DENKA SEIKEN CO., LTD.

Patent Trials and Appeals Board

Dec 30, 2021

2021001912 (P.T.A.B. Dec. 30, 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.
14/917,790 03/09/2016 Koichi INANO 0760-0462PUS1 7732
2292 7590 12/30/2021
BIRCH STEWART KOLASCH & BIRCH, LLP
8110 Gatehouse Road
Suite 100 East
Falls Church, VA 22042-1248
EXAMINER
HILL, MYRON G
ART UNIT PAPER NUMBER
1648
NOTIFICATION DATE DELIVERY MODE
12/30/2021 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):
mailroom@bskb.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
__________

Ex parte KOICHI INANO, TAKASHI MIYAZAWA, and
OSAMU ISHIKAWA
__________

Appeal 2021-001912
Application 14/917,790
Technology Center 1600
__________

Before RICHARD M. LEBOVITZ, JOHN G. NEW, and
DAVID COTTA, Administrative Patent Judges.

COTTA, Administrative Patent Judge.

DECISION ON APPEAL

This is an Appeal under 35 U.S.C. § 134 involving claims to a method for
measuring influenza A virus.1 The Examiner rejected the claims as failing to
comply with the written description requirement. A hearing was held on
September 27, 2021, a transcript from which has been entered into the record
(“Tr.”). We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM and enter a NEW GROUND OF REJECTION.

1 We use the word “Appellant” to refer to “applicant” as defined in 37 C.F.R.
§ 1.42. Appellant identifies DENKA SEIKEN CO., LTD., the real party in interest
as Appeal Br. 3.
Appeal 2021-001912
Application 14/917,790

2
STATEMENT OF THE CASE
The Specification discloses that “[i]nfluenza virus is a virus having
segmental negative-strand RNA as the genomic gene, which is composed of eight
segments, that is, HA, NA, PA, PB1, PB2, M, NP, and NS segments.” Spec. ¶ 4.
According to the specification “[i]nfluenza virus can be divided into type A, type
B, and type C depending on the antigenicities of matrix protein (M1) and
nucleoprotein (NP) among the proteins constituting the virus.” Id. “Two different
genes, M1 and M2, are encoded in the M segment of influenza A virus” with each
encoding a constituent protein. Id. ¶ 5. The Specification teaches that the M1
protein is “localized such that the inside of the viral envelope is lined therewith,
and it is thought that M1 substantially plays a role as a shell.” Id.
The Specification discloses how influenza was detected before the method
claimed by the Appellant:
In conventional detection of influenza, an anti-NP antibody, anti-M2
antibody, or the like has been particularly used. Although there are
reports in which, for example, an anti-M1 antibody which undergoes
antigen-antibody reaction with M1 was used in a study, the anti-M1
antibody was not used for an immunoassay device for the purpose of
aiding diagnosis.
Id. ¶ 8 (internal citations omitted). According to the Specification “the reactivity
was low in these methods depending on the subtype of the influenza A virus.” Id.
¶ 11.
The Specification discloses that “[a]s a result of intensive study, the present
inventors succeeded in preparation of an anti-influenza A monoclonal antibody
which specifically reacts with influenza A virus, using M1 of influenza A virus as
an antigen.” Id. ¶ 13. This method has the advantage that it “enables measurement
of influenza A virus subtypes which have been difficult to detect by conventional
immunoassays using an anti-NP monoclonal antibody.” Id
Appeal 2021-001912
Application 14/917,790

