Spec. 1:20–22. Further,
[b]ecause of the harmful role of human TNFα (hTNFα) in a
variety of human disorders, therapeutic strategies have been
designed to inhibit or counteract hTNFα activity. In particular,
antibodies that bind to, and neutralize, hTNFα have been sought
as a means to inhibit hTNFα activity. Some of the earliest of
such antibodies were mouse monoclonal antibodies (mAbs),
secreted by hybridomas prepared from lymphocytes of mice
immunized with hTNFα.
Id. at 1:33–2:2.
“Th[e] invention provides human antibodies, preferably recombinant
human antibodies, that specifically bind to human TNFα.” Id. at 3:25–26.
Appellants explain,
Claim 20 relates to a liquid pharmaceutical composition
for the treatment of a disorder in which TNFα is detrimental,
comprising a recombinant anti-TNFα antibody produced by
Chinese hamster ovary (CHO) cells and a pharmaceutically
acceptable carrier. The claimed antibody has light and heavy
variable regions corresponding to adalimumab (sold under the

2 Oxford Dictionary of Biology 7th ed., antibody (2015), available at
http://www.oxfordreference.com/view/10.1093/acref/9780198714378.001.0
001/acref-9780198714378-e-262?rskey=hYIlYh&result=301 (visited May
10, 2017).
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trade name HUMIRA®), which was the first fully human
monoclonal antibody approved by the United States Food and
Drug Administration (FDA).
App. Br. 10 (internal footnotes omitted). Appellants further explain,
HUMIRA® is approved for use in the treatment of
multiple diseases, including moderate to severe rheumatoid
arthritis, psoriatic arthritis, ankylosing spondylitis, moderate to
severe Crohn’s disease, moderate to severe polyarticular juvenile
idiopathic arthritis, and moderate to severe plaque psoriasis, and
has proven to be highly effective and safe as a therapeutic
antibody due, at least in part, to its minimal levels of
immunogenicity in human patients.
Id. at 11 (internal footnote omitted).
The appealed claim can be found in the Claims Appendix of the
Appeal Brief; it reads as follows:
20. A liquid pharmaceutical composition for the treatment of a
disorder in which TNFα is detrimental, comprising a
recombinant anti-TNFα antibody produced by Chinese hamster
ovary (CHO) cells and a pharmaceutically acceptable carrier,
wherein the antibody comprises a human kappa light chain
constant region and a human IgG1 heavy chain constant region,
wherein the light chain variable domain of the antibody
comprises the amino acid sequence of SEQ ID NO:1, and the
heavy chain variable domain of the antibody comprises the
amino acid sequence SEQ ID NO:2, and
wherein the liquid composition is suitable for subcutaneous
injection in a human subject.
App. Br. 65 (Claims App’x).
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The following rejections are on appeal:3
A. Claim 20 stands rejected on the ground of nonstatutory
obviousness-type double patenting over claims 1–5 and 7 of Salfeld 8134 in
view of Ramage,5 Goochee,6 and Trill.7 Ans. 4.
B. Claim 20 stands rejected on the ground of nonstatutory
obviousness-type double patenting over claims 18–41 and 54–56 of
Salfeld 8948 in view of Le,9 Ramage, Goochee, and Trill. Ans. 54–55.
C. Claim 20 stands rejected on the ground of nonstatutory
obviousness-type double patenting over claims 1–6 of Salfeld 40110 in view
of Ramage, Goochee, and Trill. Ans. 60.
D. Claim 20 stands rejected on the ground of nonstatutory
obviousness-type double patenting over claims 1–15, 27–40, 52–60, 72–79,

3 Claim 20 was also rejected over U.S. Patent Application No. 14/183,845,
which was abandoned January 6, 2016. The respective rejection is
dismissed as moot.
4 U.S. Patent No. US 8,197,813 B2 (issued June 12, 2012 to Jochen G.
Salfeld et al.) (“Salfeld 813”).
5 U.S. Patent No. 5,644,036 (issued July 1, 1997 to Paul Ian Nicholas
Ramage and Geoffrey Allen) (“Ramage”).
6 Charles F. Goochee et al., The Oligosaccharides of Glycoproteins:
Bioprocess Factors Affecting Oligosaccharide Structure and their Effect On
Glycoprotein Properties, 9 BIOTECH 1347–55 (1991) (“Goochee”).
7 John J. Trill et al., Production of Monoclonal Antibodies in COS and CHO
Cells, 6 CURRENT OP. IN BIOTECH 553–60 (1995) (“Trill”).
8 U.S. Patent No. US 8,414,894 B2 (issued Apr. 9, 2013 to Jochen G. Salfeld
et al.) (“Salfeld 894”).
9 U.S. Patent No. 5,656,272 (issued Aug. 12, 1997 to Junming Le et al.)
(“Le”).
10 U.S. Patent No. US 8,372,401 B2 (issued Feb. 12, 2013 to Jochen G.
Salfeld et al.) (“Salfeld 401”).
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91–99, 111–118, 130–132 of Salfeld 76111 in view of Gombotz,12 Ramage,
Goochee, and Trill. Ans. 65.
E. Claim 20 stands rejected on the ground of nonstatutory
obviousness-type double patenting over claims 1–30 of Salfeld 38213 in view
of Ramage, Goochee, and Trill. Ans. 70.

FINDINGS OF FACT
Unless otherwise indicated herein, we adopt the Examiner’s findings
of fact, reasoning on scope and content of the prior art, and conclusions set
out in the Final Action and Answer regarding the rejection. We set forth the
following findings of fact to highlight certain evidence.
FF2. Salfeld 813 claims 1, 4, 5, and 7 recite:
1. An isolated human antibody, or an antigen-binding portion
thereof, that dissociates from human TNFα (hTNFα) with a Kd
of 1 x 10-8 M or less and a Koff rate constant of 1 x 10-3 s-1 or less,
both determined by surface plasmon resonance, and inhibits
human TNFα-induced expression of ELAM-1 on human
umbilical vein endothelial cells.
4. The isolated human antibody, or antigen-binding portion
thereof, of claim 1, which is a recombinant antibody, or antigen-
binding portion thereof.
5. The isolated human antibody of claim 1, which has an IgG1
heavy chain constant region.

