Ex Parte Mezo et al

Board of Patent Appeals and Interferences

Jun 30, 2011

11676148 (B.P.A.I. Jun. 30, 2011)

UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte ADAM R. MEZO, KEVIN A. McDONNELL,
CRISTINA A. TAN HEHIR, and ALFREDO CASTRO
__________

Appeal 2011-000031
Application 11/676,148
Technology Center 1600
__________

Before DONALD E. ADAMS, ERIC GRIMES, and MELANIE L.
McCOLLUM, Administrative Patent Judges.

GRIMES, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to peptides
that inhibit antibody binding to human neonatal Fc receptor (human FcRn).
The Examiner has rejected the claims as nonenabled and lacking adequate
written description in the Specification. We have jurisdiction under 35
U.S.C. § 6(b). We reverse.
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STATEMENT OF THE CASE
The Specification discloses that “FcRn binds to the constant region of
IgG, known as Fc . . . [and] functions in adults to protect IgG from
degradation” (Spec. 3), and that “agents that block or antagonize the binding
of IgG to FcRn may be used in methods of regulating, treating or preventing
disorders involving immune reactions, such as, e.g., autoimmune and
inflammatory diseases” (id. at 5).
Claims 1-3, 5, 6, 9, 13-15, 17-19, 25, 28, 30-35, 40, 41, 43-48, and 53-
57 are on appeal. Claim 1 is representative and reads as follows:
1. A peptide capable of inhibiting the binding of the Fc portion of a
human immunoglobulin (IgG) to human Fc neonatal receptor (FcRn),
comprising the sequence:
-Gly-X6-X7-X8-X9-X10-X11-
wherein:
- X6 is chosen from positively charged amino acids, aromatic amino
acids, positively charged aromatic amino acids, and analogs thereof;
- X7 is chosen from phenylalanine and phenylalanine analogs,
- X8 and X9 are each independently chosen from glycine, sarcosine,
aspartic acid, D-amino acids, α-aminoisobutyric acid, and analogs thereof, or
X8 when taken together with X9, forms a dipeptide mimetic;
- X10 is chosen from amino acids and analogs thereof, or X10, when
taken together with X9, forms a dipeptide mimetic;
- X11 is chosen from tyrosine and tyrosine analogs; and
wherein the peptide ranges from 7 to 50 amino acids in length, and the
peptide inhibits the binding of human FcRn to human IgG.

