Ex Parte Ogasawara et al

Patent Trial and Appeal Board

Dec 28, 2016

11992750 (P.T.A.B. Dec. 28, 2016)

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
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APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
11/992,750 06/18/2008 Hideaki Ogasawara 25689-0004US1 2022
26211 7590 12/30/2016
FISH & RICHARDSON P.C. (NY)
P.O. BOX 1022
MINNEAPOLIS, MN 55440-1022
EXAMINER
JUEDES, AMY E
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
12/30/2016 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
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PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte HIDEAKI OGASAWARA, KEIKO MIZUNO,
YOSHIHISA ARITA, MIYUKINISHIMURA, and TOSHIO IMAI1
Appeal 2014-009797
Application 11/992,750
Technology Center 1600
Before FRANCISCO C. PRATS, TAWEN CHANG, and
TIMOTHY G. MAJORS, Administrative Patent Judges.
PRATS, Administrative Patent Judge.
DECISION ON APPEAL
This appeal under 35 U.S.C. § 134(a) involves claims to an antibody,
or a functional fragment of an antibody, that binds to a protein involved in
the interaction between T cells and dendritic cells. The Examiner entered an
alternative rejection for anticipation and/or obviousness.
We have jurisdiction under 35 U.S.C. § 6(b). We reverse.
STATEMENT OF THE CASE
Appellants’ invention involves the isolation of a protein, termed
“TARM” (T cell-interacting Activating Receptor on Myeloid Cells), which,
1 Appellants identify Eisai R&D Management Co., Ltd. as the real party in
interest. App. Br. 1.
Appeal 2014-009797
Application 11/992,750
in humans, has the amino acid sequence shown in SEQ ID NO: 10. Spec.
11, 24. In particular, the Specification discloses that dendritic cells,
which have an antigen-presenting function, adhere to T cells via the TARM
protein. Id. 176. The Specification discloses, moreover, that antibody that
prevents adhesion of TARM to T cells has a therapeutic effect in a mouse
model of rheumatoid arthritis. Id. 177.
Claims 7 and 9 are the appealed claims, and read as follows (App. Br.
10):
7. An antibody or a functional fragment thereof which
binds to a membrane or secretory protein consisting of the
amino acid sequence of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID
NO: 6, SEQ ID NO: 8, SEQ ID NO: 10 or SEQ ID NO: 12,
wherein said antibody or a functional fragment thereof inhibits
adhesion of a T cell to said membrane or secretory protein, and
said antibody is monoclonal.
9. The antibody or a functional fragment thereof
according to claim 7, which is an antibody or a functional
fragment thereof which binds to a membrane or secretory
protein consisting of the amino acid sequence of SEQ ID NO:
10.
The sole rejection before us for review is the Examiner’s
rejection of claims 7 and 9 under 35 U.S.C. § 102(b) as anticipated by
or, in the alternative, under 35 U.S.C. § 103(a) as obvious over
Boyle.2 Ans. 3^4.
In response to a species election requirement, Appellants elected the
protein having the amino acid sequence of SEQ ID NO: 10 (human TARM
2 WO 01/55335 A2 (published Aug. 2, 2001).
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Application 11/992,750
protein) as the protein that binds the claimed antibody or fragment. See
App. Br. 2.
We, therefore, limit our analysis of claims 7 and 9 to the patentability
of the elected species, and the extent to which the claims read on them. See
Ex parte Ohsaka, 2 USPQ2d 1460, 1461 (BPAI 1987).
DISCUSSION
As stated in In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992):
[T]he examiner bears the initial burden ... of presenting a
prima facie case of unpatentability. . . .
After evidence or argument is submitted by the applicant
in response, patentability is determined on the totality of the
record, by a preponderance of evidence with due consideration
to persuasiveness of argument.
We agree with Appellants that a preponderance of the evidence does
not support the Examiner’s prima facie case of anticipation, or the
Examiner’s prima facie case of obviousness, over Boyle.