11 U.S. Patent No. US 7,588,761 B2 (issued Sept. 15, 2009 to Jochen G.
Salfeld et al.) (“Salfeld 761”).
12 U.S. Patent No. 6,036,978 (issued Mar. 14, 2000 to Wayne R. Gombotz
and SiowFong Wee) (“Gombotz”).
13 U.S. Patent No. 6,090,382 (issued July 18, 2000 to Jochen G. Salfeld et
al.) (“Salfeld 382”).
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7. A pharmaceutical composition comprising the isolated human
antibody of claim 1, and a pharmaceutically acceptable carrier.
Salfeld 813 51:2–52:10; see also Final Action 4–7, 19–20, and Ans. 3,
4–5, 7, 15, 36, 40, 48–49, 52–53 (discussing Salfeld 813).
FF3. Salfeld 894 claims 38–40 and 55 recite:
38. The isolated human antibody, or antigen-binding portion
thereof, of claim 18 or 25, with a light chain variable region
(LCVR) comprising the amino acid sequence of SEQ ID NO: 1
and a heavy chain variable region (HCVR) comprising the amino
acid sequence of SEQ ID NO: 2.
39. The isolated human antibody, or antigen-binding portion
thereof, of claim 18 or 25, which has an IgG1 or an IgG4 heavy
chain constant region.
40. The isolated human antibody, or antigen-binding portion
thereof, of claim 18 or 25, which has a kappa light chain constant
region.
55. A pharmaceutical composition comprising an isolated human
antibody, or antigen-binding portion thereof, which dissociates
from human TNFα with a Kd of 1 x 10-8 M or less and a Koff rate
constant of 1 x 10-3 s-1 or less, both determined by surface
plasmon resonance, and neutralizes human TNFα cytotoxicity in
a standard in vitro L929 assay with an IC50 of 1-10-7 M or less,
and a pharmaceutically acceptable carrier,
wherein the composition is suitable for administration
according to a mode selected from the group consisting of
an intravenous injection, a subcutaneous injection, an
intraperitoneal injection, and an intramuscular injection.
Salfeld 894 53:24–35, 54:53–63; see also Final Action 28–33, and
Ans. 3, 54–55, 57–59 (discussing Salfeld 894).
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FF4. Salfeld 401 claims 1 and 5 recite:
1. An isolated human anti-TNFα antibody, or an antigen-binding
portion thereof, comprising a light chain variable region (LCVR)
comprising the amino acid sequence of SEQ ID NO: 1 and a
heavy chain variable region (HCVR) comprising the amino acid
sequence of SEQ ID NO: 2, wherein the antibody, or antigen-
binding portion thereof, comprises an IgG1 heavy chain constant
region and a kappa light chain constant region.
5. A pharmaceutical composition comprising the antibody, or
antigen-binding portion thereof, of claim 1, and a
pharmaceutically acceptable carrier.
Salfeld 401 49:60–67, 51, 4–6; see also Final Action 33–37, and Ans.
3, 60, 62–64 (discussing Salfeld 401).
FF5. Salfeld 761 claims 78–80 recite:
78. A composition comprising an absorption delaying agent and
a human antibody that binds TNFα and is the antibody D2E7, or
an antigen-binding portion thereof.
79. A pharmaceutical composition comprising the antibody, or
antigen-binding portion thereof, of claim 78, and a
pharmaceutically acceptable carrier.
80. A method for treating a subject suffering from a disorder in
which TNFα activity is detrimental comprising administering to
the subject the pharmaceutical composition of claim 79.
Salfeld 761 55:14–23; see also Final Action 37–41, and Ans. 3, 65,
67–69 (discussing Salfeld 761).
FF6. “Antibody D2E7” is the human anti-TNFα antibody found
in Humira®, also called adalimumab. App. Br. 10 n.7.
FF7. Salfeld 382 claims 15, 16, and 24 recite:
15. An isolated human antibody, or an antigen binding portion
thereof, with a light chain variable region (LCVR) comprising
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the amino acid sequence of SEQ ID NO: 1 and a heavy chain
variable region (HCVR) comprising the amino acid sequence of
SEQ ID NO: 2.
16. The isolated human antibody of claim 15, which has an IgGl
heavy chain constant region.
24. A pharmaceutical composition comprising the antibody, or
antigen-binding portion thereof, of any one of claims 1-23, and a
pharmaceutically acceptable carrier.
Salfeld 382 56:57–63, 57:28–30; see also Final Action 42–45, and
Ans. 3, 70, 72–74 (discussing Salfeld 382).
FF8. It is not disputed that the “human antibody,” “human anti-
TNFα antibody,” “human antibody that binds TNFα,” “antibody [that]
comprises the amino acid sequence of SEQ ID NO: 1, and . . . the
amino acid sequence of SEQ ID NO: 2” and “the antibody D2E7,”
recited by the various claims of the Salfeld patents identified in the
findings of fact, supra, and the “anti-TNFα antibody” and “antibody
[that] comprises the amino acid sequence of SEQ ID NO:1, and . . .
the amino acid sequence SEQ ID NO:2,” recited by appealed claim
20, are the same. See generally App. Br. and Reply Br.
FF9. Ramage “relates to a purified preparation of monoclonal
antibodies against the antigen CDw52, to their use in therapy and to
processes for their production” (Ramage 1:9–11), in particular, to “an
IgG1 antibody, [which] has been humanized[,] . . . known as Campath
1H” (id. 2:1–3) (a lymphoma cancer treatment). See also Final Action
3–7, 12, and 14–17, and Ans. 3–4, 6–7, 9–11, and 14–15 (discussing
Ramage). Ramage discloses “the purified anti-CDw52 antibody of the
invention may be a . . . human antibody.” Ramage 6:9–10; see also
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Final Action 4, 7, 11, 26–29, 33, 37–38, 41, 42, and 45, and Ans. 3, 4–
5, 14–15, 17–18, 24–26, 29–30, 34–36, 38–40, 42–43, 46–48, 54, 55–
56–57, 59, 60–61, 64, 65–66, 69–71, and 74–75 (discussing Ramage).
FF10. Ramage discloses that “[a]ntibodies which are intended for
use in medical therapy may need to be administered repeatedly, so the
need to remove foreign immunoglobulins is important as such
administration may produce an immune response and induce
nephrotoxicity, serum sickness and in severe cases anaphylactic
shock.” Ramage 2:15–20; see also Final Action 4, 7, 11, 26–29, 33,
37–38, 41, 42, and 45, and Ans. 3, 4–5, 14–15, 17–18, 24–26, 29–30,
34–36, 38–40, 42–43, 46–48, 54, 55–56–57, 59, 60–61, 64, 65–66,
69–71, and 74–75 (discussing Ramage).
FF11. Ramage discloses “use of a purified preparation of an anti-
CDw52 antibody in the manufacture of a medicament . . . [for]
treating a human being.” Ramage 6:50–54; see also Final Action 4, 7,
11, 26–29, 33, 37–38, 41, 42, and 45, and Ans. 3, 4–5, 14–15, 17–18,
24–26, 29–30, 34–36, 38–40, 42–43, 46–48, 54, 55–56–57, 59, 60–61,
64, 65–66, 69–71, and 74–75 (discussing Ramage).
FF12. Ramage discloses “[s]uch formulations preferably include,
in addition to antibody, a physiologically acceptable diluent or carrier
. . . . Suitable carriers include but are not limited to physiological
saline . . . . Routes of administration are routinely parenteral
including intravenous, intramuscular, subcutaneous and
intraperitoneal injection or delivery.” Ramage 6:64–7:10; see also
Final Action 4, 7, 11, 26–29, 33, 37–38, 41, 42, and 45, and Ans. 3, 4–
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5, 14–15, 17–18, 24–26, 29–30, 34–36, 38–40, 42–43, 46–48, 54, 55–
56–57, 59, 60–61, 64, 65–66, 69–71, and 74–75 (discussing Ramage).
FF13. Ramage discloses that “[a]ntibodies according to the
invention may be prepared using a recombinant expression system,
the preferred system is a mammalian expression system using Chinese
hamster ovary (CHO) cells.” Ramage 3:52–55; see also Final Action
4, 7, 11, 26–29, 33, 37–38, 41, 42, and 45, and Ans. 3, 4–5, 14–15,
17–18, 24–26, 29–30, 34–36, 38–40, 42–43, 46–48, 54, 55–56–57, 59,
60–61, 64, 65–66, 69–71, and 74–75 (discussing Ramage).
FF14. Goochee discloses that workers in the relevant technical
field have
detected the presence of the Galα(1,3)Gal epitope on the
surface of SP/2 myeloma cells and on secreted mouse
monoclonal antibodies. . . . In contrast, the Galα(1,3)Gal epitope
is not found on the cell surface of many cultured human cells,
including normal human fibroblasts and the HL60 and HeLa cell
lines. This epitope is also not apparent in glycoproteins from
recombinant CHO cells, including human interferon-B1, EPO,
and t-PA, nor is if found in EPO produced by recombinant BHK
cells. These data suggest that α(1,3)galactosyltransferase
activity in these two rodent cell types is diminished or absent.
The CHO cell line does harbor DNA that hybridizes with a probe
or a murine α(1,3)galactosyltransferase, but northern blot
analysis reveals no evidence of α(1,3)galactosyltransferase
message in CHO cells.
Goochee 1350 (internal citations omitted); see also Final Action 4–5,
15, 17, 18, 21, 24–26, 28, 30, 33–34, 37–38, and 42–43, and Ans. 3–5,
8, 13–18, 22–24, 29, 33, 36, 38–40, 42–43, 45–48, 54–56, 60–61, 65–
66, and 70–71 (discussing Goochee).
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FF15. Goochee discloses “approximately 100 µg/ml of human
IgG recognize the ‘Galα(1,3)Gal’ structure generated by mammalian
cell lines possessing α(1,3)galactosyltransferase.” Goochee 1351
(internal citations omitted); see also Final Action 4–5, 15, 17, 18, 21,
24–26, 28, 30, 33–34, 37–38, and 42–43, and Ans. 3–5, 8, 13–18, 22–
24, 29, 33, 36, 38–40, 42–43, 45–48, 54–56, 60–61, 65–66, and 70–71
(discussing Goochee).
FF16. Further to the preceding findings of fact regarding
Goochee, Goochee discloses:
Human EPO produced by recombinant CHO cells is the
only recombinant therapeutic glycoprotein for which extensive
clinical trial data involving antibody development has been
published. No antibodies against recombinant EPO have been
detected in patients receiving this product, even after chronic
administration up to 18 months. Takeuchi and coworkers have
reported the oligosaccharide structures from human urinary EPO
and recombinant CHO-derived EPO to be essentially identical,
with the exception that the CHO-produced material contains
sialic acid only in an α2,3 linkage, while the human urinary
material contains both the α2,3 and α2,6 linkages. The absence
of antibodies to EPO from recombinant CHO is an important and
encouraging result.
Goochee 1351 (internal citations omitted); see also Final Action 4–5,
15, 17, 18, 21, 24–26, 28, 30, 33–34, 37–38, and 42–43, and Ans. 3–5,
8, 13–18, 22–24, 29, 33, 36, 38–40, 42–43, 45–48, 54–56, 60–61, 65–
66, and 70–71 (discussing Goochee).
FF17. Further to the preceding findings of fact regarding
Goochee, Goochee concludes: “Chinese hamster ovary cells have
emerged as the cell line of first choice for the synthesis of
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recombinant human therapeutic glycoproteins, although CHO cells do
poses deficiencies that may limit their applicability in specific cases
. . . .” Goochee 1353; see also Final Action 4–5, 15, 17, 18, 21, 24–
26, 28, 30, 33–34, 37–38, and 42–43, and Ans. 3–5, 8, 13–18, 22–24,
29, 33, 36, 38–40, 42–43, 45–48, 54–56, 60–61, 65–66, and 70–71
(discussing Goochee).
FF18. Trill is directed to the production of monoclonal antibodies
in COS and CHO cells and discloses “[i]n order to meet the demand
for clinical supplies, a gradual increase has occurred in the usage of
dihydrofolate reductase negative (DHFR-) Chinese hamster ovary
(CHO) cells for large-scale antibody production,” and “[u]sing a
variety of mammalian expression vectors and selection/amplification
protocols, CHO cell lines capable of producing monoclonal antibodies
at levels exceeding 1gl-1 can now be obtained in an almost routine
fashion.” Trill 553 (abstract); see also Final Action 4–5, 22–23, 28,
30, 33–34, 37–39, and 42–43, and Ans. 4–6, 14–15, 17–21, 28–29, 36,
40, 43, 46–48, 53–56, 60–61, 65–66, and 70–72 (discussing Trill).
FF19. Trill disclosed:
In the recent past, myeloma cells (SP 2/0, YB 2/0, NSO and
P3X63.Ag8.653) were primarily used for high-level production
of mAbs. Over the past few years, however, more and more
laboratories have been reporting the successful use of DHFR–
CHO cells (DUKX–B11 and DG–44) for high-level mAb
production. For example, Page and Sydenham used DUKX–B11
CHO cells to generate a stable cell line expressing the humanized
mAb Campath-1H at levels of 100 milligrams per 106 cells per
day. Using the same host cells, Fouser et al. reported the
generation of cell lines expressing a chimeric anti-ganglioside
GD2 antibody at 80–110 milligrams per 106 cells per day.
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Recently, Reff et al. have reported the utility of DG44 CHO cells
in producing a chimeric antibody against CD20 at levels of 30
milligrams per 106 cells per day after only one round of gene
amplification (see below).
Trill 555 (internal citations omitted); see also Final Action 4–5, 22–
23, 28, 30, 33–34, 37–39, and 42–43, and Ans. 4–6, 14–15, 17–21,
28–29, 36, 40, 43, 46–48, 53–56, 60–61, 65–66, and 70–72
(discussing Trill).
FF20. Further to the preceding findings of fact relating to Trill,
Trill identifies the following advantages offered by protein (mAb)
production via CHO cells: (1) cells are readily transfectable; (2) able
to grow in suspension and serum-free medium; (3) capable of growth
at high densities; (4) based on all data, no differences exist in the
function of mAbs produced in either myeloma or CHO cells; (5) well
established track record for expressing heterologous gene products
(other than mAbs); (6) proven successful in the co-expression of
foreign genes, such as those encoding glutamine synthetase (GS),
adenosine deaminase (ADA), and DHFR; (7) reports describing the
modification of CHO cells to express heterologous proteins quickly
and at high levels (e.g., stable expression of adenovirus E1A); and (8)
high-level expression achieved. Trill 555–56; see also Final Action
4–5, 22–23, 28, 30, 33–34, 37–39, and 42–43, and Ans. 4–6, 14–15,
17–21, 28–29, 36, 40, 43, 46–48, 53–56, 60–61, 65–66, and 70–72
(discussing Trill).
FF21. Le is directed to “[a]nti-TNF antibodies, fragments and
regions thereof which are specific for human tumor necrosis factor-α
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(TNFα) and are useful in vivo for diagnosis and therapy of a number
of TNFα-mediated pathologies and conditions . . . .” Le Abstract; see
also Final Action 28–29, and Ans. 54–55 and 58–59 (discussing Le).
FF22. Le discloses that, in expressing anti-TNF peptides of Ab
fragments,
[p]referred hosts are bacterial or eukaryotic hosts
including bacteria, yeast, insects, fungi, bird and mammalian
cells either in vivo, or in situ, or host cells of mammalian, insect,
bird or yeast origin. It is preferred that the mammalian cell or
tissue is of human, primate, hamster, rabbit, rodent, cow, pig,
sheep, horse, goat, dog or cat origin, but any other mammalian
cell may be used.
Le 26:30–36; see also Final Action 28–29, and Ans. 54–55 and 58–59
(discussing Le).
FF23. Further to the immediately preceding finding of fact, Le
discloses:
Preferred hosts are mammalian cells, grown in vitro or in
vivo. Mammalian cells provide post-translational modifications
to immunoglobulin protein molecules including leader peptide
removal, folding and assembly of H and L chains, glycosylation
of the antibody molecules, and secretion of functional antibody
protein.
Mammalian cells which can be useful as hosts for the
production of antibody proteins, in addition to the cells of
lymphoid origin described above, include cells of fibroblast
origin, such as Vero (ATCC CRL 81) or CHO-K1 (ATCC CRL
61).
Le 30:13–23; see also Final Action 28–29, and Ans. 54–55 and 58–59
(discussing Le).
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FF24. Le discloses:
treatment compris[ing] parenterally administering a single
or multiple doses of the antibody, fragment or derivative.
Preferred for human pharmaceutical use are high affinity potent
hTNFα-inhibiting and/or neutralizing murine and chimeric
antibodies, fragments and regions of this invention.
. . . [And] [b]ecause proteins are subject to being digested
when administered orally, parenteral administration, i.e.,
intravenous, subcutaneous, intramuscular, would ordinarily be
used to optimize absorption.
Le 35:10–24; see also Final Action 28–29, and Ans. 54–55 and 58–59
(discussing Le).
FF25. Gombotz discloses:
This invention pertains to controlled release
pharmaceutical compositions containing a polypeptide
[including a monoclonal antibody that is immunoreactive against
TNFα, IL-6 or IL-1] and a salt of an alginic acid. This invention
also is directed to methods of treating inflammatory bowel
diseases that are mediated by tumor necrosis factor, interleukin-
6 or interleukin-1 by administering such controlled enteric
release formulations to a patient.
Gombotz 1:10–16, 2:56–64, 4:16–17; see also Final Action 37 and 41,
and Ans. 3, 65, and 70 (discussing Gombotz).
FF26. Smith14 discloses that “the α1,3-galactosyltransferase . . .
transfers Gal from UDP-Gal in α1,3-linkage” and, unless engineered
to do so, CHO cells do not contain murine α1,3-galactosyltransferase
genomic DNA sequences and do not exhibit α1,3-galactosyltransferse