3
Claims 1, 2, 4, 5, 10, 11, 22, and 23 are on appeal. Claim 1 is
representative and reads as follows:
1. A method for measuring influenza A virus, said method
comprising
measuring influenza A virus by a sandwich immunoassay
comprising an antigen-antibody reaction between a monoclonal
antibody, or an antigen binding fragment thereof, and influenza A
virus in a sample,
wherein said monoclonal antibody, or the antigen binding
fragment thereof, specifically reacts with matrix protein (M1)
of influenza A virus,
wherein said method uses a first antibody, or an antigen
binding fragment thereof, which specifically binds to the amino
acids sequence IRHENRMVLASTTA (SEQ 1D NO:47), and/or
a second antibody, or an antigen binding fragment thereof,
which specifically binds to the amino acids sequence
DLLENLQAYQ (SEQ ID NO:23), and
wherein said first antibody, or the antigen binding
fragment thereof, and said second antibody, or the antigen
binding fragment thereof, are produced by immunizing an
animal with the matrix protein (Ml) of influenza A,
recovering antibody producing cells comprising at least spleen
or lymphocyte cells from said animal,
fusing said antibody producing cells with mouse myeloma cells
to prepare hybridoma cells,
cloning said hybridoma cells and
selecting said first antibody, or the antigen binding fragment
thereof, and/or said second antibody, or the antigen binding fragment
thereof, from the monoclonal antibodies produced by the cloned
hybridomas.
Appeal Br. 22 (Claims Appendix).

Appeal 2021-001912
Application 14/917,790

4
ANALYSIS
Claim 1 recites a method of measuring influenza A virus. The method
employs two antibodies: “a first antibody, . . . which specifically binds to the
amino acid sequence IRHENRMVLASTTA” and “a second antibody, . . . which
specifically binds to the amino acid sequence DLLENLQAYQ.” In rejecting claim
1 for failure to comply with the written description requirement, the Examiner
found that Appellant had not shown “possession of the genus of antibodies that
bind the recited epitope[s].” Ans. 4. The Examiner explained:
Here, appellant has defined the binding partner of the antibody not the
antibody itself. There is no showing of a structure function
relationship that allows recognition of the genus of possible antibodies
without having to screen for additional members of the genus. The
MPEP for written description, as noted above, require[s] disclosure of
a representative number of species of the genus or structure-function
relationship either disclosed or known in the art. Knowing how to
make antibodies does not teach or disclose the structure of the
antibody required for the specified binding function.
Ans. 8. On the record before us, we agree with the Examiner that claim 1 does not
comply with the written description requirement.
A description adequate to satisfy the written description requirement must
“clearly allow persons of ordinary skill in the art to recognize that [the inventor]
invented what is claimed.” Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336,
1351 (Fed. Cir. 2010) (enbanc). “[T]he test for sufficiency 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.” Id. In the case of a genus, “an adequate written description of a claimed
genus requires more than a generic statement of an invention’s boundaries.” Ariad
598 F.3d at 1349–50. “[S]ufficient description of a genus instead requires the
disclosure of either a representative number of species falling within the scope of
Appeal 2021-001912
Application 14/917,790

5
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.” Id. at 1350.
A functionally claimed genus “can meet the written description requirement when
the art has established a correlation between structure and function” however,
“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.
Here, it is undisputed that the claim language requiring a “a first antibody,
. . . which specifically binds to the amino acid sequence IRHENRMVLASTTA”
and a “a second antibody, . . . which specifically binds to the amino acid sequence
DLLENLQAYQ” encompasses a vast genus of antibodies. Appeal Br. 15–16
(Arguing that the using the antigen described in Example 1, one could “generate an
extremely large set of antibodies which meet the functional requirements of the
claims.”).
To support the “extremely large” genus of antibodies meeting the functional
binding requirements recited in the claim 1, Appellant directs us to “Example 1” of
the Specification, which, according to Appellant, “describes the preparation of a
monoclonal antibody against M1 protein.” Appeal Br. 15; see also Spec. ¶¶ 50–54
(Example 1). Appellant also directs us to the Specification’s disclosure of two
exemplary antibodies. Appeal Br. 15 (citing Spec. ¶¶ 20, 66–69 (Example 3), Fig
4). The two exemplary antibodies – “antibody a” and “antibody b” – are described
in the Specification as being “reactive with . . . peptides” corresponding to
sequences recited in the claims. Spec. ¶ 68. No further description of “antibody a”
or “antibody b” is provided. Id.; see also, generally Spec.
We agree with the Examiner that the disclosure of the Specification does not
meet the requirements for supporting a functionally claimed genus. Appellant does
Appeal 2021-001912
Application 14/917,790