Boyle discloses the evaluation of polynucleotides from cDNA
libraries from a number of biological sources, among them bone marrow
mRNA. Boyle, Abstract. Based on sequence analysis of those
polynucleotides, Boyle predicted the existence of a number of polypeptides,
including a polypeptide encoded by SEQ ID NO: 66. Id. at 4, 19—21, 129—
1313. The Examiner asserts (Ans. 3), and Appellants do not dispute, that the
amino acid sequence of SEQ ID NO: 66 is identical to SEQ ID NO: 10 of
Appellants’ claim 1.
Boyle also identified a number subsequences of SEQ ID NO: 66 that
were homologous to regions of known proteins, and designated the predicted
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polypeptide of SEQ ID NO: 66 as the “leukocyte immunoglobulin receptor­
like polypeptide” or “LIR-like” polypeptide. Boyle 19, 130.
Although Boyle did not ascertain the specific function of the predicted
protein encoded by SEQ ID NO: 66, as the Examiner points out (Ans. 3—4),
Boyle discloses a number of T cell-related assays that may be used to
ascertain the function of the proteins described in the reference. Boyle 58—
59, 66—69. As the Examiner also points out, Boyle discloses the suitability
of preparing antibodies to the proteins predicted by its sequence analysis,
including preparing antibodies to the protein encoded by SEQ ID NO: 66.
Id. at 94.
Thus, as the Examiner contends, Boyle describes generating
antibodies to a protein having an amino acid sequence identical to the
elected species of protein recited in Appellants’ claims 7 and 9. Appellants’
claims, however, also require the claimed antibody to “inhibit[] adhesion of
a T cell to said membrane or secretory protein, and said antibody is
monoclonal.” App. Br. 10 (claim 7).
As Appellants point out, the Arita Declaration (“Arita Decl.”)3
discloses that 15 monoclonal antibodies were generated against the TARM
protein having SEQ ID NO: 10, but only 12 of those clones inhibited
adhesion in the assay described at || 215—217 of Appellants’ Specification.
Arita Decl. 2. Appellants contend, therefore, that Boyle does not inherently
describe antibodies that meet the adhesion feature of claims 7 and 9. See
App. Br. 3.
3 Declaration of Yoshihisa Arita under 37 C.F.R. 8 1.132 (signed December
22, 2011).
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Application 11/992,750
In response, the Examiner contends that the “evidence cited by
Appellant demonstrates that of 15 antibodies produced that bind to cell
expressed TARM protein, 12 clones did ha[ve] the function of inhibiting T
cell adhesion (i.e. 80%).” Ans. 4. Moreover, the Examiner contends, Boyle
“discloses producing antibodies by the same methods of the instant
application, and discloses antibodies that bind to cell-associated protein (see
page 95 and 97, in particular).” Id. at 4—5. In addition, the Examiner
contends, Boyle “discloses screening processes for the produced antibodies,
including functional assays employing T cells and dendritic cells which
would lead to the identification of antibodies identical to the instant claims
(see pages 58-59 and 66-68, in particular).” Id. at 5.
Appellants have the better position.
It is well settled that inherency “may not be established by
probabilities or possibilities. The mere fact that a certain thing may result
from a given set of circumstances is not sufficient.” In re Oelrich, 666 F.2d
578, 581 (CCPA 1981); see also Agilent Technologies, Inc. v. Affymetrix,
Inc., 567 F.3d 1366, 1383 (Fed. Cir. 2009) (“The very essence of inherency
is that one of ordinary skill in the art would recognize that a reference
unavoidably teaches the property in question.”) (emphasis added).
Thus, in the present case, even if we assume, based on the Arita
Declaration, that there was an 80% probability that antibodies to Boyle’s
protein of SEQ ID NO: 66 would inhibit adhesion as required by Appellants’
claims, that likelihood is insufficient to show that Boyle’s antibodies
unavoidably meet the claimed adhesion feature. Accordingly, because the
Examiner has not shown that Boyle’s antibodies either expressly or
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Application 11/992,750
inherently possess all of the properties required by Appellants’ claims, we
reverse the Examiner’s anticipation rejection over Boyle.
