Ex Parte Van Venrooij et al

Patent Trial and Appeal Board

Nov 7, 2013

11834557 (P.T.A.B. Nov. 7, 2013)

UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
__________

Ex parte WALTHERUS JACOBUS WILHELMUS VAN VENROOIJ,
GERARDUS ANTONIUS SCHELLEKENS,
JOZEF MARIA HENDRIK RAATS, and
RENE MICHAEL ANTONIUS HOET
__________

Appeal 2012-004620
Application 11/834,557
Technology Center 1600
__________

Before DEMETRA J. MILLS, ERIC GRIMES, and
JEFFREY N. FREDMAN, Administrative Patent Judges.

FREDMAN, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal1 under 35 U.S.C. § 134 involving claims to a peptide
and a method of detecting rheumatoid arthritis. The Examiner rejected the
claims as failing to satisfy the written description requirement and as
anticipated. We have jurisdiction under 35 U.S.C. § 6(b). We reverse.

1 Appellants identify the Real Parties in Interest as Stichting Voor
De Technische Wetenschappen, Axis Shield, and Euro-
Diagnostica. (see App. Br. 2).
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Statement of the Case
Background
“The present invention relates to a peptide derived from an antigen
recognized by autoantibodies from patients with rheumatoid arthritis, which
peptide is reactive with autoimmune antibodies from a patient suffering from
rheumatoid arthritis” (Spec. 1, ll. 1-5).
The Claims
Claims 23-35 are on appeal. Independent claim 23 is representative
and reads as follows:
23. A synthetic peptide which comprises an amino acid
sequence that is the same as that of a fragment having no
more than 19 amino acids of the amino acid sequence of
SEQ ID NO: 17 and having sufficient length to act as an
epitope for antibody binding, except that said peptide has at
least one arginine residue of SEQ ID NO: 17 replaced by a
citrulline residue,
which peptide is specifically immunoreactive with
anti-filaggrin antibodies present in the serum of subjects
suffering from rheumatoid arthritis.

The issues
A. The Examiner rejected claims 23-35 under 35 U.S.C. § 112, first
paragraph, written description (Ans. 4-7).
B. The Examiner rejected claims 23-35 under 35 U.S.C. § 102(b) as
anticipated by Van Venrooij2 (Ans. 7).

2 Van Venrooij et al., US 6,858,438 B2, issued Feb. 22, 2005.
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A. 35 U.S.C. § 112, first paragraph, written description
The Examiner finds that the “specification as filed did not disclose a
composition consisting of the protein of SEQ ID NO:17, nor the claimed
citrullinated fragments thereof” (Ans. 5). The Examiner finds that Gan,
which was cited in the Specification as disclosing “known cDNA sequences
of human profilaggrin” (Spec. 5), was not “incorporated by reference.
Further, a review of the reference does not disclose the amino acid sequence
of SEQ ID NO:17 therein. The closest sequence in the reference to that of
SEQ ID NO:17 is a consensus sequence of a 324 amino acid repeat that is
found in human filaggrin” (Ans. 5). The Examiner finds that the
“specification does not provide support for the various length filaggrin
peptides of the instant claims” (Ans. 5).
The issue with respect to this rejection is: Does the evidence of record
support the Examiner’s conclusion that the Specification fails to provide
descriptive support for the claimed synthetic peptides?
Findings of Fact
1. The Specification teaches “[p]eptides were selected for
synthesis on the basis of amino acid sequences derived from known cDNA
sequences of human profilaggrin (Ref. 2; Ref. 3)” (Spec. 5, ll. 11-13).
2. The Specification teaches that “Ref. 3” is a paper by Gan et al.,
Organization, structure, and polymorphisms of the human profilaggrin gene,
29 BIOCHEMISTRY 9432-9440 (1990) (Spec. 12, ll. 17-20).
3. The Specification teaches that “the peptide is characterized in
that the modified arginine residue's side chain is a side chain according to
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Formula I . . . and the modified arginine residue is in particular a citrulline
residue” (Spec. 2, ll. 10-18).
4. The Specification teaches that it “is also possible to shorten the
peptides by one or more amino acids, provided this does not have a
significantly adverse effect on the reactivity” (Spec. 4, l. 17 to 5, l. 1).
5. Table 1 of the Specification is reproduced below:

