Ex Parte 7381804 et al

Patent Trial and Appeal Board

Jun 25, 2013

95000440 (P.T.A.B. Jun. 25, 2013)

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.
95/000,440 03/18/2009 7381804 03369/7001505-000 2649
22852 7590 06/25/2013
FINNEGAN, HENDERSON, FARABOW, GARRETT & DUNNER
LLP
901 NEW YORK AVENUE, NW
WASHINGTON, DC 20001-4413
EXAMINER
TURNER, SHARON L
ART UNIT PAPER NUMBER
3991
MAIL DATE DELIVERY MODE
06/25/2013 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)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE PATENT TRIAL AND APPEAL BOARD
____________

Maxygen, Inc.
Requester

v.

Amgen, Inc.
Patent Owner and Appellant
____________

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Technology Center 3900
____________

Before LORA M. GREEN, RICHARD M. LEBOVITZ, and
RAE LYNN P. GUEST, Administrative Patent Judges.

GUEST, Administrative Patent Judge.

DECISION ON APPEAL
This is a decision on appeal by the Patent Owner from the Patent
Examiner‟s decision to reject pending claims in an inter partes
reexamination of U.S. Patent 7,381,804 B2.
1
The Board‟s jurisdiction for
this appeal is under 35 U.S.C. §§ 6(b), 134, and 315. We AFFIRM.

1
US 7,381,804 B2, issued June 3, 2008, to Timothy D. Osslund (hereinafter
“the ‟804 Patent).
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I. BACKGROUND
The claims of the ‟804 Patent are drawn to a group of analogs of
granulocyte colony-stimulating factor (“G-CSF”), which have various
modified amino acid residues from the G-CSF amino acid sequence. The
analogs may have the same G-CSF function, in the same or to a varying
degree, or certain functions may be improved or lessened, such as a
biological activity (including hematopoietic activity), shelf-life, stability,
and ease of formulation, as desired. See ‟804 Patent, col. 4, ll. 31-59.
A request for inter partes reexamination under 35 U.S.C. §§ 311-318
and 37 C.F.R. §§ 1.902-1.997 for the ‟804 Patent was filed February 6, 2009
by Maxygen, Inc. (hereinafter “Requester”). See Request for Inter Partes
Reexamination; Requester Responsive Brief (hereinafter “Req. Res.
Br.”), dated February 6, 2012, at 1. The Patent Owner is Amgen, Inc.
(hereinafter “Patent Owner”). Patent Owner Appeal Brief (hereinafter “PO
App. Br.”), dated January 4, 2012, at 4. Claims 1-8 are pending and stand
rejected. An oral hearing was held May 22, 2013. A transcript of the
hearing will be entered into the record in due course.
Patent Owner appeals the Examiner‟s decision to reject the claims
under 35 U.S.C. § 103. For each rejection, Patent Owner argues claims 1-4
and 6-8 as a group and separately argues the patentability of claim 5.
Claim 1 is representative of claims 1-4 and 6-8 and reads as follows:
1. A G-CSF analog having hematopoietic activity
comprising an internal core of helices A, B, C and D and
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external loops as set forth in FIG. 3
2
and an amino acid
sequence, wherein the amino acid sequence differs from that of
SEQ ID NO:2
3
in that
a) lysine residues at positions 17 and 41 are substituted;
and
b) at least one amino acid sequence in an external loop is
altered to include one or more lysine amino acid residues,
wherein one or more of said lysine amino acid residues is
covalently modified with polyethylene glycol (PEG),
wherein an N-terminal methionine as set forth in SEQ ID
NO.2 is optional.
PO App. Br., Claim App‟x at A-1. Claim 5, argued separately, reads as
follows:
5. A G-CSF analog having hematopoietic activity
comprising and internal core of helices A, B, C and D and
external loops as set forth in FIG. 3 and an amino acid
sequence, wherein the amino acid sequence differs from that of
SEQ ID NO:2 in that
a) lysine residues at positions 17 and 41 are substituted;
b) at least three amino acid residues, other than said
lysine residue at position 17 of helix A, which are not essential
for structural integrity, are substituted, wherein the three
substituted amino acid residues are located in different helices,

2
FIG. 3 of the ‟804 Patent is a “ribbon diagram” illustrating the 4-hecial
structure of G-CSF, with the helices label A, B, C, and D. The description
of Figure 3 of the ‟804 Patent identifies the amino acid residue numbers
associated with each of helices A-D. See ‟804 Patent, col. 11, l. 62 to col.
12, l. 2.

