Ex Parte Pfizenmaier et al

Board of Patent Appeals and Interferences

Mar 22, 2010

10389223 (B.P.A.I. Mar. 22, 2010)

UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte KLAUS PFIZENMAIER, HARALD WAJANT,
DIETER MOOSMAYER, and THOMAS WUEST
__________

Appeal 2009-009661
Application 10/389,223
Technology Center 1600
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Decided: March 22, 2010
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Before LORA M. GREEN, JEFFREY N. FREDMAN, and
STEPHEN WALSH, Administrative Patent Judges.

WALSH, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134(a) involving claims to a
polypeptide and a composition comprising the polypeptide. The Patent
Examiner rejected the claims as anticipated. We have jurisdiction under
35 U.S.C. § 6(b). We affirm.
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STATEMENT OF THE CASE
Claims 1, 3, 5, 7, 9, 16 and 19 are on appeal.1 Claim 1 is
representative and reads as follows:
1. A polypeptide comprising:
(i) a segment (1) comprising the extracellular domain of FasL;
(ii) a segment (2) comprising a non-multimerizing peptide linker
that is linked to the N-terminus of segment (1); and
(iii) a segment (3) comprising a single chain antibody that
selectively recognizes a specific target molecule on a cell
surface,
said segment (3) being linked to the N-terminus of segment (2),
wherein the FasL extracellular domain causes formation of a trimer,
wherein the trimer of the extracellular domain alone has no or limited
biological activity,
wherein the biological activity of the extracellular domain trimer is
activated upon the binding of the segment (3) portion of the
polypeptide to the target molecule on the cell surface, and
wherein the biological activity comprises the ability to induce
apoptosis.

The Examiner rejected claims2 1, 3, 5, 7, 9, 16 and 19 under 35 U.S.C.
§ 102(e) as anticipated by Queen.3
Claims 3, 5, 7, 9, 16 and 19 have not been argued separately and
therefore stand or fall with claim 1. 37 C.F.R. § 41.37(c)(1)(vii).

1 Claims 2, 6, 8, 10, 24 and 25 were cancelled, and claims 4, 11-15, 17, 18
and 20-23 were withdrawn. (App. Br. 4.)
2 Although the Examiner’s Answer states that “claims 1-10, 16 and 18-19”
are rejected, the inclusion of claims 2, 6, 8, 10 and 18 appears to be a typo.
The Examiner agreed (Ans. 2) with Appellant’s Brief that claims 2, 6, 8 10
were cancelled, and that claim 18 was withdrawn.
3 US Patent No. 6,046,310, issued to Cary L. Queen, Apr. 4, 2000.
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ANTICIPATION
The Issue
The Examiner’s position is that Queen taught “Fas ligand (FasL)
fusion proteins wherein FasL is linked to an antibody that binds a cell
surface marker, including a cytokine receptor, wherein the antibody may be
a single chain antibody (scFv) and Queen et al also teach the use of short
peptide linkers (i.e., non-multimerizing) to link the C-terminus of the single
chain antibody to the N-terminus of FasL.” (Ans. 3-4.)
Appellants contend that the principles of “selection invention” apply,
and the rejection is improper for the following three reasons:
1) the claimed fusion polypeptide is not sufficiently
delineated by Queen in a succinct, cohesive disclosure;
2) the 670,462 possible fusion proteins disclosed by
Queen are not sufficiently limited in number; and
3) the structure and mechanism of action of the fusion
polypeptide cohesively disclosed in Queen differs from the
claimed invention.

App. Br. 12.
The issue with respect to this appeal is whether Queen described the
claimed fusion polypeptide.