6
not direct us to persuasive evidence supporting that “antibody a” is representative
of the genus of antibodies that binds to the claimed sequence
IRHENRMVLASTTA or that “antibody b” is representative of the genus of
antibodies that binds to the claimed sequence DLLENLQAYQ. Ariad, 598 F.3d at
1350. Nor does Appellant direct us to evidence of structural features common to
the members of the genus such that the person of ordinary skill can “‘visualize or
recognize’ the members of the genus.” Id. Indeed, Appellant does not direct us to
any description of “antibody a” or “antibody b” beyond the description of the
epitopes to which they bind. See generally, Appeal Br. The record is thus devoid
of evidence supporting a correlation between the structure and function of antibody
a and antibody b, as is necessary to support a functionally claimed genus. Ariad,
598 F.3d at 1350.
Much of Appellant’s argument centers on distinguishing this case from
Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017). Appellant argues that the
Federal Circuit merely rejected a jury instruction allowing the jury to find written
description based a showing that it was routine and conventional to make and use
the claimed antibodies because it improperly transformed a factual issue into a
legally required inference. Appeal Br. 13–14. Appellant thus contends that Amgen
“leaves open the possibility that ‘a functional genus claim to corresponding
antibodies, is one in which the underlying science establishes that a finding of
‘make and use’ (routine or conventional production) actually does equate to the
required description of the claimed products.’” Id. at 13. We are not persuaded.
Although Appellant correctly characterizes Amgen as reversing a written
description jury instruction on the basis that it improperly took a factual issue away
from the jury, this procedural posture does not give fact finders the freedom to find
written description support based solely on a description of the antigen to which an
Appeal 2021-001912
Application 14/917,790

7
antibody binds and/or a description of how to make the claimed antibody. Indeed,
the Amgen court explicitly states that the “newly characterized antigen” test, which
allowed patentees to claim antibodies by the epitope to which the bind, “flouts
basic legal principles of the written description requirement.” Amgen, 872 F.3d at
1378. The Amgen court also flatly rejected the notion that written description
could be grounded on a description of how to make and use the claimed antibodies.
Id. at 1378 (“By permitting a finding of adequate written description merely from a
finding of ability to make and use, the challenged sentence of the jury instruction
in this case ran afoul of what is perhaps the core ruling of Ariad.”). Moreover, a
recent Federal Circuit case found that, as a matter of law, a jury could not find
written description for claims reciting single-chain antibody variable fragments
(“scFv”) based on evidence that scFvs were known in the art (as was how to make
them), that the patent at issue included two working examples of scFvs, and that
scFvs have common structural features. Juno Therapeutics, Inc., v. Kite Pharma,
Inc. 10 F.4th 1330, 1336 (Fed. Cir. 2021) (“We agree with [defendant] that no
reasonable jury could find the ’190 patent’s written description sufficiently
demonstrates that the inventors possessed the full scope of the claimed
invention.”).
Appellant argues that, the claims in this appeal “are not even directed to
antibodies, per se, as they were in Amgen,” but rather to “a method of using a first
monoclonal antibody . . . and/or a second monoclonal antibody” which bind to a
specific amino acid sequence. Appeal Br. 14–15. We do not find this persuasive
because, although the claims are directed to a method, that method requires the use
of specifically recited antibodies. See e.g., Appeal Br. 22, (Claims App.)
(“[W]herein said method uses a first antibody, or an antigen binding fragment
Appeal 2021-001912
Application 14/917,790