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Principles of Law
Falko-Gunter teaches that “we hold that where, as in this case,
accessible literature sources clearly provided, as of the relevant date, genes
and their nucleotide sequences (here ‘essential genes'), satisfaction of the
written description requirement does not require either the recitation or
incorporation by reference (where permitted) of such genes and sequences.”
Falko-Gunter Falkner v. Inglis, 448 F.3d 1357, 1368 (Fed. Cir. 2006).
“[T]he determination of what is needed to support generic claims to
biological subject matter depends on a variety of factors, such as the existing
knowledge in the particular field, the extent and content of the prior art, the
maturity of the science or technology, the predictability of the aspect at
issue, and other considerations appropriate to the subject matter.” Capon v.
Eshhar, 418 F.3d 1349, 1359 (Fed. Cir. 2005).
“[A]pplicants have some flexibility in the ‘mode selected for
compliance’ with the written description requirement,” but a specification
must “set forth enough detail to allow a person of ordinary skill in the art …
to recognize that the inventor invented what is claimed.” University of
Rochester v. G.D. Searle & Co., Inc., 358 F.3d 916, 928 (Fed. Cir. 2004).
Analysis
Claim 23 requires that the synthetic peptides are 19 amino acids or
shorter from the profilaggrin sequence, but which retain immunoreactivity
with anti-filaggrin antibodies in rheumatoid arthritis patients.
Consistent with Falko-Gunter, Appellants have demonstrated that an
accessible literature source, Gan, cited by the Specification describes the
profilaggrin sequence from which peptides are derived (FF 1-2). The
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Specification exemplifies thirteen different 19 amino acid peptides in Table
1 (FF 5) and expressly indicates that it is possible to shorten the peptides (FF
4).
We appreciate the Examiner's concern that “the claimed peptides and
methods are supported only by material that was improperly amended into
the specification and, thus, comprise the amending of new matter into the
claims” (Ans. 9), but conclude that no incorporation would have been
necessary to support the subject matter of the claims. Falko-Gunter holds
that written descriptive support does not require incorporation by reference,
so long as the compounds were known in the prior art. See Falko-Gunter
Falkner, 448 F.3d at 1368. Therefore, whether the incorporation by
reference is itself proper or not is irrelevant, since the claims may properly
be supported by the disclosure of the profilaggrin sequence in the prior art
(FF 2).
To the extent that the Examiner’s rejection is also based on the
absence of a representative number of species (see Ans. 6), we find that the
instant situation is very different than Rochester, where the claims were
drawn to unidentified, unknown inhibitor compounds, with no working
examples. As the Examiner recognizes, Appellants’ Specification provides a
number of different peptides of different lengths, from both the amino and
carboxy terminus of the profilaggrin protein (see Ans. 11; FF 5). Further, it
is also clear that Appellants’ invention is not intended to be the concept of
profilaggrin peptides, but rather their use in the detection of rheumatoid
arthritis, which is susceptible to routine screening for function.

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The instant situation is, therefore, much closer to that in Capon, where
the prior art provides the underlying information regarding the members of
the genus. As in Capon, there is no inventive contribution by Appellants
inherent in the profilaggrin sequence, but rather the asserted invention is the
novel use of such non-naturally occurring peptides, modified with citrulline,
as reagents for the detection of rheumatoid arthritis.
Conclusion of Law
The evidence of record does not support the Examiner’s conclusion
that the Specification fails to provide descriptive support for the claimed
synthetic peptides.
B. 35 U.S.C. § 102(b) over Van Venrooij
The Examiner finds that as “none of the priority documents disclose
the claimed protein fragments of SEQ ID NO:17, and the incorporation of
the amino acid sequence of SEQ ID NO:17 into the instant specification and
claims was improper, the benefit of priority is denied” (Ans. 7). The
Examiner finds that the “'438 patent teaches a peptide of the instant claims
(see particularly Table 1). The reference further teaches the methods of the
instant claims (See particularly, Materials and Methods, beginning at column
3, and Results, beginning at column 5)” (Ans. 7).
The instant application is a continuation of U.S. application
11/059,775 which is itself a continuation of U.S. application 09/308,150
which matured into U.S. patent 6,858,438, the reference at issue. Therefore,
the disclosure of the instant application is identical to that of U.S. patent
6,858,438.
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Since, as discussed above, we find that the instant application properly
has descriptive support for the claims, we also find that the instant
application receives benefit of priority to U.S. application 09/308,150.
Therefore, these applications share the same priority date and the patent was,
therefore, not patented or described in a printed publication prior to the date
of application for patent in the United States as required for a rejection under
35 U.S.C. § 102(a) or (b).
We, therefore, reverse the anticipation rejection.
SUMMARY
In summary, we reverse the rejection of claims 23-35 under 35 U.S.C.
§ 112, first paragraph, written description.
We reverse the rejection of claims 23-35 under 35 U.S.C. § 102(b) as
anticipated by Van Venrooij.

REVERSED
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