Findings of Fact
1. The Examiner found that Queen taught “the Ig-FasL polypeptide
comprises the extracellular domain FasL amino acids that are identical
to the FasL extracellular domain of SEQ ID NO:14 presently
claimed.” (Ans. 4.)
2. The Examiner found that Queen taught that “the Ig-FasL fusion has
reduced ability to apoptose target cells alone because within the fusion
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protein the FasL moiety forms monomers or dimers and not trimers.”
(Id.)
3. Queen’s Example 1 described cloning FasL cDNA. (Queen, col. 12,
ll. 39-51.)
4. Queen’s Example 2 described construction of an Ig-FasL expression
vector coding for a polypeptide having an Ig heavy chain attached via
a peptide linker of 34 or 5 FasL amino acids to the 145 C-terminal
extracellular residues of human FasL. (Id. at col. 13, ll. 52-61.)
5. Queen’s Example 5 described expression of an Ig-FasL polypeptide.
(Id. at col. 14, ll. 21-43.)
6. Queen’s Example 4 described additional Ig-FasL fusion polypeptides,
all having the same native extracellular human FasL domain described
in Examples 1 through 3. (Id. at col. 14, l. 45 - col. 15, l. 24.)
7. Queen’s Examples 5 and 6 described expression of HuABL364 Ig-
FasL polypeptide, which had the same native extracellular human
FasL domain. (Id. at col. 15, l. 25 – col. 16, l. 54.)
8. According to Queen’s Example 6, apoptotic activity of the
HuABL364 Ig-FasL polypeptide was likely due to oligomerization
because the polypeptide aggregated as shown by gel filtration. (Id. at
col. 16, ll. 46-54.)
9. Queen’s Example 7 described Ig-FasL mutant polypeptides, in which
the wild type FasL fragment was replaced with mutants. (Id. at col.
16, ll. 55-67.)
10. Queen’s Example 7 reported the apoptotic activity of the Ig-FasL
fusion polypeptide having the wild type human sequence, and
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contrasted the wild type sequence activity to fusion polypeptides
having mutant FasL domains. (Id. at Table 3, col. 18, ll. 4-20.)
11. According to Queen, the comparative data in Table 3 showed that the
mutants of Queen’s invention “offer numerous advantages over other
treatments for autoimmune disease or cancer.” (Id. at col. 18, ll. 21-
25.)
12. In an embodiment of Queen’s invention, the antibody may be a single-
chain antibody. (Id. at col. 4, ll. 61-66.)
12. Appellants’ Specification states: “preferred for segment (3) of a
polypeptide according to the present invention are antibody fragments
in various antibody forms, e.g., scFv, Fab or complete
immunoglobulin.” (Spec. 7:5-6.)
13. Appellants’ Specification states: “a preferred polypeptide . . .
(segment(3)) N-terminally a murine, humanized or human single
chain antibody fragment (scFv) consisting of VH-peptide-linker-VL . .
. .” (Id. at 7:8-12.)

Principles of Law
To anticipate a claim, a prior art reference must disclose every
limitation of the claimed invention, either explicitly or
inherently. Anticipation is an issue of fact, and the question
whether a claim limitation is inherent in a prior art reference is
a factual issue.

In re Schreiber, 128 F.3d 1473, 1477 (Fed. Cir. 1997) (citations omitted).
“Absent claim language carrying a narrow meaning, the PTO should only
limit the claim based on the specification or prosecution history when those
sources expressly disclaim the broader definition.” In re Bigio, 381 F.3d
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1320, 1325 (Fed. Cir. 2004). “A reference is no less anticipatory if, after
disclosing the invention, the reference then disparages it. Thus, the question
whether a reference ‘teaches away’ from the invention is inapplicable to an
anticipation analysis.” Celeritas Technologies, Ltd. v. Rockwell Intern.
Corp., 150 F.3d 1354, 1361 (Fed. Cir. 1998). “[I]f granting patent
protection on the disputed claim would allow the patentee to exclude the
public from practicing the prior art, then that claim is anticipated.” Schering
Corp. v. Geneva Pharmaceuticals, Inc., 339 F.3d 1373, 1379 (Fed. Cir.
2003) (quotation omitted).