8
thereof, which specifically binds to the amino acids sequence
IRHENRMVLASTTA.”).
Appellant argues that “the claimed invention only requires the use of well
known, conventional techniques to generate generic monoclonal antibodies binding
to the amino acid sequence IRHENRMVLASTTA (SEQ ID NO:47) or the amino
acid sequence DLLENLQAYQ (SEQ ID NO:23) of matrix protein (M1) of
influenza A virus.” Appeal Br. 15. According to Appellant “the process outlined
at Example 1 is a standard method of forming an antibody” that had “been around
for decades at the time the present application was filed.” Id. at 15–16 (emphasis
omitted). We are not persuaded because, as discussed above, one cannot show
written description by showing how to make and use antibodies.
Appellant argues that the inventors “had in fact, before the effective priority
date of the present application, following the protocols outlined in the Examples
generated a significant number of clones which met the functional requirements of
the claims” as evidenced at least by the Rizk Declaration. Appeal Br. 16 (citing
Rizk Decl. ¶¶ 17–19). We do not find this persuasive. The Specification provides
evidence of only two antibodies, and defines those antibodies only by the epitope
to which they bind. The cited paragraphs of the Rizk Declaration speak only to the
ability of the skilled artisan to generate antibodies, not to the number of antibodies
actually generated or disclosed in the Specification. See e.g., Rizk Decl. ¶¶ 17
(“[A] person trained in the art would be able to produce such antibodies.”), 18
(“[T]he inventors of the present application were capable of making any reasonable
number of antibody clones specific to the region of the 173rd to 186th amino acids
(IRHENRMVLASTTA) or the region of the 232nd to 241st amino acids
(DLLENLQAYQ) in the C-terminus portion of M1 influenza A protein as they
wished.”).
Appeal 2021-001912
Application 14/917,790

9
Accordingly, we agree with the Examiner that the Specification does not
provide written description support for the genus of monoclonal antibodies recited
in the claim. At oral argument, counsel for Appellant directed our attention to
Appeal No. 2020-006045. Tr. 14. That case involved an application filed by
Appellant and claims directed to a “method for detecting influenza B virus in an
immunoassay” using a “labelled monoclonal antibody or antigen binding fragment
thereof” that “reacts specifically with the region of the 125th to 248th amino acids
of M1 [matrix protein of influenza B virus].” Appeal No. 2020-006045, at 2–3.
The panel in that case found that the claims were supported in part because prior
art disclosed at least three antibodies that reacted with the claimed sequence – i.e.,
“the region of the 125th to 248th amino acids of M1.” Id. at 7–8 (citing Bucher
1989 as disclosing “3 antibodies that react with peptide 5 from the C-terminus of
the M1 protein”), 9 (citing Invitrogen Corp. v. Clontech Laboratories, Inc., 429
F.3d 1052, 1073 (Fed. Cir. 2005)) (finding written description support for claims
directed to a reverse transcriptase (“RT”) where the sequences of “representative
RT genes were known in the art.”); see also, Streck, Inc. v. Research & Diagnostic
Systems, Inc., 665 F.3d 1269, 1285 (Fed. Cir. 2012) (“[I]n some instances, a
patentee can rely on information that is ‘well-known in the art’ to satisfy written
description.”). Here, Appellant does not direct us to, and we do not find, evidence
that the prior art disclosed antibodies that bind the claimed sequences
(IRHENRMVLASTTA and DLLENLQAYQ). For this reason, we reach a
different decision than did the panel in Appeal No. 2020-006045. Accordingly, we
affirm the Examiner’s rejection of claim 1 for failure to comply with the written
description requirement.
Claims 2, 4, 5, 10, 11, 22, and 23 depend from claim 1 and additionally
recite: various influenza A virus subtypes with which the monoclonal antibody
Appeal 2021-001912
Application 14/917,790

