Research Institute at Nationwide Children's Hospital

Patent Trials and Appeals Board

Apr 12, 2021

2020006226 (P.T.A.B. Apr. 12, 2021)

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.
15/308,445 11/02/2016 Christopher Breuer NWCH 2014-002 4119
23579 7590 04/12/2021
PABST PATENT GROUP LLP
1545 PEACHTREE STREET NE
SUITE 320
ATLANTA, GA 30309
EXAMINER
HOWARD, ZACHARY C
ART UNIT PAPER NUMBER
1646
NOTIFICATION DATE DELIVERY MODE
04/12/2021 ELECTRONIC
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.
Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the
following e-mail address(es):
docketing@pabstpatent.com
PTOL-90A (Rev. 04/07)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte CHRISTOPHER BREUER, NARUTOSHI HIBINO,
VIDU GARG, and CAMERON BEST
____________

Appeal 2020-006226
Application 15/308,445
Technology Center 1600
____________

Before DONALD E. ADAMS, FRANCISCO C. PRATS, and
TAWEN CHANG, Administrative Patent Judges.

ADAMS, Administrative Patent Judge.

DECISION ON APPEAL
Pursuant to 35 U.S.C. § 134(a), Appellant1 appeals from Examiner’s
decision to reject claims 2–4, 8–20, 22, and 23 (see Appeal Br. 2).2 We have
jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.

1 We use the word “Appellant” to refer to “applicant” as defined in 37
C.F.R. § 1.42. Appellant identifies the real party in interest as “Research
Institute at Nationwide Children’s Hospital, the assignee of record, and its
licensee, Lyst Therapeutics” (Appellant’s March 20, 2020, Appeal Brief
(Appeal Br.) 2).
2 Pending claims 21 and 24 stand “withdrawn from consideration as being
drawn to a non-elected invention” (Appeal Br. 2).
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STATEMENT OF THE CASE
Appellant’s disclosure relates “to compositions, devices, and methods
for enhancing vascular tissue regeneration, as well as reducing morbidity
and mortality associated with neointimal hyperplasia and fibroproliferative
disease” (Spec.3 ¶ 4). Appellant’s independent claim 16 is reproduced
below:
16. A method of reducing or preventing macrophage
infiltration, scar formation, or stenosis in a subject, comprising
administering to a subject up to three days prior to
surgery, at the time of surgery, or up to 14 days after surgery an
effective amount of a composition comprising:
a) a LYST inhibitor consisting of a monoclonal
antibody or antibody fragment inhibiting lysosomal trafficking
regulator (LYST) having the same binding specificity as the
antibody used in Example 5, in an amount effective to reduce or
prevent macrophage infiltration, natural killer cell activation,
and to reduce or prevent platelet activation in the subject; and
b) a physiologically acceptable carrier,
wherein the amount of the LYST inhibitor does not
prevent vascular neotissue formation in the subject,
optionally in combination with one or more additional
therapeutic agents,
wherein the LYST inhibitor is administered in an amount
and at a time effective to decrease scar formation, myocardial
infarction, scarring adhesions, and liver fibrosis or to reduce or
prevent platelet activation that could lead to arterial or venous
thrombosis in a subject.
(Appeal Br. 25–26.)
Claims 2–4, 8–20, 22, and 23 stand rejected under the written
description provision of 35 U.S.C. § 112(a).