14 Smith et al., Transfer and Expression of a Murine UDP-Gal:β-D-Gal-
αl,3-Galactosyltransferase Gene in Transfected Chinese Hamster Ovary
Cells, 265 J. BIO. CHEM. 6225–34 (1990) (“Smith”).
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activity. Smith 6225, 6232; see also Final Action 17, 19, and 25, and
Ans. 4, 23, 39, 42, and 45 (discussing Smith).
FF27. Appellants state, “Appellants do not dispute that it was
known in the prior art that CHO cells did not express α-1,3-
galactosyltransferase” (App. Br. 36) and further concede, “[t]he
person of ordinary skill may have even been motivated to try CHO
cells given the fact that CHO cells lack α-1,3-galactosyltransferase”
(Reply Br. 15).
FF28. Appellants contend the person of ordinary skill in the art:
in February 1996, is a Senior Scientist with experience in the
discovery, production and characterization of therapeutic
antibodies, including murine, chimeric or humanized
monoclonal antibodies. This hypothetical person of ordinary
skill in the art also has experience with research-scale
manufacturing, ultimately leading to commercial scale
manufacturing (given that the antibody is part of a
pharmaceutical composition). This ordinarily skilled person is
either: (A) a person with at least a Bachelor’s degree in biology,
chemistry, biochemistry, chemical engineering, or a related field
who has multiple years of experience in antibody production in
an industrial setting; or (B) a person with an advanced degree
(M.S. or Ph.D.) in biology, chemistry, biochemistry, chemical
engineering, or a related field who has at least 2-3 years of
experience in antibody production in an industrial setting.
Declaration Under 37 C.F.R. § 1.132 of Dr. Peter Mezes (dated Sept.
4, 2014) (“Mezes Decl.”) ¶ 12. The Examiner does not contend
otherwise and we accept this as representative of the relevant level of
skill in the art.
FF29. As of February 9, 1996, there would have been motivation
to produce a human anti-TNFα antibody, according to appealed claim
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20, using Chinese Hamster Ovary (CHO) cells as host cells, as a
liquid pharmaceutical composition having a pharmaceutically
acceptable carrier, and suitable for subcutaneous injection in a human
subject, and the skilled artisan would have had a reasonable
expectation of successfully so doing. See findings of fact, supra.