10
undergoes antigen-antibody reaction (claim 2), the regions where claimed amino
acid sequences (IRHENRMVLASTTA and DLLENLQAYQ) can be found on the
M1 protein of the influenza A virus (claims 4 and 5), the type of immunoassay
used (claim 10), an additional antibody-antigen reaction between a monoclonal
antibody and a nucleoprotein of influenza A virus (claim 11), and various peptide
sequences with which the claimed antibodies do not react (claims 22 and 23).
Appellant does not direct us to additional or different evidence showing support for
any of these claims. Instead, for each of these claims, Appellant states:
The binding properties of the antibodies (not the specific amino acid
sequences thereof) are what cause the antibodies to be useful in the
specific method of the present invention. Thus, [each of these claims]
complies with the written description requirement for at least the
reasons set forth in connection with claim 1.
Appeal Br. 17–20. We do not find this argument persuasive for the reasons
discussed above with respect to claim 1. Accordingly, we affirm the Examiner’s
rejection of claims 2, 4, 5, 10, 11, 22, and 23 for failure to comply with the written
description requirement.
NEW GROUND OF REJECTION
Under the provisions of 37 C.F.R. § 41.50(b), we enter the following new
ground of rejection. Claim 1 is rejected under 35 U.S.C. 103(a) as obvious over
Bucher 19892 and Bucher 1991.3

2 Bucher et al., M Protein (M1) of Influenza Virus: Antigenic Analysis and
Intracellular Localization with Monoclonal Antibodies, 63(9) Journal of Virology
3622–3622 (1989) (“Bucher 1989”).
3 Bucher et al., Rapid Detection of Type A Influenza Viruses with Monoclonal
Antibodies to the M Protein (M1) by Enzyme-Linked Immunosorbent Assay and
Time-Resolved Fluoroimmunoassay, 29(11) Journal of Clinical Microbiology,
2484–2488 (1991) (“Bucher 1991”).
Appeal 2021-001912
Application 14/917,790

11
Findings of Fact
1. Bucher 1991 discloses the use of monoclonal antibodies to the M1
protein to detect influenza A virus. Bucher 1991 Abstract (“Monoclonal
antibodies (MAbs) to the M protein (M1) were used in the development of direct
detection systems for type A influenza viruses in clinical specimens.”).
2. Bucher 1991 discloses detecting M1 protein of influenza A virus
using a time-resolved fluoroimmunoassay (TRFIA). Id. at 2485. “The assay was
performed with microstrips previously coated overnight at room temperature with
0.5 to 1.0 μg of unlabelled MAb in 250 μl of carbonate buffer (pH 9.6) per well.”
Id. “Europium-chelated MAb (50 ng in 100 μl) was added immediately after the
specimen, and the microstrips were incubated at 37°C for 1 h.” Id. “[T]hree
MAbs, 2BB10-G9, 1G8-A11, and 1G11-D11, were selected for use as detector
antibodies and conjugated with europium chelate for use in TRFIA.” Id. at 2486.
“Seven MAbs recognizing three antigenic sites of M1 were used as capture
antibodies.” Id. “The optimal combination for detecting M1 proved be the use of
1G11-D11 as a capture antibody and 2BB10-G9-europium as an indicator
antibody.” Id.
3. Bucher 1991 discloses that “[h]ybridoma lines secreting MAbs to M1
were produced by fusion of spleen cells from mice immunized with M1 with
myeloma cells.” Id.
4. Bucher 1991 discloses that the M1 protein is “the most invariant
antigen of type A influenza viruses,” and, “[a]s such, M1 serves as an excellent
target for the detection of infection with type A influenza viruses.” Id. at 2484.
5. Bucher 1989 discloses “a panel of 16 monoclonal antibodies”
recognizing at least three antigenically distinct regions of M1. Bucher 1989,
Abstract.
Appeal 2021-001912
Application 14/917,790