3
SEQ. ID NO:2 is the unaltered amino acid sequence for human G-CSF.
See ‟804 Patent, col. 11, ll. 51-53.
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said helices selected from the group consisting of helix A, helix
C and helix D; and
c) at least one lysine amino acid residue is covalently
modified with polyethylene glycol (PEG),
wherein an N-terminal methionine as set forth in SEQ ID
NO:2 is optional.
PO App. Br., Claim App‟x. at A-2 to A-3.
The claims are all drawn to analogs of G-CSF having hematopoietic
activity having a 4-helical structure wherein the analog differs from
unaltered G-CSF in particular ways. The independent claims require the
following alterations to G-CSF:
i. the lysine residues at positions4 17 and 41 are substituted (claim 1-
5);
ii. any amino acid residue on “an external loop” altered to a lysine
which is then covalently modified with polyethylene glycol (PEG)
(claims 1 and 2);
iii. any lysine covalently modified with PEG (claims 3-5); and
iv. the substitution of any amino acid that is “not essential for
structural integrity” in at least one of helix A, C or D (claim 2), in

4
Each of the claims also recites that “an N-terminal methionine as set forth
in SEQ ID NO:2 is optional.” In other words, the position numbering of the
amino acid residues may differ by 1 in identical sequences which do not
include the N-terminal methionine as part of the amino acid sequence of G-
CSF. For example, the lysine at positions 17 and 41 in the claims would
appear as lysine at positions 16 and 40 in prior art references that do not
include the N-terminal methionine.

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helix C (claim 3), in both helices A and C (claim 4), and in each of
helices A, C and D (claim 5).
5

Claim 6 is directed to the analogs of claims 1-5, wherein there is reduced
hematopoietic activity compared to unaltered recombinant G-CSF. Claim 7
is directed to the analogs of claim 6 which also have improved serum half-
life compared to unaltered recombinant G-CSF. Claim 8 is directed to the
analog of claim 6, where the hematopoietic activity of the analog is
determined via a particular assay. See generally, PO App. Br., Claim App‟x.

II. REJECTIONS BASED ON A COMBINATION OF PRIOR
ART DESCRIBING ANALOGS OF G-CSF KNOWN IN THE ART
The Examiner maintains the rejection of claims 1-8 under 35 U.S.C.
§ 103 based on the following references either as stated or in view of
additional prior art (see Appendix D of PO App. Br.):
1. Camble ‟6306 and Shaw ‟5847 (Rejection 1; Rejections 2-4 cite
additional prior art);
2. Camble ‟630 and Shaw ‟8248 (Rejection 5);

5
The ‟804 Patent identifies that helix A includes amino acids at positions
11-39, helix B includes amino acids at positions 72-91, helix C includes
amino acids at positions 100-123, and helix D includes amino acids at
positions 143-173. ‟804 Patent, col. 11, ll. 62-67.