DISCUSSION
I. CLAIM INTERPRETATION
There is a dispute regarding the interpretation of claim 20, specifically
the meaning of the claim language, “pharmaceutical” or “pharmaceutical
composition,” which impacts each determination of the Examiner and each
argument set forth by Appellants. See Reply Br. 3–5; App. Br. 17, 19–20,
22–26, 28, 31, 45, 48–49, 51, 52, and 54; Ans. 9–10, 15, 17, 19, 21–22, 24–
25, 27–30, and 43–44; and Final Action 24; see also Mezes Decl. ¶¶ 14, 16,
17, 18, 22–24, and 25 (“an industrial setting” and “commercial purposes”
established as the perspective from which declarant forms his opinions).
Claim 20 does not expressly recite producing antibodies on a commercial or
industrial scale or a product suitable for FDA approval or
commercialization. Thus, the issue to be resolved is whether the term
“pharmaceutical” (or “pharmaceutical composition”) invokes such
commercial and/or industrial production and/or regulatory-approval
concerns for the skilled artisan.
“Absent claim language carrying a narrow meaning, the PTO should
only limit the claim based on the specification or prosecution history when
those sources expressly disclaim the broader definition.” In re Bigio, 381
F.3d 1320, 1325 (Fed. Cir. 2004). The claim language is accorded its plain
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meaning under the broadest reasonable interpretation of the claims. Cuozzo
Speed Tech., LLC v. Lee, 136 S. Ct. 2131, 2145 (2016) (the Patent Office,
for more than 100 years, has applied the broadest reasonable construction
standard in proceedings). “The ordinary and customary [plain] meaning of a
claim term may be determined by reviewing a variety of sources. Some of
these sources include the claims themselves; dictionaries and treatises; and
the written description, the drawings, and the prosecution history.”
Brookhill-Wilk 1, LLC v. Intuitive Surgical, Inc., 334 F.3d. 1294, 1298 (Fed.
Cir. 2003) (citations omitted).
Appellants contend the Examiner did not give enough weight to the
claim term “pharmaceutical” when construing the claims and that the skilled
artisan’s choice of a host cell to produce the recited antibodies must take this
into account, i.e., consider commercialization requirements and FDA
regulations when analyzing motivation (for obviousness). Reply Br. 4.
Appellants contend the claim term “pharmaceutical” limits the invention to a
“commercial product (i.e., a pharmaceutical formulation)” and, in turn that
“‘liquid pharmaceutical formulation’” means “a commercial product which
would be produced on an industrial scale.” Id.; App. Br. 25–26. As support
for this position, Appellants cite the Macmillan dictionary and provide the
following definition of pharmaceutical: “relating to the production or sale
of medicines and drugs used for treating medical conditions.” Id.
Appellants also cite this same dictionary for a definition of formulation, as
follows: “a product such as a drug or skin cream.” Id. at 26.
The Examiner does not expressly interpret the claim term
“pharmaceutical,” but responded to Appellants’ arguments by finding that
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the claims do not require production on a commercial and/or
industrial scale. Nor do the claims require stable antibody
production and high yields. . . .
. . . [And,] there is no requirement in patent law that a person of
ordinary skill be motivated to develop the claimed invention
based on a rationale that forms the basis for FDA approval.
Ans. 21–22.
We look to the Specification to determine whether it assigned a
particular meaning to the term “pharmaceutical” (or “pharmaceutical
composition”). The Specification uses the term, but does not define it. See
Spec. 28:19–26. The Specification indicates that “pharmaceutical
compositions [can be] suitable for administration to a subject” and can
include “a pharmaceutically acceptable carrier,” which is identified by
several examples, which are identified as being “physiologically
compatible.” Id. Further, the Specification indicates that “pharmaceutical
compositions of the invention may include a ‘therapeutically effective
amount’ or a ‘prophylactically effective amount’ of an antibody or antibody
portion of the invention.” Spec. 34:3–5. Thus, we find the Specification
does not provide a definition for the claim term “pharmaceutical,” and we
find the claim should be interpreted per its plain meaning as would be
understood by the skilled artisan.
We consider Appellants’ evidence regarding their contended meaning
of “pharmaceutical,” identified, supra. Appellants unnecessarily introduce
into their proposed construction the term formulation, which is not a claim
term and is superfluous in view of the claim term composition, and then seek
to also construe this newly introduced term in addition to the claim term
pharmaceutical. We find this does not foster a better understanding of the
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disputed claim language. While the definition cited by Appellants from
Macmillan is a valid definition, it relates to the term pharmaceutical’s use as
a descriptive term, an adjective used to describe a characteristic of another
thing, e.g., a pharmaceutical company describes a company that makes
and/or sells pharmaceuticals. Claim 20, however, uses the term
pharmaceutical (or pharmaceutical composition) to identify a thing (as a
noun, that is, something for the treatment of a disorder in which TNFα is
detrimental). Thus, we look for a definition consistent with this usage.
We look to the Merriam-Webster dictionary, which defines the term
pharmaceutical (noun) as: “a medicinal drug.”15 Nowhere does the
Specification use the term pharmaceutical (or pharmaceutical composition)
in a way that is inconsistent with this definition or to invoke any
commercialization, industrial-scale production, or FDA-approvability
considerations. We understand “a medicinal drug” to be the plain meaning
of the term pharmaceutical (or pharmaceutical composition) as it would be
understood by one of ordinary skill in the art as of the invention date. Had
Appellants desired (or if they desire) a more restrictively defined invention
that does invoke concepts of commercialization, industrial-scale, and/or
FDA-approvability, properly specific and definitive claim language could
have been (or could be) used.

15 Merriam-Webster, pharmaceutical, available at https://www.merriam-
webster.com/dictionary/pharmaceutical (visited Apr. 27, 2017). (cf.
WEBSTER’S II NEW RIVERSIDE UNIVERSITY DICTIONARY 880 (1984)
(“Pharmaceutical . . . n. A drug or medication”)).
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We address Appellants’ arguments and evidence and the Examiner’s
determinations and evidence in view of this interpretation of the disputed
claim language.
II. OBVIOUSNESS-TYPE DOUBLE PATENTING
“[T]he law of obviousness-type double patenting looks to the law of
obviousness generally,” such that, “if the later expiring patent is ‘merely an
obvious variation of an invention disclosed and claimed in the [reference]
patent,’ the later expiring patent is invalid for obviousness-type double
patenting.” AbbVie Inc. v. Mathilda and Terence Kennedy Inst. of
Rheumatology Trust, 764 F.3d 1366, 1378–79 (Fed. Cir. 2014) (alteration in
original) (citing Amgen Inc. v. F. Hoffman-La Roche Ltd., 580 F.3d 1340
(Fed. Cir. 2009) and Eli Lilly & Co. v. Teva Parenteral Meds., Inc., 689 F.3d
1368 (Fed. Cir. 2012), and quoting In re Vogel, 422 F.2d 438, 41 (CCPA
1970)). “The non-claim portion of the earlier patent ordinarily does not
qualify as prior art against the patentee.” Id. at 1379 (quoting Eli Lilly, 689
F.3d at 1379).
“[O]bviousness is not demonstrated merely by showing that an earlier
expiring patent dominates a later expiring patent” and “a narrow species can
be non-obvious and patent eligible despite a patent on its genus.” Id.
However, “not every species of a patented genus is separately patentable,” as
they may be anticipated or obvious over the prior art. Id. For example, as is
well established in the law of obviousness, where “prior art references
‘provide[d] ample motivation to narrow the [a previously patented] genus
. . . to a few [species]’ . . . [the Federal Circuit] concluded that the species at
issue . . . was unpatentable.” Id. (first and second alteration in original)
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(quoting and citing Pfizer, Inc. v. Apotex, Inc., 480 F.3d 1348, 1366, 1372
(Fed. Cir. 2007)).
Also well established in the law of obviousness is that “[a] species
contained in a previously patented genus may be patentable if the species
manifests unexpected properties or produces unexpected results.” Id. at
1380. However, even though “[e]vidence of unexpected results [must] be
[considered] . . . even if that evidence was obtained after the patent’s filing
or issue date,” Bristol-Myers Squibb Co. v. Teva Pharma. USA, Inc., 769
F.3d 1339, 1342 (Fed. Cir. 2014) (third alteration in original) (denying reh’g
en banc) (quoting Genetics Inst., LLC v. Novartis Vaccines Diagnostics,
Inc., 655 F.3d 1291, 1307 (Fed. Cir. 2011)), “[m]ere recognition of latent
properties in the prior art does not render nonobvious an otherwise known
invention,” In re Baxter Travenol Labs., 952 F.2d 388, 392 (Fed. Cir. 1991).
“[A]dditional unexpected properties, however, d[o] not upset an already
established motivation to modify a prior art compound [or method to make
the compound] based on the expected properties of the resulting compound.”
Bristol-Myers Squibb Co. v. Teva Pharma. USA, Inc., 752 F.3d 967, 976
(Fed. Cir. 2014) (citing In re Dillon, 919 F.2d 688, 693 (Fed. Cir. 1990)),
reh’g en banc denied, 769 F.3d 1339.
The Rejection Over Salfeld 813
The Examiner determined that it was obvious to produce an antibody
as claimed in Salfeld 813 in CHO cells, and, thus, the antibody of appealed
claim 20, based on the disclosure of Ramage. Ans. 5; see also FF1, FF7–
FF12. The Examiner also determined that Ramage disclosed, and so,
rendered obvious, an antibody-based aqueous (liquid) pharmaceutical
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composition (suitable for subcutaneous injection), such as recited by
appealed claim 20. FF8–FF11. Beyond Ramage’s teaching and suggestion
to use CHO host cells to produce antibodies for human therapy, the
Examiner identified other motivation to do so, stating, after citing Goochee
and Trill:
One of ordinary skill in the art would be motivated to make
this modification in order to achieve efficient synthesis of the
antibody, and because of the expected convenience expected
from using CHO cells, namely the cells are readily transfectable,
are able to grow in suspension and serum-free medium, are
capable of growth at high densities, have a well-established track
record for expressing heterologous gene products, have proven
successful in the in the past, offer the use of co-amplification
with a number of different selectable genes, offer more human-
like glycosylation pattern and offer high level expression.
Recombinant expression in CHO cells would provide a source of
antibody.
Ans. 6; see also FF13–FF19.
We find the Examiner has established that the appealed claim is
obvious over the claims of Salfeld 813, and Ramage, Goochee, and Trill.
Appellants have submitted arguments and associated evidence in the form of
literature and declarations under 37 C.F.R. § 1.132.16 Having carefully
considered this with the Examiner’s evidence, we find Appellants have not
produced evidence showing, or persuasively argued, that the Examiner’s
determinations on obviousness-type double patenting are incorrect. Only