12
Analysis
Bucher 1991 teaches a detecting influenza A using a sandwich immunoassay
comprising an antigen-antibody reaction between a monoclonal antibody and
influenza A virus in a sample. FF1, FF2. Bucher 1991’s assay uses a monoclonal
antibody that specifically reacts with matrix protein M1 of influenza A virus. Id.
The monoclonal antibodies used in Bucher 1991’s assay were produced by fusing
antibody producing cells spleen cells from mice myeloma cells to prepare
hybridoma cells. FF3.4 Bucher 1991 thus discloses all of the elements of claim 1
except that it does not disclose antibodies that bind to the specific sequences
recited in claim 1. For the reasons discussed below, we find that it would have
been obvious to detect influenza A virus using monoclonal antibodies that bind to
the claimed sequences.
The Specification discloses that influenza A M1 “is a protein constituted by
252 amino acid residues.” Id. ¶ 18. According to the Specification, the “[a]mino
acid sequences of A-M1 are known, and described in, for example GenBank:
ACD37490 (SEQ ID NO: 1).” Id. ¶ 19. Absent unexpected results or other
objective indicia of non-obviousness, it would have been obvious to detect
influenza A virus using a monoclonal antibody that binds to any portion of the M1
protein in view of Bucher 1991’s teaching that the M1 protein is “the most

4 In addition, we note that the language in claim 1 reciting how the claimed
monoclonal antibodies are produced appears to be product-by-process claim
language which does not lend patentability to an otherwise obvious product (here,
the monoclonal antibodies). In re Thorpe, 777 F.2d 695, 697, 227 USPQ 964, 966
(Fed. Cir. 1985) (“The patentability of a product does not depend on its method of
production. If the product in a product-by-process claim is the same as or obvious
from a product of the prior art, the claim is unpatentable even though the prior
product was made by a different process.”) (internal citation omitted).
Appeal 2021-001912
Application 14/917,790

13
invariant antigen of type A influenza viruses,” and, “[a]s such, M1 serves as an
excellent target for the detection of infection with type A influenza viruses.” FF4.
The current record also supports that the skilled artisan would have had a
reasonable expectation of success in obtaining monoclonal antibodies that bind the
claimed amino acid sequences. As explained in the Rizk Declaration:
[T]he antibodies of the claimed invention are not just specific to M1
antigen, but instead specific to the region of the 173rd to 186th amino
acids (IRHENRMVLASTTA) or the 232nd to 241st amino acids
(DLLENLQAYQ) in the C-terminus portion of M1 influenza A
protein. However, it would be reasonably expected that a significant
portion (but not all) of antibodies against Ml protein would be specific
to the C-terminus portion thereof.

* * *

[T]he method described [in the Specification] to isolate the above
mentioned antibodies is not the only method for isolating such types
of antibodies, and a person skilled in the field would conceivably use
another routine technique, such as phage display to isolate antibodies
with the ability to bind specifically to the region of the 173rd to 186th
amino acids (IRHENRMVLASTTA) or the region of the 232nd to
241st amino acids (DLLENLQAYQ) in the C-terminus portion of M1
influenza A protein. Phage display protocols have been established
prior to the patent applications in 2013 (See Fellouse, et al, Journal of
Molecular Biology, vol. 273, p.924-940 (2007) and Colwill, et al,
Nature Methods, vol. 8, p. 551-558 (2011)) and a person trained in the
art would be able to produce such antibodies using a phage display
library selection against the M1 antigen followed by screening to
determine a set of suitable antibodies for the detection of the M1
antigen.
Rizk Decl. ¶¶ 13, 17. Moreover, Bucher 1991 and Bucher 1989 demonstrate the
ability to obtain monoclonal antibodies to the M1 protein of the influenza A virus.
FF1, FF2, FF5. Thus, the evidence of record supports the conclusion that the
ordinary artisan would have had a reasonable expectation of success in obtaining
Appeal 2021-001912
Application 14/917,790