Analysis
The Examiner found that Queen described a fusion polypeptide
comprising the same FasL extracellular domain that is segment (1) in
Appellants’ claim 1. The evidence supports that finding. (FF1 and 3.) The
Examiner also found that Queen taught that a single chain antibody may be
used in an embodiment of Queen’s invention. The evidence supports that
separate finding. (FF12.) However, Queen described its invention as fusion
polypeptides built with a mutated FasL extracellular domain, not with the
wild type domain. Queen distinguished fusion polypeptides made with the
wild type domain from the fusion polypeptides of its invention. (FF10.)
Thus, when Queen explicitly stated that single chain antibody may be used
in an embodiment of its invention, it was describing a fusion protein made
with single chain antibody and a mutated FasL extracellular domain. As the
Examiner acknowledged, Queen’s mutated FasL domains were explicitly
described as not forming trimers, in contrast to Appellants’ claim 1. Taken
in context, we do not agree that Queen’s mention of single chain antibodies
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referred to fusion polypeptides of the kind that Appellants claim, because it
was intended to be applied to polypeptides of Queen’s invention, i.e., FasL
fusion polypeptides that do not trimerize.
The Examiner has also referred to the entire Queen document. We
find that Queen’s Examples 1-6 explicitly describe a three-part fusion
polypeptide comprising an antibody chain, a linker, and a wild type FasL
extracellular domain. (FF3-8.) Queen’s Example 7 contrasts the activity of
the wild-type fusion polypeptide with the mutated versions of Queen’s
invention. (FF9-11.)
Queen’s working examples are a succinct, cohesive disclosure of a
wild type fusion polypeptide. Appellants’ argument to the contrary is
unpersuasive because it ignores Queen’s working examples. Similarly,
Appellants’ argument about the many possible embodiments of Queen’s
invention is unpersuasive because it ignores the disclosure of the wild type
fusion polypeptide described, made and used for comparison testing in
Queen’s working examples.
We next consider Appellants’ third argument, that “the structure and
mechanism of action of the fusion polypeptide cohesively disclosed in
Queen differs from the claimed invention.” (App. Br. 12.) Queen’s fusion
polypeptide has three parts: an antibody chain, a linker, and the extracellular
domain of FasL.
The Specification discloses that antibody fragments are preferred for
segment (3). (FF12.) The Specification also discloses that a preferred
antibody consists of VH-peptide-linker-VL. (FF13.) However, we find no
explicit definition of the claim term “single chain antibody” that would
structurally distinguish Queen’s fusion polypeptide comprising a single
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chain antibody from the polypeptide of claim 1. The Pfizenmaier
Declaration describes the claimed fusion polypeptide as containing “a single
chain antibody fragment (Constructs (D), (E) and (F), page 14-15 of
specification).” (Decl. ¶5.) The Declaration Exhibits A, B, and C are said to
show the structure and mechanism of the preferred VH-peptide-linker-VL.
Claim 1, however, is not limited to the preferred structures described at
Specification pages 14-15, and in the Declaration. We are not persuaded
that Queen’s fusion polypeptide is structurally different from claim 1’s
polypeptide.
Mechanistically, claim 1’s segment (2) linker is “non-multimerizing.”
Queen described its corresponding linker as 34 amino acids, or alternatively
five amino acids, from FasL. (FF4.) There is no evidence, and Appellants
do not allege, that Queen’s 34 amino acid linker or five amino acid linker
forms multimers. As claimed, the FasL extracellular domain causes
formation of a trimer. Queen’s wild type FasL extracellular domain causes
formation of a trimer, because it is the same FasL extracellular domain that
Appellants use for segment (1). We are therefore not persuaded that the
polypeptide of claim 1 has a different mechanism of action from the
polypeptide Queen described in detail at Examples 1-6. Referring to
Queen’s disclosure at cols. 5-6, Appellants argue that Queen’s molecules
first form a trimer, and then the trimers double-up to form a hexamer. (App.
Br. 20-21.) Because Appellants are referring to the polypeptides containing
mutant FasL domains, it is not clear that the argument applies to Queen’s
wild type FasL polypeptide of Examples 1-6. However, even if the wild
type fusion polypeptide goes on to form a hexamer after forming a trimer,
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that subsequent event would not distinguish claim 1, which as written, does
not exclude subsequent mechanisms occurring after trimer formation.
Put another way, Queen anticipated claim 1 because claim 1 would
block the public from making the wild type FasL fusion polypeptide that
Queen described in its working examples. See, e.g., Schering, 339 F.3d at
1379.
CONCLUSION
Queen described the claimed polypeptide and therefore anticipated
claim 1.
SUMMARY
We affirm the rejection of claims 1, 3, 5, 7, 9, 16 and 19 under
35 U.S.C. § 102(e) as anticipated by Queen.
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).

AFFIRMED

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