16 Mezes Decl.; Declaration Under 37 C.F.R. § 1.132 of Christopher
Chumsae, dated Jan. 10, 2014 (“Chumsae Decl.”); and Declaration Under
37 C.F.R. § 1.132 of Dr. Jochen Salfeld, dated Jan. 10, 2014 (“Salfeld
Decl.”).
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those arguments made by Appellants in the Briefs have been considered in
this Decision. Arguments not presented in the Briefs are waived. See 37
C.F.R. § 41.37(c)(1)(iv) (2015). We address Appellants’ arguments below.
1. Appellants’ First Argument: no motivation to use CHO cells
Appellants argue that the Salfeld 813 claims do not cover antibodies
“produced by CHO cells,” and in 1996 there would be no motivation or
expectation of success in selecting CHO cells (particularly over mouse
myeloma cells) for such a purpose. App. Br. 15–16. Appellants contend
that the skilled artisan would have had a “wide variety of available cellular
systems” for producing antibodies, with CHO cells being just one type,
without special motivation to select it from among the group and, as support,
Appellants cite, inter alia, Jenkins,17 Pietersz,18 Gramer,19 Logan,20 Poul,21

17 Nigel Jenkins et al., Getting the Glycosylation right: Implications for the
Biotechnology Industry, 14 NATURE BIOTECH. 975–81 (1996) (“Jenkins”).
18 Geoffrey A. Pietersz et al., In vitro and in vivo Antitumour Activity of a
Chimeric Anti-CD19 Antibody, 41 CANCER IMMUNOL. IMMUNOTHER 53–60
(1995) (“Pietersz”).
19 Michael J. Gramer & Charles F. Goochee, Glycosidase Activities of the
293 and NS0 Cell Lines, and of an Antibody-Producing Hybridoma Cell
Line, 43 BIOTECH. & BIOENGINEERING 423–28 (1994) (“Gramer”).
20 John S. Logan, Transgeniuc Animals: Beyond ‘Funny Milk,’ 4 CURRENT
OP. IN BIOTECH. 591–95 (1993) (“Logan”).
21 Marie-Alix Poul et al., Design of Cassette Baculovirus Vectors for the
Production of Therapeutic Antibodies in Insect Cells, 1 IMMNOTECHNOLOGY
189–96 (1995) (“Poul”).
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Potter,22 Hiatt 1989,23 Hiatt 1993,24 Shaw,25 Batra,26 Schläpfer,27 Slavin,28
Barnes,29 Page,30 and Ghaderi.31 App. Br. 16–19. Appellants also contend

22 Kathleen N. Potter et al., Antibody Production in the Baculovirus
Expression System, 10 INTERN. REV. IMMUNOL. 103–12 (1993) (“Potter”).
23 Andrew Hiatt et al., Production of Antibodies in Transgenic Plants, 342
NATURE 76–78 (1989) (“Hiatt 1989”).
24 Andrew Hiatt & Julian K-C Ma, Characterization and Application of
Antibodies Produced in Plants, 10 INTERN. REV. IMMUNOL. 139–52 (1993)
(“Hiatt 1993”).
25 Denise R. Shaw et al., Characterization of a Mouse/Human Chimeric
Monoclonal Antibody (17-La) to a Colon Cancer Tumor-Associated
Antigen, 138 J. IMMUNOLOGY 4534–38 (1987) (“Shaw”).
26 Surinder K. Batra et al., Mouse/Human Chimeric Mel-14 Antibody:
Genornic Cloning of the Variable Region Genes, Linkage to Human
Constant Region Genes, Expression, and Characterization, 13 HYBRIDOMA
87–97 (1994) (“Batra”).
27 Beatrice S. Schläpfer et al., Development of Optimized Transfectoma Cell
lines for Production of Chimeric Antibodies in Hollow Fiber Cell Culture
Systems, 45 BIOTECH AND BIOENGINEERING 310–19 (1995) (“Schläpfer”).
28 Dale C. Slavin-Chiarini et al., Biological Properties of Chimeric Domain-
deleted Anticarcinoma Immunoglobulins, 55 CANCER RES. 5957–67 (1995)
(“Slavin”).
29 Louse M. Barnes et al., Advances in Animal Cell Recombinant Protein
Production: GS-NSO Expression System, 32 CYTOTECHNOLOLGY 109–23
(2000) (“Barnes”). While not within the prior art timeframe and, therefore,
not particularly relevant and not relied upon in reaching our decision, we
note Barnes discloses the extensive use of CHO cells (with some
disadvantages), as competition with mouse myeloma cells, as host cells.
30 U.S. Patent No. 5,545,403 (issued Aug. 13, 1996) (“Page”).
31 Darius Ghaderi et al., Implication of the Presence of N-
glycollylneuraminic acid in Recombinant Therapeutic Glycoproteins, 28
NATURE BIOTECH. 863–67 (2010) (“Ghaderi”). While not within the prior
art timeframe and, therefore, not particularly relevant and not relied upon in
our decision, we note Ghaderi does identify an FDA-approved, fully human
antibody produced in CHO cells, i.e., Vectibix (panitumumab).
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(citing the Mezes Declaration) that, in 1996, CHO cells would not be the
choice of host cells “in an industrial setting for use in a liquid
pharmaceutical composition.” App. Br. 17; see also id. at 18 (indicating that
FDA approval would be a concern in selecting host cells). Appellants also
criticize the Examiner’s reliance on Goochee as teaching CHO cells were
widely used and appropriate for producing glycoproteins because they are
not “the claimed antibody.” App. Br. 21–22.
Having considered Appellants’ arguments and evidence, we are not
persuaded. Per our claim interpretation, supra, the appealed claim does not
require commercialization and/or industrial-scale production and/or FDA-
approvability and the skilled artisan’s concerns over such are not relevant or
determinative in analyzing obviousness; what is required by the claim is a
liquid pharmaceutical composition, i.e., a liquid medicinal drug, that
contains the recited antibody produced by CHO cells, with a
pharmaceutically acceptable carrier, suitable for subcutaneous injection in a
human subject. See claim 20 and claim interpretation discussion, supra.
Also, because the opinions set forth in the Mezes Declaration are premised
on the skilled artisan having such non-relevant concerns, we do not find this
evidence persuasive. See, e.g., Mezes Decl. ¶¶ 12 (“leading to commercial
scale manufacturing”), 14 (“in an industrial setting”), 16 (“approved by the
FDA”), 17 (“commercial manufacturing . . . capable of high yield, which is
essential for production of a therapeutic antibody in an industrial setting”),
18 (“production costs” and “commercial purposes”), 22 (“decreasing levels
. . . over time”), 24 (“in an industrial setting”), and 25 (“SUMMARY: . . . in
an industrial setting”).
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Salfeld 813 claims the same antibody as appealed claim 20, as a
pharmaceutical with a pharmaceutically acceptable carrier (FF1, FF7), but
not that it was produced with CHO cells, is specifically in liquid form, or is
suitable for subcutaneous injection in a human. Ramage teaches and
suggests producing such antibodies using CHO cells, and providing the
antibodies-so-produced in a liquid pharmaceutical suitable for subcutaneous
injection. FF8–FF12. Contrary to Appellants’ contentions, Goochee
bolsters the Examiner’s rationale for motivation to use CHO cells to produce
antibodies for human therapy, as it identifies that CHO cells do not produce
α(1,3)galactosyltransferase such that their (CHO) use would be expected to
result in producing proteins (glycoproteins) that do not include α-1,3-Gal,
like human cells, and that “[CHO] cells have emerged as the cell line of first
choice for the synthesis for recombinant human therapeutic glycoproteins.”
FF13–FF16. The Examiner identifies that human anti-TNFα antibodies fall
within the group of recombinant therapeutic glycoproteins. Ans. 8–9.
Further, the Examiner finds Trill identifies a variety of reasons there would
be motivation to use CHO cells as hosts for protein (e.g., mAbs) production.
FF17–FF19.
Regarding Appellants’ contention that CHO cells were merely one
non-obvious option from a variety of host cell types, we are not persuaded.
While the references cited by Appellants do identify a variety of host cell
types, none of the evidence persuades us that Ramage, Goochee, and Trill
would not motivate the skilled artisan to use CHO cells as hosts and,
moreover, several of Appellants’ cited references support the Examiner’s
position that CHO cells were suitable and/or preferred for the task. For
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example, Jenkins indicates that CHO cell lines were used for recombinant
protein synthesis (an antibody is a protein), that CHO cell lines can be
genetically modified to resemble the human glycan profile, and that CHO
cells may prove useful hosts. Jenkins 977. Also, Gramer indicates that
“Chinese hamster ovary (CHO) cells have been widely used to produce
recombinant glycoproteins.” Gramer 423 (right col.). And, Page discloses
that its invention relates to “a CHO cell-line capable of producing a human
antibody.” Page Abstract. In view of such disclosures, Appellants’
evidence is inconsistent, at best.
2. Appellants’ Second Argument: the art generally teaches away
Appellants argue that
“[a] key consideration of any cell line to be used for commercial
manufacture of a therapeutic human antibody would be stability,
e.g., stable expression of product over 40 or more rounds of cell
division. One of ordinary skill would have looked to a cell line
capable of high yield, which is essential for production of
therapeutic antibody in an industrial setting.”
App. Br. 22–23 (quoting Mezes Decl. ¶ 17). In view of this contended
consideration, Appellants cite Brown32 and Trill as indicating that CHO cells
were insufficient to satisfy the skilled artisan’s desire for high yield and
stability and as concluding mouse myeloma cells would be preferred over
CHO cells. App. Br. 23–24. Regarding this argument, Appellants also set
forth their proposed interpretation of the claim term “pharmaceutical” (or
“pharmaceutical composition”), addressed above. App. Br. 25–26.