6
EP 0 459 630 A2, published April 12, 1991 and naming Roger Camble, et
al. as inventors (hereinafter “Camble ‟630”).

7
US 4,904,584, issued February 27, 1990 to Gray Shaw (hereinafter “Shaw
‟584”).

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3. Camble ‟2959 (Rejection 6; Rejections 7-10 cite additional prior
art);
4. Camble ‟295 and Shaw ‟584 (Rejection 11); and
5. Shaw ‟584 and Cunningham10 (Rejection 12; Rejections 13-14 cite
additional prior art).
Although each of the rejections was considered separately, the
rationale used by the Examiner and the Requester and the arguments
presented by the Patent Owner are substantially the same for each of the
rejections.
The Examiner finds that Camble ‟630 discloses G-CSF analogs
having mutations in helices A, C and/or D and mutations that include
external loop substitutions with lysine. RAN 4, 10 and 16. The Examiner
finds that Camble ‟630 discloses exemplary analogs that meet some of the
limitations of the claims, namely: a) a molecule that includes substitutions in
helices A and C and an external loop lysine substitution, b) a molecule that
includes helices A, C, and D substitutions and an external loop lysine
substitution, and c) a molecule having a helix A substitution, a substitution
of the lysine in the 41 position, and an external loop substitution. RAN 4.
Indeed, Camble ‟630 discloses various specific point mutations falling

8
WO 89/05824, published June 29, 1989 and naming Gray Shaw as the sole
inventor (hereinafter “Shaw ‟824”).

9
GB 2 246 295 A, published January 29, 1992 and naming Roger Camble et
al as inventors (hereinafter “Camble ‟295”).

10
WO 92/21029, published November 26, 1992 and naming Brian
Cunningham, et al. as inventors (hereinafter “Cunningham”).
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within helix A, the AB extended loop, helix C and helix D. See e.g., Camble
‟630, p. 2, l. 38-p. 3, l. 7. Further, Camble ‟630 states that these mutations
can be combined. Id. (stating that the derivatives have “at least one” of the
point mutations); see also p. 3, ll. 8-18 and the Examples (providing specific
analogs with more than one of the disclosed point mutation). The Examiner
also notes that “[o]ther Camble ‟630 molecules also apply to the claims.”
RAN 4. As pointed out by the Examiner, the examples of Camble ‟630 have
some degree of activity, even if very low, and solution solubility. RAN 4;
Camble ‟630, p. 3, ll. 34-36 and p. 27, l. 49- p. 29, l. 44.
The Examiner finds that Camble ‟630 and Camble ‟295 are
cumulative in their teaching. RAN 10.
The Examiner finds that that Cunningham describes G-CSF analogs
with “substitutions at site 1 and/or site 2 within helices A, C, D and an
external loop as well as Lys-PEG modifications.” RAN 16. Indeed,
Cunningham teaches
The helical domains of site 2 (helix A or C), preferably helix C,
are the preferred mutagenesis locations for site 2. The helical
domains of site 1 (helix A or D), preferably helix D, are the
preferred locations for variation in site 1. Typically, only 1
residue is varied for each site, although it is within the scope of
this invention to vary at least 1 residue in each domain of each
site (2 for site 2, 3 for site 1). In other embodiments, 2 or more
residues, usually up to about 5 residues, are varied at each
domain.
Cunningham, p. 11, ll. 11-17. The Examiner finds that the molecules of
Cunningham are shown to exhibit agonist or antagonist properties. RAN 16.
The Examiner finds that Shaw ‟584 discloses analogs of G-CSF
having “enhanced pharmacokinetic properties including reduced adverse
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immune response, increased solubility, desirable circulatory levels and
therapeutic efficacy.” RAN 4. The Examiner finds that Shaw ‟584
discloses customizing lysine insertions, deletions or Lys to Arg
11

substitutions and Arg to Lys substitutions. The purpose of the modifications
disclosed by Shaw ‟584 are “to provide for homogeneous preparations
whereby Lys residues that are inaccessible or are undesirable for hydrophilic
modification, for example which show reduced biological activity upon
modification, may be removed while hydrophilic moieties may be inserted
or substituted to mimic native structures or prolong serum half-life.” RAN
4-5. The Examiner finds that Shaw ‟584 includes specific Lys to Arg
substitutions at residues 17 and 41, as claimed, further Lys to
Arg substitutions at positions 24 and 35 (AB extended loop), and Arg to Lys
substitutions, namely at positions 23 (helix A) and positions 147, 148, 167
and 170 (all helix D), which are subsequently modified with PEG. RAN 5;
Shaw ‟584, col. 9, ll. 65 to col. 10, l. 8.
Shaw ‟824 is the international version of Shaw ‟584, and the
Examiner find that two references are cumulative. RAN 9.
Generally, the Examiner determined that it would have been obvious
to one of ordinary skill in the art to combine the modifications of the various
described analogs for the purposes taught by the prior art, namely because
the Camble references teach activity and solution stability, the Shaw
references teach reduced adverse immune response, increased solubility,
desirable circulatory levels and therapeutic efficacy, and Cunningham