The Examiner has rejected all of the claims on appeal under 35 U.S.C.
§ 112, first paragraph, for lack of enablement (Answer 3-8) and lack of
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adequate written description (Answer 8-13). Both rejections rely on the
same interpretation of the claims.
The Examiner finds that the “specification defines amino acid analog
thereof e.g., twenty encoded amino acids, including non-encoded amino
acids and peptides, any amino acids, or any small molecule mimetic of any
amino acid, see page 15-16, paragraph 0049, in particular” (Answer 5). The
Examiner also finds that the “terms ‘e.g.,’, ‘includes’, ‘for example’ are
open-ended and not limiting to such disclosed residues. As such, the analog
thereof as specified in X6-X7-X8-X9-X10-X11 of the core sequence -Gly-X6-
X7-X8-X9-X10-X11- of claim 1 are not limited to the ones disclosed in the
specification” (id. at 6).
The Examiner concludes that the “claims encompass innumerous [sic]
peptide analog[s] ranging from 7 to 50 amino acids in length . . . wherein the
core sequence -Gly-X6-X7-X8-X9-X10-X11- has no resemblance to core
sequence GHFGGXY (SEQ ID NO: 14)” (id. at 4). See also Office action
mailed May 28, 2009, page 9 (“Given the open-ended definition of such
amino acid analog, dipeptide mimetic, tyrosine analogs, phenylalanine
analog . . . , the claimed peptide has no resemblance to the core peptide of
SEQ ID NO: 14”).
The Examiner rejected the claims as nonenabled because
“[e]nablement is not commensurate in scope with how to make and use any
peptide analog ranging from 7 to 50 amino acids in length wherein the core
sequence -Gly-X6-X7-X8-X9-X10-X11- has no resemblance to core consensus
sequence GHFGGXY” (Answer 4). Similarly, the Examiner rejected the
claims for lack of adequate written description because “[a]t the time of
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filing, applicants are [sic] not in possession of any peptide analog rang[ing]
from 7 to 50 amino acids in length comprising any core sequence that has no
resemblance to the consensus sequence GHFGGXY of SEQ ID NO: 14” (id.
at 9).
Appellants contend that the
inventors discovered that “[p]eptides that demonstrate the
ability to bind FcRn and/or block the binding of FcRn to the Fc
portion of IgG share certain commonalities or features.”
Specification at [0073]. In particular, those peptide each have a
binding sequence for FcRn binding that is derived from, and
closely related to, a short consensus motif identified through
phage display experiments. Specification at Example 3 and
[00204].
(Appeal Br. 7.)
Appellants argue that the “specification provides ample direction or
guidance to enable practice of the full scope of the invention, including
structure and biological activity data for approximately three hundred
peptides” (id. at 16). Appellants argue that the “structure/function data for
almost 300 peptides provides the skilled artisan with a clear picture of how
to practice the claimed invention by identifying which substitutions work
well and which do not” (id. at 21). Appellants provide an exhibit
summarizing the exemplified peptides and their binding properties (Appeal
Br. 23 n.2, 51-66).
With regard to the written description rejection, Appellants argue that
the
specification does disclose structural features shared by
peptides and modified peptides of the claimed genus. These
features are set forth in the formulas in claims 1 and 2 and each
variable is carefully defined throughout the specification in
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such a way as to allow one of skill in the art to recognize the
identity of the members of the claimed genus. Moreover, the
specification describes the complete structure of nearly 300
modified peptides representative of the claimed genus.
(Id. at 45.)
We will reverse both of the rejections on appeal. The Examiner’s
rejections are based on an interpretation of the claims as encompassing
peptides that have “no resemblance to core sequence GHFGGXY” (Answer
4). As we understand it, the Examiner’s reasoning is that the claims
encompass “analogs” at each of the X6 through X11 positions and the
Specification’s definition of analogs is open-ended; therefore, the peptide
defined by the formula in claim 1 can have “any amino acids, or any small
molecule mimetic of any amino acid” (Answer 5) at each of the X6 through
X11 positions, resulting in peptides that have “no resemblance to core
sequence GHFGGXY” (id. at 4; see also id. at 9 (same claim interpretation
relied on in the description rejection)).
“[D]uring examination proceedings, claims are given their broadest
reasonable interpretation consistent with the specification.” In re Hyatt, 211
F.3d 1367, 1372 (Fed. Cir. 2000). That interpretation “applies to the
verbiage of the proposed claims the broadest reasonable meaning of the
words in their ordinary usage as they would be understood by one of
ordinary skill in the art, taking into account whatever enlightenment . . . may
be afforded by the written description contained in the applicant’s
specification.” In re Morris, 127 F.3d 1048, 1054 (Fed. Cir. 1997).
Here, the Specification does not define an analog of an amino acid as
any of the “twenty encoded amino acids, including non-encoded amino acids
and peptides, any amino acids, or any small molecule mimetic of any amino
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acid,” as the Examiner interpreted it (Answer 5). The Specification states
that “[a]n ‘amino acid analog’ is an amino acid, or a small molecule mimetic
of an amino acid, that shares a common chemical, charge, steric, or other
property of a given amino acid” (Spec. 16-17, ¶ 49).
Reading the claim language as it would be understood by one of
ordinary skill in the art, the Specification’s definition of an “analog” of a
given amino acid means a molecule that shares the chemical properties that
are specific to that amino acid, rather than the properties of amino acids in
general. This interpretation is consistent with the specific examples of
analogs that are provided in the Specification. (See Spec. 17: “For example,
analogs of alanine include, e.g., β-alanine, ethylglycine, α-aminoisobutyric
acid, and D-alanine; analogs of cysteine include, e.g., homocysteine, D-
cysteine, and penicillamine;” etc.).
Giving the verbiage of the claims its broadest reasonable
interpretation also requires interpreting, for example, the claim terms
“phenylalanine analogs” and “tyrosine analogs” to mean different things, so
as to give meaning to those claim terms. The Examiner’s interpretation –
that an “analog” of a specific amino acid can be any amino acid or any small
molecule mimetic of any amino acid – is unreasonably broad because it
gives the same scope to, among other terms, “phenylalanine analogs” and
“tyrosine analogs.” The Examiner’s interpretation would therefore read out
of the claim the word “phenylalanine” in “phenylalanine analogs” and the
word “tyrosine” in “tyrosine analogs.” Cf. Texas Instruments, Inc. v. United
States Int’l Trade Comm., 988 F.2d 1165, 1171 (Fed. Cir. 1993) (“[T]o
construe the claims in the manner suggested by TI would read an express
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limitation out of the claims. This we will not do.”). As discussed above, the
proper interpretation requires that “phenylalanine analogs” share properties
in common with phenylalanine, while “tyrosine analogs” share properties in
common with tyrosine, and thus gives meaning to all of the terms of the
claim.
We agree with Appellants that the claims, properly interpreted, are
supported by a disclosure that provides an adequate written description and
enables practice of the full scope of the claimed invention without undue
experimentation.
SUMMARY
We reverse both of the rejections on appeal.

REVERSED

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