3 Breuer et al., US 2017/0073401 A1, published Mar. 16, 2017.
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ISSUE
Does the preponderance of evidence on this record support
Examiner’s finding that Appellant’s Specification fails to provide written
descriptive support for the claimed invention?
ANALYSIS
The method of Appellant’s claim 16, reproduced above, comprises,
inter alia, the administration of a LYST inhibitor to a subject, wherein the
LYST inhibitor consists of a monoclonal antibody or antibody fragment
having the same binding specificity as the antibody used in Example 5 of
Appellant’s Specification. In addition, Appellant’s claim 16 requires that
the monoclonal antibody or antibody fragment is administered in an amount
effective to reduce or prevent macrophage infiltration, natural killer cell
activation, and platelet activation in the subject, and in an amount and at a
time effective to decrease scar formation, myocardial infarction, scarring
adhesions, and liver fibrosis or to reduce or prevent platelet activation that
could lead to arterial or venous thrombosis in a subject.
Examiner finds that although Appellant’s Specification does not
identify the anti-LYST antibody used in Example 5 of Appellant’s
Specification, Breuer declares that the antibody used in Example 5 of
Appellant’s Specification was “the ABCAM mouse monoclonal antibody
ab118121” (hereinafter “ab118121 antibody”) (Ans. 9; see Breuer Decl.4
¶ 13 (Breuer declares that “[w]e used the ABCAM mouse monoclonal
antibody ab118121 made using amino acids 1-101 of Human LYST as the
immunogen.”); see also Appeal Br. 13 (Appellant states that “[t]he antibody