11
“Lys” is a common three letter abbreviation for a lysine amino acid
residue. “Arg” is a common three letter abbreviation for an arginine amino
acid residue.
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teaches agonist and antagonist properties. RAN 5, 9-10, 15, 16-17. Based
on the success of Camble, Shaw, and cited prior art, the Examiner found that
such modified analogs would have been expected to retain hematopoietic
activity and structural integrity (id.)
Camble ‟295 expressly references that the analogs of Camble ‟295
(and Camble ‟630) may be further modified as disclosed by Shaw ‟584.
RAN 10; Camble ‟295, p. 11, full ¶ (“The proposed modifications . . . may
thus, for example be applied to either native G-CSF having Cys
17
of the
native sequence replaced by Ser
17
or to allelic variants and analogues thereof
known to possess at least one of the biological properties of naturally
occurring G-CSF such as those described in [among others] US Patent No.
4,904,584 [Shaw ‟584].”). All of the rejections that feature Camble ‟295
incorporate the teachings of Shaw ‟584 by reference. See e.g., RAN 10-11.
The remaining references
12
cited by the Examiner are generally relied
upon to provide further evidence that it was known in the art at the time of
the invention that substitutions at the locations identified in the Camble
references, the Shaw references and Cunningham would exhibit some degree
of activity and would not affect structural integrity.

