Ex Parte Fu

Board of Patent Appeals and Interferences

Apr 12, 2010

10865623 (B.P.A.I. Apr. 12, 2010)

UNITED STATES PATENT AND TRADEMARK OFFICE
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BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
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Ex parte YANG-XIN FU
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Appeal 2009-010614
Application 10/865,623
Technology Center 1600
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Decided: April 12, 2010
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Before TONI R. SCHEINER, RICHARD M. LEBOVITZ, 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 for a
method to induce T-cell anti-tumor activity. The Patent Examiner rejected
the claims for failure to comply with the written description requirement.
We have jurisdiction under 35 U.S.C. § 6(b). We reverse.
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Application 10/865,623

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STATEMENT OF THE CASE
According to the Specification, the LIGHT protein has a role in T cell
activation. (Spec. 2:[0009].) “Mutant LIGHT (LIGHTm) is generated to
prevent protease digestion so LIGHT can be expressed on tumor cells.” (Id.
at 3:[00012].) “Mutant light (designated LIGHTm), has the proteolytic site
EKLI from positions 79-82 deleted from the amino acid sequence of normal
LIGHT (FIG. 3A) (Tamada et al., 2000).”1 (Id. at 3:[00013].)
Claims 7-9 and 17 are on appeal. (App. Br. 2.)2 Claim 7 is
representative and reads as follows:
7. A protease resistant mutant LIGHT protein having the amino acid
sequence of LIGHT with a protease site between the transmembrane
domain and amino acid position 85 in the extracellular domain with a
deletion in the protease site, wherein the mutant LIGHT protein is
stably present on the surface of a tumor cell.

The Examiner rejected claims 7-9 and 17 under 35 U.S.C. § 112, first
paragraph, as failing to comply with the written description requirement.

WRITTEN DESCRIPTION
The Issue
The Examiner’s position is that the Specification “provides no
teaching on a mutant LIGHT protein as claimed including intracellular
(amino acid position 1-46), transmembrane (amino acid position 47-77), and
extracellular domain (amino acid position 78-240) with mutations or

1 Koji Tamada et al., Modulation of T-cell-mediated immunity in tumor and
graft-versus-host disease models through the LIGHT co-stimulatory
pathway, 6 NATURE MEDICINE 283-289 (2000).
2 Supplemental Appeal Brief dated Oct. 2, 2008.
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deletions at proteolytic site (amino acid position 79-82).” (Ans. 3.)
According to the Examiner, “[t]he scope of the claims includes a genus
having numerous structural variants.” (Id.) The Examiner finds the
disclosure “insufficient to describe the genus.” (Id. at 6.)
Appellant contends that the LIGHT protein’s amino acid and
nucleotide sequences were well known in the art before the Application was
filed. (App. Br. 11.) Appellant provides (1) a copy of a figure adapted from
Tamada with underlining showing the LIGHT transmembrane domain and
the protease site, and (2) a copy of Fig. 3A from the Application as filed,
said to show the relative locations of the transmembrane domain, the
extracellular domain and the protease site in the LIGHT protein. (Id. at 6.)
Appellant further argues that “[t]he fact that the generated mutant LIGHT
protein that has an inactivated protease site between the transmembrane
domain and position 85 of the LIGHT protein I stably present on the surface
of a tumor cell, demonstrates that if there are other protease sites, they are
not functionally relevant for the purpose of stimulating an immune response
within the tumor environment.” (Id. at 8.)
The issue with respect to this rejection is whether the evidence
supports a finding that a person of ordinary skill in the art would not credit
Applicant with possession of the proteins defined by claim 7.

Findings of Fact
1. Tamada disclosed the full length sequence of murine and human
LIGHT proteins. (Tamada 284, Fig. 1a.)
2. According to Tamada, the name LIGHT is “derived from:
homologous to lymphotoxins, shows inducible expression, and
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Application 10/865,623

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competes with herpes simplex virus glycoprotein D for herpes virus
entry mediator;” and LIGHT has “Genome Database designation,
TNFSF14.” (Tamada, 283, second paragraph.)
3. Appellant’s Fig. 3A shows a schematic representation of the LIGHT
protein, indicating where four amino acids were deleted. (Spec.
6:[00019].)
4. Appellant’s Fig. 9 “shows the nucleic acid sequence that encodes a
LIGHT protein. . . . the region encoding a proteoloytic site that has
been deleted in LIGHTm is underlined.” (Spec. 7:[00025].)
5. The record includes a Declaration of Yang-Xin Fu under 37 C.F.R.
§ 1.132.
6. Declarant Fu states: “[b]ased on the disclosure of a proteolytic site
EKLI at positions 79-82 in a murine LIGHT sequence in the patent
application, I identified a corresponding site EQLI at positions 81-84
near the transmembrane domain of the human LIGHT sequence by a
computer alignment of the murine and the human LIGHT sequences.”
(Decl. ¶ 5.)
7. Declarant Fu states: “based on the disclosure of a proteolytic site in
murine LIGHT sequence and following methods disclosed in the
present patent application, I was able to obtain a protease resistant
mutant human LIGHT sequence.” (Id. at ¶ 7.)

Principles of Law
“[W]here . . . accessible literature sources clearly provided, as of the
relevant date, genes and their nucleotide sequences . . . satisfaction of the
written description requirement does not require either the recitation of …
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such genes and sequences.” Falko-Gunter Falkner v. Inglis, 448 F.3d 1357,
1363 (Fed. Cir. 2006). “It is not necessary that every permutation within a
generally operable invention be effective in order for an inventor to obtain a
generic claim, provided that the effect is sufficiently demonstrated to
characterize a generic invention.” Capon v. Eshhar, 418 F.3d 1349, 1359
(Fed. Cir. 2005).

Analysis
The LIGHT protein was known in the art before Appellant filed the
Application. (FF1, 2.) In the Specification, Appellant disclosed a protease
site said to have been unrecognized in the art. Appellant claims to have
discovered that when the protease site is mutated by deletion, the mutant
LIGHT protein will have a stable presence on the surface of a tumor cell.
The protease site is described as the four amino acid sequence EKLI in the
murine sequence at about position 85. Declarant Fu states that there is a
similar site in the human sequence. (FF6.)
The Examiner finds no description of a “genus,” which the Examiner
says has “numerous structural variants.” The claim is directed to “a protease
resistant mutant LIGHT protein with . . . a deletion in the protease site.” We
agree the claim is generic. However, we do not see evidence that a person of
skill in the art would find the Specification’s description of the genus of
deletion mutants within a four amino acid subsequence to be inadequate for
the purpose of describing the invention defined in claim 7.
In Amgen Inc. v. Hoechst Marion Roussel, Inc., 314 F.3d 1313, 1332
(Fed.Cir.2003) the court explained that the written description requirement
may be satisfied “if in the knowledge of the art the disclosed function is
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sufficiently correlated to a particular, known structure.” We find that
Appellant’s Specification establishes a correlation between deletions in the
LIGHT protease site and the stable presence of protease resistant LIGHT on
the surface of a tumor cell. Accordingly, we agree with Appellant that the
evidence supports finding that a person of ordinary skill in the art would
credit Appellant with possession of the mutant LIGHT protein defined in
claim 7.

CONCLUSION
The evidence of record supports finding that a person of ordinary skill
in the art would credit Applicant with possession of the protein defined by
claim 7.

SUMMARY
We reverse the rejection of claims 7-9 and 17 under 35 U.S.C. § 112,
first paragraph, as failing to comply with the written description
requirement.

REVERSED

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