4 Declaration of Dr. Christopher Kane Breuer, signed October 24, 2019.
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used in Appellant’s Example 5 is the ab118121 antibody that is highly
specific for LYST.”)). Examiner, therefore, finds that Appellant’s
Specification provides written descriptive support “for the claimed method
with respect to the antibody used in Example 5 (i.e., the ab11821 antibody)”
(Ans. 9–10; see also id. at 13 (Examiner finds that Appellant’s “description
of Examples 1-5 . . . only provide[s] a ‘reduction to practice’ for the
antibody used in Example 5, which has been established to be the . . .
[ab118121] antibody”); see also id. at 16–17).
Examiner finds, however, that Appellant’s claim 16 is not limited to
the ab11821 antibody, but is “instead directed to a genus that encompasses
any monoclonal antibody structure having the same ‘binding specificity’ as
the” ab11821 antibody and fragments thereof, which inhibit LYST and,
thereby, are effective to reduce or prevent macrophage infiltration, natural
killer cell activation, and reduce or prevent platelet activation; and decrease
scar formation, myocardial infarction, scarring adhesions, and liver fibrosis,
or to reduce or prevent platelet activation that could lead to arterial or
venous thrombosis, in a subject, as required by Appellant’s claim 16 (Ans.
10; see also id. at 13; id. at 18). In this regard, Examiner finds that a
monoclonal antibody or fragment thereof that has the same “binding
specificity” as the ab11821 antibody is a monoclonal antibody or fragment
thereof that binds the same epitope as the ab11821 antibody (id. at 10).
Therefore, we are not persuaded by Appellant’s contention that “binding to a
specific portion of LYST is not critical” and “[i]t is not required to know
what epitope the anti-LYST antibody binds” (Appeal Br. 20; cf. Reply Br. 6
(Appellant contents “the region of LYST required for activity in two animal
models was . . . identified by Appellant” and “[t]his demonstrates that
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[Appellant] knew the critical region of a known protein, LYST, required for
activity, demonstrated through amino acid substitution and through the use
of a monoclonal antibody”)).
Examiner finds that Appellant’s Specification “does not disclose any
other monoclonal antibody structure that has the function of being a LYST
inhibitor or any other monoclonal antibody structure that has the same
binding specificity as the [ab11821] antibody” (Ans. 10; see Appeal Br. 20
(Appellant contends that the inhibition of LYST activity is critical to its
claimed invention)). In this regard, Examiner finds that although
Appellant’s Specification discloses that
“[a] variety of antibodies that bind the human LYST protein are
commercially available from multiple sources, for example,
Santa Cruz Biotechnology, CA, US, Cat. No. sc-136746” . . .,
this [disclosure] does not describe which, if any, of these
purported antibodies that bind to LYST are also inhibitors of
LYST and/or hav[e] the same binding specificity as [the]
ab118121 [antibody] as required for use in [the method of
Appellant’s claim 16].
(Ans. 10; see also id. at 16; Spec. ¶ 76.) Examiner further finds that the sc-
136746 antibody disclosed in Appellant’s Specification “is a polyclonal
antibody” and, thus, is outside the scope of Appellant’s claim 16, which is
“limited to [the] use of monoclonal antibodies” (Ans. 10). Therefore, we are
not persuaded by Appellant’s contentions regarding the sc-136746 antibody
(see Appeal Br. 18–19). Examiner further finds that Appellant fails to
establish an evidentiary basis on this record to support a finding that the sc-
136746 antibody “is a LYST inhibitor or ha[s] the same binding specificity
as [the] ab118121 [antibody]” (Ans. 10; see also id. at 16).
For the foregoing reasons, Examiner finds that “[t]he limited
disclosure[, in Appellant’s Specification,] that LYST-binding antibodies
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exist is not sufficient to describe the genus of antibody structures having the
required functionality; i.e., inhibiting LYST functionality and having the
same binding specificity as [the] ab 118121 [antibody]” (id. at 10; see also
id. at 16).
Examiner finds that although the ab11821 antibody was generated
using a fragment of LYST consisting of amino acids 1-101, neither
Appellant’s Specification nor the evidence of record describes the epitope
within this 101 amino acid fragment of LYST that is bound by the ab11821
antibody (id. at 11). In this regard, Examiner reasons that because
antibodies generally bind epitopes that are approximately 5–7 amino acids in
length, it is likely that the LYST fragment used to make the ab118121
antibody “contains multiple possible epitopes, and even [if the 101 amino
acid LYST fragment contains only one epitope,] a single epitope is capable
of generating multiple antibody structures (having different CDRs) that bind
to it” (id.). Stated differently, even if the LYST fragment used to make the
ab118121 antibody contained only one epitope, a person of ordinary skill in
this art would reasonably expect other antibodies having the same binding
specificity as ab118121 to have different structures, e.g., different antibody
CDR and framework regions, including framework regions that affect the
structure of the antibody’s binding site. Thus, Examiner finds that
Appellant’s “disclosure of a single antibody structure[, the ab118121
antibody,] . . . that binds to LYST is not sufficient to describe the structure
of the genus of antibodies that inhibit LYST functionality and have the same
binding specificity” (Ans. 11; see also id. at 13 (Examiner finds that “the
portion of each antibody that provides its binding specificity, the set of
six . . . [CDRs], is independent of the set found in each other antibody, and
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thus knowledge of one set of CDRs does not provide any predictable
information about other sets of CDRs that provide binding specificity, even
with regard to the same [epitope]”)).
For the foregoing reasons, we are not persuaded by Appellant’s
contentions regarding the CDRs of the ab118121 antibody (Reply Br. 3; see
also id. at 6–7 and 9). For the reasons discussed above, a person of ordinary
skill in this art would understand that Appellant’s claim 16 is not limited to
the ab118121 antibody, that although the CDRs of the ab118121 antibody