As to the obviousness component of the rejection, the Examiner
contends that, “[alternatively, it would be obvious to follow the teachings of
the [Boyle] reference, to produce and screen for antibodies that inhibit T cell
function using the standard, art recognized assays disclosed by the
references, and the assays would produce antibodies identical to those of the
instant claims.” Ans. 5. In particular, the Examiner contends:
Alternatively, it would be obvious to produce and identity the
antibodies of [Boyle] using the disclosed functional assays,
such as using the dendritic cell dependent assays, which
identify proteins expressed by dendritic cells that activate naive
T cells, as disclosed on page 69. Said assay would identity an
antibody that inhibits T cell activation, which is necessarily
linked to the adhesion function of the T cells ....
Ans. 6.
We acknowledge that Boyle discloses approximately 9 different
assays that may be used to determine whether its predicted proteins are
involved in activation of naive T cells by dendritic cells. Boyle 69. We
acknowledge also, as the Examiner contends (Ans. 6), that Boyle discloses
that blocking T cell function is a desirable property potentially possessed by
its proteins. Boyle 67.
Boyle, however, discloses that its predicted proteins may potentially
modulate a significant number of other immune response-related processes,
in either stimulating or inhibiting roles, which can be ascertained using a
variety of animal models or assays. Id. at 67—69. Boyle similarly discloses
numerous T cell-related proliferation assays that may be also be used to
determine the function of its predicted proteins. Id. at 57—59. Boyle also
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Application 11/992,750
posits that its proteins may have other biological functions, including effects
on stem cell growth, hematopoiesis, tissue growth, chemotaxis activity, and
others. Id. at 59—65, 69-80.
As noted above, Boyle does not describe or ascertain any particular
function for the protein of SEQ ID NO: 66. Thus, to obtain the antibody of
Appellants’ claims by following Boyle’s disclosure, an ordinary artisan
would have had to first ascertain the function of the protein of Boyle’s SEQ
ID NO: 66, which involves performing any number of the numerous
different assays Boyle describes, with no specific guidance identified by
either the Examiner or Boyle as to which particular assays would be most
pertinent to the protein of SEQ ID NO: 66, or whether those assays would
necessarily demonstrate the adhesion-inhibiting property recited in
Appellants’ claims. Then, having followed that unguided pathway to
ascertain the biological activity of the protein, the ordinary artisan would
have to generate antibodies to the protein, and determine whether the
antibody inhibited the protein’s T cell adhesion function, an assay for which
Boyle, again, provides no specific guidance.
We are not persuaded, therefore, that Boyle suggests the antibody of
Appellants’ claims with adequate specificity. Rather, we agree with
Appellants (see Reply Br. 5), that given the breadth of Boyle’s disclosure, an
ordinary artisan lacked a reasonable expectation of success in arriving at the
claimed antibodies.
As our reviewing court has explained, “[ojbviousness does not require
absolute predictability of success .... [For obviousness under § 103,] all
that is required is a reasonable expectation of success.” In re Kubin, 561
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Application 11/992,750
F.3d 1351, 1360 (Fed. Cir. 2009) (quotingIn re O’Farrell, 853 F.2d 894,
903-04 (Fed. Cir. 1988) (emphasis removed).
Nonetheless, in the present case, in which an ordinary artisan must
vary numerous parameters, select from numerous choices, or apply a
potentially promising but unguided general approach, we are unpersuaded
the skilled person would have predictably gone down the path proposed by
the Examiner. See In re O’Farrell, 853 F.2d at 903. Indeed, given the
numerous choices and lack of specific guidance provided by Boyle, we find
the present case to be substantially similar to the scenario criticized by the
court in Kubin, in which the obviousness proponent “merely throws
metaphorical darts at a board filled with combinatorial prior art
possibilities.” Kubin, 561 F.3dat 1359.
In sum, for the reasons discussed, Appellants persuade us that a
preponderance of the evidence does not support the Examiner’s prima facie
case of obviousness. Accordingly, we reverse the Examiner rejection of
claims 7 and 9 under § 103(a) over Boyle.
SUMMARY
We reverse the Examiner’s rejection of claims 7 and 9 under
35 U.S.C. § 102(b) as anticipated by or, in the alternative, under 35 U.S.C.
§ 103(a) as obvious over Boyle.
REVERSED
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