12
The Examiner relies upon Gaertner, Statke-Ishikawa, Tanaka ‟91, Souza
‟643, and Kuga as evincing enhanced or retained biological activity. See
e.g., RAN 6 and 8. The Examiner relies upon Lau ‟90, Wells ‟90, Bowie
‟89, Bowie ‟90, O‟Shea, Tsuji, Souza ‟643, Kuga and Layton as evincing at
known mutations maintained structural stability of the molecule. See, id. at
7-8 and 8-9. Please reference the Request for Inter Partes Reexamination,
filed February 6, 2009 for the full citations for these references.
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Discussion
Patent Owner argues that the prior art discloses a very large number of
point mutations and no reasons to pick the particular point mutations recited
in the claims. PO App. Br. 11-13. Patent Owner contends that the
Examiner‟s rejections start with Example 28 of Camble ‟630, because it is
the only disclosed analog with substitutions in each of helices A, C, and D,
and Example 7 of Shaw, because it is a clear example where Lys was
substituted in positions 17 and 41, but the Examiner did not provide a reason
to have selected these analogs as desirable over all others disclosed for
further modification. Id. at 8 (citing Procter and Gamble Co. v. Teva Pharm.
USA, Inc., 566 F.3d 989, 994 (Fed. Cir. 2009); Takeda Chem. Indus. Ltd. v.
Alphapharm Pty. Ltd., 492 F.3d 1350, 1357 (Fed. Cir. 2007) as holding that
“For a new claimed compound, a prima facie case of obviousness requires a
reasoned identification of some motivation that would have led one skilled
in the art to 1) select a lead compound from the prior art, and 2) modify that
compound in a particular way to achieve the claimed invention.”).
We are not persuaded that the Examiner is picking and choosing
particular analogs from the prior art. Rather, the Examiner is correctly
considering what the teaching of the prior art as a whole would have meant
to a person of ordinary skill in the art. In re Etter, 756 F.2d 852, 859 (Fed.
Cir. 1985) (en banc) (“[T]he criterion being not whether the references could
be physically combined but whether the claimed inventions are rendered
obvious by the teachings of the prior art as a whole.”).
As a whole, the teachings of the Camble, Shaw and Cunningham
references describe reasons why known modifications to G-CSF would
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provide various types of known improvement over unaltered G-CSF. All
three references establish that one of ordinary skill in the art was familiar
with making mutations in G-CSF and determining which mutations had
advantageous properties. The Examiner provides examples of particular
analogs that have modifications in helices A, C, D and in an external loop,
but the Examiner further states that: “While [an exemplary particular]
modification is highlighted, it is not the only combination of preferred
molecules which applies to the ‟804 claims.” See RAN 5, 10-11, 15, 16-17.
Accordingly, we understand the Examiner taking the position that any of the
disclose analog mutations described in the art having a particular function,
whether that function be agonist properties, improved solution stability or
improved solubility, would have been a suitable substitution to the G-CSF
protein. Thus, the prior art provide sufficient reasons why the skilled
artisan would have made one or more of the known substitutions to the G-
CSF protein.
The combination of these various modifications appears to be no more
than the predictable use of known modifications to G-CSF according to the
known effects of that particular modification. KSR Int'l Co. v. Teleflex Inc.,
550 U.S. 398, 417 (2007) (The question to be asked is “whether the
improvement is more than the predictable use of prior art elements according
to their established functions.”). While it is apparent that certain exemplary
combinations would have fallen within the scope of the claims, the claims
are quite broad and many combinations of modifications disclosed in the art
would have met the claims‟ limitations.
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We are not concerned about the sheer number of analogs disclosed by
the proposed modifications of the prior art. The prior art appear to disclose a
finite number of point mutations and directs the skilled artisan to particular
exemplary analogs combining those point mutations to demonstrate
preferred properties. While the number of possible analogs disclosed by the
point mutations in the prior art is large, the list is not infinite as Patent
Owner suggests. Patent Owner has provided no persuasive evidence to
suggest that the preparation and testing of a large number of analogs having
the various mutations recited in the prior art would have been anything but
routine. KSR, 500 U.S. at 421 (“When there is a design need or market
pressure to solve a problem and there are a finite number of identified,
predictable solutions, a person of ordinary skill has good reason to pursue
the known options within his or her technical grasp. If this leads to the
anticipated success, it is likely the product not of innovation but of ordinary
skill and common sense.”). To the contrary, the success reported in the cited
prior art references, including Camble, Shaw, and Cunningham, provides
strong evidence that one of ordinary skill in the art routinely produced
modified G-CSF analogs and knew how to routinely determine their
activities. The prior art has shown that the problems of activity, solution
stability, solubility, etc. are all addressed by known mutations in the art. The
skilled artisan would have pursued any combination of these known options
to provide a particularly desired improvement over unaltered G-CSF.
Patent Owner further argues that Example 28 of Camble ‟630 and
other preferred analogs have particularly low activity, thus allegedly
teaching away from combination, and that analogs disclosed in Shaw are
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untested for biological activity and are thus merely prophetic in nature.
According to Patent Owner, the skilled artisan would not rely on these
analogs as desirable modifications. PO App. Br. 13 and 16-17, and 18-21.
We are not persuaded by this argument. Claims 1-5 recite that the
analog has “hematopoietic activity,” which is not defined in the claims or the
‟804 Patent to be of any particular amount of activity, and thus encompasses
analogs with even minimal activity. See also claim 6 (indicating that
analogs with a hematopoietic activity that is “lower than the hematopoictic
[sic] activity of unaltered recombinant human G-CSF in vitro” are
encompassed by the independent claims). As indicated by Patent Owner,
Camble „630 expressly discloses analogs with low specific activity (see
Camble „630, p. 28-29). A “known or obvious composition does not
become patentable simply because it has been described as somewhat
inferior to some other product for the same use.” In re Gurley, 27 F.3d
551, 553 (Fed. Cir. 1994). Moreover, Cunningham describes making
polypeptide antagonists that interfere with ligand binding (Cunningham, p.
3, ll. 17-18; p. 4, ll. 14-35; RAN 42). Thus, low activity may be just as
desirable of a property, perhaps such that the analog may be used as an
agonist or antagonist, as is high activity.
Further, as discussed above, we do not agree that the Examiner is
solely relying on Example 28 of Camble ‟630, but rather is relying on the
general teaching of Camble ‟630 that modifications in helix A, helix C, helix
D, or any combination thereof were known in the art as having at least
improved solution stability. Similarly, the Examiner is not relying on any
particular Example of Shaw ‟584, but rather the general teaching of Shaw
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that it was known in the art to modify the Lys and Arg residues in G-CSF,
including PEG binding of Lys residues, for various desired properties.
Patent Owner further argues that unpredictability in single and
combined point mutations in G-CSF creates no expectation of success
regarding structural integrity and desired activity. PO App. Br. 24-25. In
particular, Patent Owner indicates that the describe mutations amount to
little more than trial and error. PO App. Br. 24. Patent Owner argues that
without the particular understanding of the three-dimensional structure first
described in the present invention, combining the mutations recited in the
prior art amount to no more than “tinkering.” Id. at 1-4 and 25. Patent
Owner relies on the Levitt and Petsko Declarations to support of this
position. Id.
Dr. Levitt‟s research, while a Ph.D. candidate at the MRC Laboratory
of Molecular Biology at Cambridge University in the early 1970‟s and
subsequently, focused on conformational analysis of protein molecules,
including computer determination of protein secondary structure and basic
rules of protein architecture. See First Levitt Decl., ¶¶ 1-3.
13
We determine
that Dr. Levitt is qualified to testify as to the state of the art in protein
structure modeling and the technology available for doing so at the time of
the presently claimed invention.
Dr. Petsko testifies that his research focuses on using protein X-ray
crystallography, molecular dynamics, site-directed mutagenesis and yeast
genetics to study “the structural basis of biochemical properties” and