are specific to the ab118121 antibody they are not inherent, or specific, to
other antibodies that bind the same epitope. To the contrary, those of
ordinary skill in this art would recognize that although different antibodies
may bind the same epitope they may have different affinities for that
epitope, establishing that structural differences are present in different
antibodies that bind the same epitope.
In addition, Examiner finds that “the structure of the binding region of
an antibody, i.e., . . . [CDRs], does not predictably correlate with its
functionality, e.g., binding to and inhibiting a particular antigen” (Ans. 14).
Stated differently, Examiner finds that “not all antibodies that bind to LYST
will necessarily be inhibitors of the protein[,] as an antibody can bind to a
protein without interfering with its function. Inhibitory antibodies only
represent a subset of the antibodies that bind to a protein” (Ans. 18).
Therefore, we are not persuaded by Appellant’s contention “that anti-LYST
antibodies are known and commercially available” (Appeal Br. 20). For the
same reason, we are not persuaded by Appellant’s contention that “[a] genus
of antibody fragments having the binding specificity of a known and
described monoclonal antibody would necessarily have the same binding
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specificity” and, thus, provides “an art-established correlation between
structure of CDRs and their function” (Reply Br. 5).
We are not persuaded by Appellant’s contention that “[i]t would be
routine to verify that the antibody or fragment thereof inhibits the activity of
LYST” (Reply Br. 3). See Lockwood v. American Airlines Inc., 107 F.3d
1565, 1572 (Fed. Cir. 1997) (“One shows that one is ‘in possession’ of the
invention by describing the invention, with all its claimed limitations, not
that which makes it obvious. One does that by such descriptive means as
words, structures, figures, diagrams, formulas, etc., that fully set forth the
claimed invention.”) (citation omitted, emphasis in original); see also Ariad
Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1352 (Fed. Cir. 2010) (en
banc) (Although those of ordinary skill in this art may understand how to
prepare antibodies, “it is the specification itself that must demonstrate
possession. And while the description requirement does not demand any
particular form of disclosure, . . . or that the specification recite the claimed
invention in haec verba, a description that merely renders the invention
obvious does not satisfy the requirement.”).
We are not persuaded by Appellant’s contention that “Examiner
erroneously interprets the ‘binding specificity’ of a monoclonal antibody
required by the claims to mean ‘binding specificity’ of a pool of polyclonal
antibodies” (Reply Br. 5). To the contrary, Examiner correctly interprets the
breadth of Appellant’s claim 16 to include any of a number of different
monoclonal antibodies that bind the same epitope of the ab11821 antibody
and is capable of achieving the functionality of Appellant’s claim 16 (see
Ans. 10).
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“[T]he test for sufficiency [of the written description] is whether the
disclosure of the application relied upon reasonably conveys to those skilled
in the art that the inventor had possession of the claimed subject matter as of
the filing date.” Ariad, 598 F.3d at 1351. To be complete, we note that the
written description standard set out in Ariad applies to antibodies. See
Amgen, Inc. v. Sanofi, 872 F.3d 1367, 1376–79 (Fed. Cir. 2017) (applying
the Ariad standard to antibodies claimed based on their binding and blocking
activities); see also AbbVie Deutschland GmbH & Co. v. Janssen Biotech,
Inc., 759 F.3d 1285, 1298-1300 (Fed. Cir. 2014) (same).
A “sufficient description of a genus . . . requires the disclosure of
either a representative number of species falling within the scope of the
genus or structural features common to the members of the genus so that one
of skill in the art can ‘visualize or recognize’ the members of the genus.”
Ariad, 598 F.3d at 1350. “[A]n adequate written description requires a
precise definition, such as by structure, formula, chemical name, physical
properties, or other properties, of species falling within the genus sufficient
to distinguish the genus from other materials.” Id. Although “functional
claim language can meet the written description requirement when the art
has established a correlation between structure and function,” “merely
drawing a fence around the outer limits of a purported genus is not an
adequate substitute for describing a variety of materials constituting the
genus and showing that one has invented a genus and not just a species.” Id.
In addition, although Appellant’s claim 16 is directed to a method
rather than a product, we note that the same standard applies with regard to
the written description requirement. As the Rochester Court made clear:
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Regardless whether a compound is claimed per se or a method
is claimed that entails the use of the compound, the inventor
cannot lay claim to that subject matter unless he can provide a
description of the compound sufficient to distinguish infringing
compounds from non-infringing compounds, or infringing
methods from non-infringing methods.
University of Rochester v. G.D. Searle & Co., 358 F.3d 916, 926 (Fed. Cir.
2004).
For the reasons discussed above, we agree with Examiner’s finding
that Appellant’s Specification fails to provide written descriptive support for
the genus of monoclonal antibodies, and fragments thereof, that fall within
the scope of Appellant’s claim 16.
CONCLUSION
The preponderance of evidence on this record supports Examiner’s
finding that Appellant’s Specification fails to provide written descriptive
support for the claimed invention. The rejection of claim 16 under the
written description provision of 35 U.S.C. § 112(a) is affirmed. Claims 2–4,
8–15, 17–20, 22, and 23 are not separately argued and fall with claim 16.5

DECISION SUMMARY
In summary:
Claim(s)
Rejected
35 U.S.C. § Reference(s)/Basis Affirmed Reversed
2–4, 8–20,
22, 23
112(a) Written
Description
2–4, 8–20,
22, 23

5 See Appeal Br. 9 (Appellant states that “the claims will be grouped
together as claims 2-5, 8-20, 22 and 23”).
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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). See 37 C.F.R
§ 1.136(a)(1)(iv).

AFFIRMED