32 M.E. Brown et al., Process Development for the Production of
Recombinant Antibodies using the Glutamine Synthetase (GS) System, 9
CYTOTECHNOLOGY 231–36 (1992) (“Brown”).
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We do not find Appellants’ arguments persuasive. As we discussed
above, we do not agree with Appellants’ proposed claim interpretation of
pharmaceutical (or pharmaceutical composition) — this term does not
invoke commercialization and/or industrial scale and/or FDA-approvability
concerns. Thus, for this reason alone, Appellants’ related arguments,
premised on such contention, that the prior art generally taught away from
the use of CHO cells as hosts are not persuasive. However, we also find that
neither Brown nor Trill teaches away from the invention or the use of CHO
cells as hosts for recombinant antibody production. For example, Brown
discloses the use of CHO cells was successful in producing antibodies in
significant quantities, in excess of 60 generations. See Brown 232–34
(Tables 1 and 2). This evidences success, even if not via an FDA-approved
industrial complex to achieve it. Also, Trill, rather than teaching away from
using CHO cells as host cells, identifies several advantages of doing so (as
the Examiner found). FF19.
3. Appellants’ Third Argument: teaching away from CHO cells
Appellants argue that a CHO cell line disclosed by Ramage for
producing the antibody Campath 1H, i.e., 3D11, was discussed in other
references as “produc[ing] decreasing levels of Campath over time,” which
would make CHO cells an unattractive choice as host cells. App. Br. 26–27
(citing Raper).33 Appellants argue the Mezes Declaration also cites Raper in

33 J. Raper et al., Long Term Stability of Expression of Humanized
Monoclonal Antibody Campath 1-H in Chinese Hamster Ovary Cells, 11
Animal Cell Tech.: Developments, Processes, and Products, Biotol Series,
European Society of Animal Cell Technology 51-53 (R. Spier, J.B. Griffiths,
C. MacDonald, Eds.) (1992) (“Raper”) (citation as provided by Appellants).
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concluding “one of ordinary skill in the art in February 1996 would have
been motivated to choose a cell line other than CHO for production of the
first fully human antibody for therapeutic use in an industrial setting in order
to achieve high production levels of HUMIRA®.” App. Br. 28 (emphasis
omitted) (quoting Mezes Decl. ¶ 24). Appellants also cite Lifely34 and
Isaacs35 as support for the contention that cells other than CHO cells would
be preferred to produce Campath 1H due, in part, to “uncertainty” regarding
the teachings of Ramage regarding CHO cell production of Campath. App.
Br. 29–30.
This argument is premised on Appellants’ incorrect claim
interpretation, which invokes commercial / industrial / regulatory
considerations. For this reason, without more, Appellants’ arguments are
not persuasive. Moreover, while Lifely may identify that Y0 cells are
preferred over CHO or NS0 cells under certain circumstances, i.e., when the
mechanism of lymphocyte depletion in vivo is ADCC rather than monocyte
killing activity (without extrapolating to other antibodies), it also identifies
that:
This antibody [CAMPATH-1H] has been expressed in several
mammalian cell lines, including Y0 rat myeloma, NS0 mouse
myeloma and Chinese hamster ovary (CHO), grown using
different culture conditions, and extensively tested in clinical
trials of lymphoproliferative disorders (Hale et al., 1988) and

34 M.Robert Lifely et al., Glycosylation and Biological Activity of
CAMPATH-1H Expressed in Different Cell Lines and Grown Under
Different Culture Conditions, 5 GLYCOBIOLOGY 813–22 (1995) (“Lifely”).
35 John D. Isaacs et al., Humanised Monoclonal Antibody Therapy for
Rheumatoid Arthritis, 340 LANCET 748–52 (1992) (“Isaacs”).
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rheumatoid arthritis (Isaacs et al., 1992), with some major
successes.
Lifely 813, 820. Thus, CHO cells would be reasonably expected to work.
And, Isaacs disclosed “[t]herapeutic-grade [CAMPATH-1H] antibody was
produced in Chinese hamster ovary cells grown in a hollow-fibre continuous
culture system.” Isaacs 748. Therefore, again, CHO cells would be
reasonably expected to work. For these reasons, also, we are not persuaded
by Appellants’ arguments.
Further, Appellants concede, “[w]hile Campath was eventually
produced commercially in CHO cells and approved by the FDA, at the time
of filing of the instant application there was uncertainty surrounding
production of this antibody in CHO cells.” App. Br. 30. “[C]ase law is clear
that obviousness cannot be avoided simply by a showing of some degree of
unpredictability in the art so long as there was a reasonable probability of
success.” Pfizer, 480 F.3d at 1364 (citing In re Corkill, 771 F.2d 1496, 1500
(Fed. Cir. 1985)). While we do not rely on Appellants’ concession or the
evidence upon which it is based in affirming the Examiner’s rejection, the
concession stands for the proposition that Appellants’ evidence does not
support the contention that the skilled artisan would be dissuaded from using
CHO cells to produce human antibodies for pharmaceuticals.
4. Appellants’ Third Argument: unexpected results
Appellants argue the invention of the appealed claim provides
unexpected results in producing a human antibody lacking α-1,3-galactose
glycan (α-1,3-Gal), thus avoiding potential “severe immune reactions in
certain patients.” App. Br. 13, 32; see also Salfeld Decl. ¶ 5. Appellants
contend that use of CHO cells to produce anti-TNFα antibodies results in “a
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relatively lower risk of causing certain immunogenicity problems in [human]
recipients” and “this benefit is unexpected inasmuch as it was not recognized
or appreciated in the area as of the priority date.” App. Br. 32. As support,
Appellants cite the declarations of Chumsae and Salfeld, and also Mezes,
which Appellants contend should have been convincing to the Examiner
“[i]f the Examiner had properly construed the claim.” App. Br. 32–34;
Reply Br. 18.
Appellants’ argument regarding unexpected results can be
summarized as follows: post-invention, it was discovered that adalimumab
(Humira®), produced in CHO cells, unexpectedly avoids potentially serious
immune reactions in patients because the antibodies do not include
potentially immunogenic α-1,3-Gal; and, despite the fact that it was known
in 199636 that CHO cells naturally do not express α-1,3-galactostransferase
and, so, the lack of α-1,3-Gal on polynucleotides produced by CHO cells
was expected, there would not have been motivation to use, or an
expectation of successfully using, CHO cells to produce therapeutic human
antibodies (“to avoid [such] potentially harmful immune responses in human