13
Declaration of Dr. Michael Levitt, dated July 9, 2009 (“First Levitt
Decl.”). Patent Owner also cites to a second Declaration of Dr. Michael
Levitt, dated December 20, 2010 (“Second Levitt Decl.”).
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“problems such as the structural origins of enzyme catalytic power and the
functional role of protein flexibility from a chemical and biophysical
perspective.” Petsko Decl. ¶ 4.
14
We determine that Dr. Petsko is qualified
to testify generally as to the ways in which changes to protein structure
affect chemical and biological properties.
In particular, Dr. Levitt testifies that at the time of the invention and
without a detailed 3D structure of a protein, “one had to exhaustively mutate
each position and measure whether activity had changed.” Second Levitt
Decl. ¶ 11. Dr. Petsko testifies that “[w]ithout the 3D structure, it is
impossible to draw any meaningful conclusions about the role of any
individual amino acid in G-CSF's structure or function and mutations in the
G-CSF protein would produce an unpredictable result.” Petsko Decl. ¶ 6.
Dr. Petsko also states that “reciprocal variability [i.e., the interaction of two
residues] is a common feature of protein evolution, and requires 3D
structural information to ascertain.” Petsko Decl. ¶ 8.
While we credit the testimony of Drs. Levitt and Petsko, we do not
find that this evidence addresses the Examiner‟s reasoning for combining the
references. The testimony does not address the known analogs in the art or
the properties they are known to provide. Rather, the testimony of Dr. Levitt
confirms that making analogs having the known mutations in the art and
testing for their properties was known and routine in the art. The skilled
artisan having evidence, from the Shaw, Camble and Cunningham
references, of known analogs which are known to have certain properties,