14
and performing the immunoassay that uses monoclonal antibodies that bind the
claimed sequences.
We note Dr. Rizk’s statement that “[i]t is most unexpected that M1 or a
specific region thereof would be excellent at detecting influenza A, wherein
traditionally an anti-NP antibody has been used.” Rizk Dec. ¶¶ 7, 15 (“The novelty
and unexpected nature of the claimed invention lies in the unexpected fact that two
antibodies specific for the C terminus portion of Ml protein provides superior
detection of influenza A.”). We do not find Dr. Rizk’s testimony persuasive of
unexpected results because Bucher 1991 provides an expectation that the M1
protein would be an excellent target for detecting influenza. FF4. Moreover, the
current record does not compare detection using the claimed method to the closest
prior art (such as, Bucher 1991’s teaching of detection using monoclonal antibody
1G11-D11 as a capture antibody and 2BB10-G9-europium as the detection
antibody). FF2; In re Baxter Travenol Labs, 952 F.2d 388, 392 (Fed. Cir. 1991)
(“[W]hen unexpected results are used as evidence of nonobviousness, the results
must be shown to be unexpected compared with the closest prior art.”).
We recognize some tension between our finding that the claimed sequences
are not supported by the Specification and our finding that the claimed sequences
would have been obvious over the prior art. In this regard, we note that the Federal
Circuit has explained that a description that renders the claimed subject matter
obvious may not provide written description support. Ariad Pharms., 598 F.3d at
1352 (“[W]hile the description requirement does not demand any particular form
of disclosure, or that the specification recite the claimed invention in haec verba, a
Appeal 2021-001912
Application 14/917,790

15
description that merely renders the invention obvious does not satisfy the
requirement.”).

CONCLUSION
Accordingly, we find that the method recited in claim 1 would have been
obvious over Bucher 1989 and Bucher 1991. Although we decline to reject claims
2, 4, 5, 10, 11, 22, and 23 pursuant to our discretionary authority under 37 C.F.R.
§ 41.50(b), we emphasize that our decision does not mean that the remaining
claims are necessarily patentable. Rather, we merely leave the patentability
determination of these claims to the Examiner. See MPEP § 1213.02.

DECISION SUMMARY
In summary:

Claims
Rejected
35 U.S.C. §  Basis/Reference(s)_ Affirmed Reversed New
Ground
1, 2, 4, 5,
10, 11, 22,
23
112  Written Description 1, 2, 4, 5,
10, 11,
22, 23

1 103(a) Bucher 1989, Bucher
1991
1
Overall
Outcome
1, 2, 4, 5,
10, 11,
22, 23
1

This decision contains a new ground of rejection pursuant to 37 C.F.R.
§ 41.50(b). Section 41.50(b) provides “[a] new ground of rejection pursuant to this
paragraph shall not be considered final for judicial review.” Section 41.50(b) also
provides:
Appeal 2021-001912
Application 14/917,790

16
When the Board enters such a non-final decision, the appellant,
within two months from the date of the decision, must exercise one of
the following two options with respect to the new ground of rejection
to avoid termination of the appeal as to the rejected claims:

(1) Reopen prosecution. Submit an appropriate amendment of
the claims so rejected or new Evidence relating to the claims
so rejected, or both, and have the matter reconsidered by the
examiner, in which event the prosecution will be remanded
to the examiner. The new ground of rejection is binding
upon the examiner unless an amendment or new…

Evidence not previously of Record is made which, in the
opinion of the examiner, overcomes the new ground of rejection
designated in the decision. Should the examiner reject the
claims, appellant may again appeal to the Board pursuant to this
subpart.

(2) Request rehearing. Request that the proceeding be reheard
under § 41.52 by the Board upon the same Record. The request
for rehearing must address any new ground of rejection and
state with particularity the points believed to have been
misapprehended or overlooked in entering the new ground of
rejection and also state all other grounds upon which rehearing
is sought.

Further guidance on responding to a new ground of rejection can be found in
the Manual of Patent Examining Procedure § 1214.01.

AFFIRMED; 37 C.F.R. § 41.50(b)