36 See Goochee (FF13–FF16); Smith (FF25), and Jenkins; see also App. Br.
22–24, 36 (“Appellants do not dispute that it was known in the prior art that
CHO cells did not express α-1,3-galactosyltransferase.”) and Reply Br. 15
(“The person of ordinary skill may have even been motivated to try CHO
cells given the fact that CHO cells lack α-1,3-galactosyltransferase.”), FF26.
Smith discloses that CHO cells only express α-1,3-galactosyltranderase
when artificially engineered to do so and, so, normally do not have the
capability to transfer Gal from UDP-Gal to the α-1,3-linkage (Smith 3225,
3232) and Jenkins discloses that CHO cell lines used for recombinant
protein synthesis have “fortuitously inactivated the gene for α-1,3-
galactosyltranferase (Jenkins 977).
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patients”) until it was eventually discovered that a potential immunogenic
problem existed because of α-1,3-Gal. See e.g., Reply Br. 14–15.
The “discovery that a claimed composition possesses a property not
disclosed for the prior art subject matter, does not by itself defeat a prima
facie case.” In re Dillon, 919 F.2d at 693. “In determining whether the
subject matter of a patent claim is obvious, neither the particular motivation
nor the avowed purpose of the patentee controls. What matters is the
objective reach of the claim. If the claim extends to what is obvious, it is
invalid under § 103.” KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 419
(2007).
Appellants’ position discounts or disregards the fact that other,
different, but sufficient motivation to produce Humira® (the antibody
constituting the active drug, in the way recited by the appealed claims, i.e.,
using CHO cells as hosts) did exist in the prior art. Appellants also base
their position on considerations for producing an FDA-approved
pharmaceutical, on an industrial scale, and for commercial purposes that are
not invoked based on the claimed invention. See discussion, supra.
“Mere recognition of latent properties in the prior art does not render
nonobvious an otherwise known invention.” In re Baxter, 952 F.2d at 392.
While evidence of unexpected results can include post-invention evidence, a
potential defect not discovered until after the invention date is not evidence
of what a skilled artisan would have expected as of the invention date. Here,
the evidence shows that the information the skilled artisan had in 1996
indicated that CHO host cells were a good choice for producing antibodies
for human therapy. FF12–FF19, FF22, FF25, FF26, FF28. The fact that,
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later, we understand an additional reason why Humira® might be
particularly effective is not the type of unexpected result (as much as it is an
uncovered latent property) than can overcome a strong case for obviousness
as of the invention date, which we have here. See Bristol-Myers, 769 F.3d
1339 (finding later discovered properties of a compound cannot influence
prior-existing motivations to use it); see also Bristol-Myers, 752 F.3d at 976
(“additional unexpected properties, however, [do] not upset an already
established motivation to modify a prior art compound [or method] based on
the expected properties of the resulting compound”).
The facts identified in the initial Federal Circuit panel’s decision in
Bristol-Myers, 752 F.3d 967, nearly parallel those here. As here, in Bristol-
Myers, the claimed invention was found to be obvious. The Bristol-Myers
invention was a pharmaceutical compound called “entecavir,” which was a
slightly-altered version of a prior art pharmaceutical compound called
“2#-CDG,” on which there was evidence, as of the invention date, of praise
for its pharmaceutical activity and the promise of therapeutic uses, as well as
evidence of the compound’s actual use in research, which showed enough
success to warrant the aforementioned praise and related high expectations.
Id. at 971–72. Based on this evidence, the Federal Circuit affirmed the
district court’s holding that the skilled artisan would have been motivated to
modify the prior art compound to form the invention compound and would
have had a reasonable expectation of success in so doing. Id. at 972.
Evidence showed, however, that years later it was discovered that this prior
art compound (2#-CDG) was actually toxic (while, presumably, the
invention compound was sufficiently not), which the patentee asserted
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would defeat any motivation to use this compound as a starting point. Id. at
974. Further, the patentee asserted that the claimed compound was
unexpectedly effective to treat hepatitis B (as well as having a high
resistance barrier and a large therapeutic window), without the toxicity
issues of the prior art compound. Id. at 977–78.
In Bristol-Myers, the Federal Circuit held that the late-discovered
unexpected results, while advantageous, did not outweigh the prior-existing
motivation to make the invention or the prior-existing reasonable
expectation the skilled artisan would have had for successfully so doing.
This is the scenario the facts present here, with the exception that, unlike the
starting prior art compound eventually found to be toxic and unusable in
Bristol-Myers, here the CHO cells, identified as useful and preferred hosts in
the prior art, have established themselves as such in the industry. Thus, we
find the Examiner presents a strong case for obviousness that is not upset by
the late-found, potentially unexpected results. We find this, without more is
sufficient to affirm the rejection.
However, we also find the declaration evidence relied upon by
Appellants unconvincing. As already discussed, above, the Mezes
Declaration is premised on an incorrect claim interpretation and, so, is not
persuasive. We note the Chumsae Declaration is largely speculative,
indicating that “galactose-α-1,3-galactose . . . can increase the
immunogenicity of the therapeutic antibodies when administered to human
subjects,” that having α-1,3-Gal on an antibody “could lead to dangerous”
conditions and it is “highly likely” (or just “likely”) that, were the claimed
antibodies produced in a mouse myeloma cell, they would have α-1,3-Gal.
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Chumsae Decl. ¶¶ 4, 6, 9, 10 (emphasis added). Chumsae identifies no
testing data to confirm this speculation and never states that producing
antibodies with CHO cells provides unexpected results. Nor does Chumsae
identify prior art evidence that undermines the teachings, discussed above,
as to the desirability of using CHO cells to express recombinant antibodies.
The Salfeld Declaration does state that “[i]n my opinion, production of
human anti-TNFα antibodies using CHO cells, as set forth in the pending
claims, results in anti-TNFα antibodies that have unexpected beneficial
properties when administered to a human subject, as compared to antibodies
produced in other host cell lines, such as mouse myeloma cell line” due to
the CHO cells-produced antibodies not “contain[ing] the galactose-α-
1,3,galactose glycan.” Salfeld Decl. ¶ 5. But, like Chumsae, Salfeld’s
statements are speculative. Salfeld indicates “[g]lycosylation of thereapeutic
antibodies can have a critical effect on immunogencity when administered
in humans,” that “production in certain mammalian expression systems can
increase the immunogenicity of therapeutic antibodies,” that “humans may
produce antibodies against this glycan epitope,” and that all these potential
effects present an “increased risk of immunogenicity when administered to
humans.” Salfeld Decl. ¶ 6 (emphasis added).
Also, the declarants’ use of hedging language to support their
opinions underscores the speculative and non-conclusive determinations of
the evidence they cite (i.e., Chung, Valliere, Raju, and Ghaderi).37 Chung

37 Christine H. Chung, M.D. et al., Cetuximab-Induced Anaphylaxis and IgE
Specific for Galactose-α-1,3-Galactose, 358 N. ENGL. J. MED. 1109–17
(2008) (“Chung”); John F. Valliere-Douglass et al., Glutamine-linked and
Non-consensus Asparagine-linked Oligosaccharides Present in Human
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identifies potential hypersensitivity to the drug cetuximab due to antibodies
for galactose-α-1,3-galactose, but indicated that the immunogenic reaction to
galactose-α-1,3-galactose is natural in only some people and is also
regionally prevalent, suggesting unknown environmental causation. Chung
1115–16. The Examiner also identifies that Chung’s disclosure of
glycosylation sites may not support Appellants’ contentions. Ans. 23.
Valliere discusses why (or why not) glycosylation resulting in incorporation
of galactose-α-1,3-galactose may occur, but does not conclude that inclusion
of α-1,3-Gal will lead to dangerous IgE-mediated anaphylaxis in patients.
See Valliere, generally. As noted above, it was previously understood that
CHO cells do not express α-1,3-galactosyltransferase and that α-1,3-Gal was
not detected in CHO cell expression systems. See Smith (FF25) and
Jenkins. Raju states, “no evidence in the literature suggests that the presence
of α-Gal epitopes on rIgG is immunogenic to humans.” Raju 44. Ghaderi
indicates “it is likely that most recombinant therapeutic glycoproteins carry
some Neu5Gc” and identifies “the presence of small amounts of Neu5Gc in
recombinant glycoproteins produced in CHO cells,” and concludes,
“findings suggest that the potential significance of the presence of Neu5Gc
on glycoprotein biotherapeutics should be revisited.” Ghaderi 863, 865–66.
Thus, none of these references definitively supports Appellants’ contentions,
even if they may inferentially do so.