14
Declaration of Dr. Gregory A. Petsko, dated July 10, 2009 (“Petsko
Decl.”).

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would have had a reasonable expectation of success in combining the
mutations of these analogs for providing the properties thereof. Patent
Owner has provided no meaningful evidence to the contrary.
While we agree that the properties identified in the prior art must be
verified for each analog and that some combined analogs may not, in fact,
possess the expected properties, verification is not indicative of non-
obviousness because the expectation of success need only be reasonable, not
absolute. Pfizer, Inc. v. Apotex, Inc., 480 F.3d 1348, 1367–369 (Fed. Cir.
2007) (simply because the properties of a compound must be verified
through testing does not mean that the compound satisfies the test for
patentability “since the expectation of success need only be reasonable, not
absolute”). The evidence shows that such verification was routine in the art.
Patent Owner further does not present any meaningful evidence that
the additional references relied upon by the Examiner fail to provide
additional evidence that the described mutations would have an expectation
of structural integrity and biological activity. See PO App. Br. 23. Thus, the
evidence further supports that the proposed modifications to G-CSF would
have been expected to provide structural integrity and biological activity.
With respect to separately argued claim 5, Patent Owner generally
repeats the arguments discussed above and further emphasizes that, for
example, Example 28 of Camble ‟630 is selected for further modification
because it is the only analog in Camble ‟630 with substitutions in each of
helices A, C and D. See e.g., PO App. Br. 12-13 and 14.
As discussed above, we find that the prior art would have led the
skilled artisan to any of the disclosed point mutations, particularly those
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described in the various examples in the prior art. While Camble ‟630 may
have included only one example with substitutions in each of helices A, C
and D, Camble ‟630 further discloses analogs with substitutions in only one
of helix A, helix C or helix D and other analogs with substitutions in more
than one of helix A, C, and D. Further, Camble ‟630 indicates that any
combination of these analogs would be expected to improve solution
solubility. See e.g., Camble ‟630, p. 3, ll. 19-21 (“The above defined
modifications may thus, if desired, be introduced into any polypeptide
having at least one of the biological properties of naturally occurring G-CSF
in order to improve the solution stability of the molecule.”).
As discussed above, even with respect to claim 5, the Examiner does
not appear to rely on specific examples in the Camble, Shaw and
Cunningham references, but rather the general teaching of properties
exhibited by known modifications to G-CSF.
Accordingly, we affirm Rejections 1-14 of all the claims maintained
by the Examiner.

II. ADDITIONAL REJECTIONS BASED ON AN
ALTERNATIVE THEORY OF OBVIOUSENSS REGARDING PRIOR
ART KNOWLEDGE OF SECONDARY STRUCTURE
The remaining rejections are based on an alternative theory of
unpatentability of claims 1-8 provided by the Requester and adopted by the
Examiner. See RAN 22-39 (discussing Rejections 15-35).
Because affirming Rejections 1-14 based on the discussion above
affirms the rejection of all of the claims under reexamination, we need not
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reach these additional rejections and thus the alternative theory proposed by
the Requester and adopted by the Examiner.

TIME PERIOD FOR RESPONSE
In accordance with 37 C.F.R. § 41.79(a)(1), the “[p]arties to the
appeal may file a request for rehearing of the decision within one month of
the date of: . . . [t]he original decision of the Board under § 41.77(a).” A
request for rehearing must be in compliance with 37 C.F.R. § 41.79(b).
Comments in opposition to the request and additional requests for rehearing
must be in accordance with 37 C.F.R. § 41.79(c) & (d), respectively. Under
37 C.F.R. § 41.79(e), the times for requesting rehearing under paragraph (a)
of this section, for requesting further rehearing under paragraph (d) of this
section, and for submitting comments under paragraph (c) of this section
may not be extended.
An appeal to the United States Court of Appeals for the Federal
Circuit under 35 U.S.C. §§ 141-144 and 315 and 37 C.F.R. § 1.983 for an
inter partes reexamination proceeding “commenced” on or after November
2, 2002 may not be taken “until all parties' rights to request rehearing have
been exhausted, at which time the decision of the Board is final and
appealable by any party to the appeal to the Board.” 37 C.F.R. § 41.81. See
also MPEP § 2682 (8th ed., Rev. 7, July 2008).

Appeal 2013-004840
Reexamination Control 95/000,440
Patent 7,381,804 B2

19

AFFIRMED

alw

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