Recombinant Antibodies Define Novel Protein Glycosylation Motifs, 285 J.
BIO. CHEM. 16012–22 (2010) (“Valliere”); T. Shantha Raju, Glycosylation
Variations with Expression Systems and Their Impact on Biological Activity
of Therapeutic Immunoglobulins, BIOPROCESS INT’L 44–53 (April 2003)
(“Raju”).
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Thus, for the reasons above, we are not persuaded by Appellants’
arguments on unexpected results.
5. Appellants’ Fifth Argument: improper reliance on the Salfeld
813 specification
Appellants argue that the Examiner improperly relied on the
Salfeld 813 specification in “asserting that CHO cells are a preferred system
for expressing the recombinant antibodies of the invention.” App. Br. 41
(internal quotation mark omitted). Appellants contend the Examiner used
the Salfeld 813 specification as prior art in rejecting appealed claim 20. Id.
at 42.
We are not persuaded by Appellants’ argument. The Examiner’s
mere identification of the stated preference for CHO host cells in the
Salfeld 813 specification does not mean the Examiner relied on the same as
prior art and it is clear that the Examine did not do so. The Examiner made
clear that the specification was reviewed to determine the “coverage” (in the
Examiner’s verbiage) of claim 20, which is permissible. See In re Vogel,
422 F.2d 438, 441–42 (CCPA 1970); see also, AbbVie, 764 F.3d at 1380–81
(we may look to an obviousness-type double patenting reference’s disclosure
to determine obviousness, to answer whether the claims merely define an
obvious variant, and regarding questions of utility). Whether it was
necessary to consult the specification of Salfeld 813 to clarify the meaning
of any of its claim language or to ascertain the scope of its claims or their
relevant utility is, ultimately, irrelevant. The Examiner need not have and
did not rely on the Salfeld 813 specification as prior art in rejecting the
claims and cited ample other prior art disclosures for this purpose.
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For the reasons discussed above, we find the balance of evidence
supports the Examiner’s position and affirm the rejection of claim 20 over
Salfeld 813.
The Rejection Over Salfeld 894
The Salfeld 894 claims, e.g., claim 55 (FF2), are directed to the
human antibody of appealed claim 20 and, also, to a pharmaceutical
composition including the antibody, suitable for subcutaneous injection.
Lacking from the Salfeld 894 claims is an indication that the pharmaceutical
was specifically liquid, that the antibody was paired with a pharmaceutically
acceptable carrier, suitability for subcutaneous injection, and that the
antibody was produced using CHO cells, which are limitations of appealed
claim 20. The “liquid,” “carrier,” and “subcutaneous injection” elements are
common, but are specifically disclosed by Ramage (FF11) and Le (FF23).
The Examiner determined, as set forth above, that Ramage, Goochee, and
Trill make the use of CHO cells to produce the antibody obvious. Ans. 54–
58.
We find the Examiner has established that the appealed claims would
be obvious over the claims of Salfeld 894, and Ramage, Goochee, Trill, and
Le. Having carefully considered Appellants’ arguments and evidence, we
find Appellants have not produced evidence showing, or persuasively
argued, that the Examiner’s determinations on obviousness-type double
patenting are incorrect. Only those arguments made by Appellants in the
Briefs have been considered in this Decision. Arguments not presented in
the Briefs are waived. See 37 C.F.R. § 41.37(c)(1)(iv) (2015). We address
Appellants’ arguments below.
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Appellants argue claim 20 is not obvious over the claims of
Salfeld 894 for the same reasons set forth regarding the claims of
Salfeld 813. App. Br. 48–49. Appellants also argue that appealed claim 20
does not recite detectably labeling and conjugating therapeutic moieties to
antibodies. Id. at 49.
To the extent Appellants’ arguments are duplicative of those made
regarding the rejection over the claims of Salfeld 813, we are not persuaded
for the reasons set forth above. We agree that appealed claim 20 does not
recite labeling, however, it does define the same antibody recited by the
claims of Salfeld 894, and producing such antibodies using CHO host cells
would be obvious, as discussed above.
For the reasons discussed above, we find the balance of evidence
supports the Examiner’s position and affirm the rejection of claim 20 over
the Salfeld 894 claims.
The Rejection Over Salfeld 401
The Salfeld 401 claims, e.g., claim 5 (FF3), are directed to the human
antibody of appealed claim 20 and, also, to a pharmaceutical composition
including the antibody, and a pharmaceutically acceptable carrier. Lacking
from the Salfeld 401 claims is an indication that the pharmaceutical is
specifically liquid, that it is suitable for subcutaneous injection, and that the
antibody was produced using CHO cells, which are each a limitation of
appealed claim 20. The “liquid” and “subcutaneous injection” elements are
common, but are specifically disclosed by Ramage (FF11). The Examiner
determined, as set forth above, that Ramage, Goochee, and Trill make the
use of CHO cells to produce the antibody obvious. Ans. 60–63.
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We find the Examiner has established that the appealed claims would
be obvious over the claims of Salfeld 401, and Ramage, Goochee, and Trill.
Having carefully considered Appellants’ arguments and evidence, we find
Appellants have not produced evidence showing, or persuasively argued,
that the Examiner’s determinations on obviousness-type double patenting
are incorrect. Only those arguments made by Appellants in the Briefs have
been considered in this Decision. Arguments not presented in the Briefs are
waived. See 37 C.F.R. § 41.37(c)(1)(iv) (2015). We address Appellants’
arguments below.
Appellants argue claim 20 is not obvious over the claims of
Salfeld 401 for the same reasons set forth regarding the claims of
Salfeld 813. App. Br. 51. To the extent Appellants’ arguments are
duplicative of those made regarding the rejection over the Salfeld 813
claims, we are not persuaded for the reasons set forth above. For the reasons
discussed above, we find the balance of evidence supports the Examiner’s
position and affirm the rejection of claim 20 over the Salfeld 401 claims.
The Rejection Over Salfeld 761
The Salfeld 761 claims, e.g., claim 79 (FF4), are directed to the
human antibody of appealed claim 20 and, also, to a pharmaceutical
composition including the antibody, and pharmaceutically acceptable carrier.
Lacking from the Salfeld 761 claims is an indication that the pharmaceutical
is specifically liquid, that it is suitable for subcutaneous injection, and that
the antibody was produced using CHO cells, which are each a limitation of
appealed claim 20. The “liquid” and “subcutaneous injection” elements are
common, but are specifically disclosed by Ramage (FF11). The Examiner
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determined, as set forth above, that Ramage, Goochee, and Trill make the
use of CHO cells to produce the antibody obvious. Ans. 65–68.
We find the Examiner has established that the appealed claims would
be obvious over the claims of Salfeld 761, Ramage, Goochee, Trill, and
Gombotz. Having carefully considered Appellants’ arguments and
evidence, we find Appellants have not produced evidence showing, or
persuasively argued, that the Examiner’s determinations on obviousness-
type double patenting are incorrect. Only those arguments made by
Appellants in the Briefs have been considered in this Decision. Arguments
not presented in the Briefs are waived. See 37 C.F.R. § 41.37(c)(1)(iv)
(2015). We address Appellants’ arguments below.
Appellants argue claim 20 is not obvious over the claims of
Salfeld 761 for the same reasons set forth regarding the claims of
Salfeld 813. App. Br. 52. Appellants also argue the ’978 patent (we
understand Appellants intended to reference Salfeld 761) claims include a
“controlled release” element that its specification does not equate to liquid
pharmaceutical compositions of any kind. Id. at 53.
To the extent Appellants’ arguments are duplicative of those made
regarding the rejection over the Salfeld 813 claims, we are not persuaded for
the reasons set forth above. Regarding the issue regarding “controlled
release,” we do not find this difference between appealed claim 20 and the
Salfeld 761 claims determinative on obviousness.
For the reasons discussed above, we find the balance of evidence
supports the Examiner’s position and affirm the rejection of claim 20 over
the Salfeld 761 claims.
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The Rejection Over Salfeld 382
The Salfeld 382 claims, e.g., claim 15 (FF6), are directed to the
human antibody of appealed claim 20 and, also, to a pharmaceutical
composition including the antibody, and pharmaceutically acceptable carrier.
Lacking from the Salfeld 382 claims is an indication that the pharmaceutical
is specifically liquid, that it is suitable for subcutaneous injection, and that
the antibody was produced using CHO cells, which are each a limitation of
appealed claim 20. The “liquid” and “subcutaneous injection” elements are
common, but are specifically disclosed by Ramage (FF11). The Examiner
determined, as set forth above, that Ramage, Goochee, and Trill make the
use of CHO cells to produce the antibody obvious. Ans. 70–73.
We find the Examiner has established that the appealed claims would
be obvious over the claims of Salfeld 382, and Ramage, Goochee, and Trill.
Having carefully considered Appellants’ arguments and evidence, we find
Appellants have not produced evidence showing, or persuasively argued,
that the Examiner’s determinations on obviousness-type double patenting
are incorrect. Only those arguments made by Appellants in the Briefs have
been considered in this Decision. Arguments not presented in the Briefs are
waived. See 37 C.F.R. § 41.37(c)(1)(iv) (2015). We address Appellants’
arguments below.
Appellants argue claim 20 is not obvious over the claims of
Salfeld 382 for the same reasons set forth regarding the Salfeld 813 claims.
App. Br. 51. To the extent Appellants’ arguments are duplicative of those
made regarding the rejection over the claims of Salfeld 813, we are not
persuaded for the reasons set forth above. For the reasons discussed above,
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we find the balance of evidence supports the Examiner’s position and affirm
the rejection of claim 20 over the claims of Salfeld 382.

SUMMARY
The obviousness-type double patenting rejection over the claims of
Salfeld 813, and Ramage, Goochee, and Trill is affirmed.
The obviousness-type double patenting rejection over the claims of
Salfeld 894, and Le, Ramage, Goochee, and Trill is affirmed.
The obviousness-type double patenting rejection over the claims of
Salfeld 401, and Ramage, Goochee, and Trill is affirmed.
The obviousness-type double patenting rejection over the claims of
Salfeld 761, and Gombotz, Ramage, Goochee, and Trill is affirmed.
The obviousness-type double patenting rejection over the claims of
Salfeld 382, and Ramage, Goochee, and Trill is affirmed.

TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).

AFFIRMED