Ex Parte Hsu

Patent Trial and Appeal Board

Dec 19, 2016

13387931 (P.T.A.B. Dec. 19, 2016)

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.
13/387,931 03/02/2012 Sheau Yu Hsu STAN-681 5724
77974 7590 12/21/2016
Stanford University Office of Technology Licensing
Bozicevic, Field & Francis LLP
201 REDWOOD SHORES
SUITE 200
REDWOOD CITY, CA 94065
EXAMINER
LEE, JIA-HAI
ART UNIT PAPER NUMBER
1676
NOTIFICATION DATE DELIVERY MODE
12/21/2016 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):
docket@bozpat.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte SHEAU YU HSU1
Appeal 2015-000612
Application 13/387,931
Technology Center 1600
Before MELANIE L. MCCOLLUM, RICHARD J. SMITH, and TIMOTHY
G. MAJORS, Administrative Patent Judges.
SMITH, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35U.S.C. § 134 involving claims to an
isolated polypeptide. We have jurisdiction under 35 U.S.C. § 6(b).
We affirm.
STATEMENT OF THE CASE
Background
“The invention provides polypeptides referred to herein as GIP55S or
GIP55G . . . The peptides are shown herein to be biologically active,
including effects on cells in the gastrointestinal tract.” (Spec. 140.)
1 According to Appellant, the real party in interest is the Board of Trustees
of the Leland Stanford Junior University. (Appeal Br. 2.)
Appeal 2015-000612
Application 13/387,931
Claims on Appeal
Claims 1 and 2 are on appeal.2 (Claims Appendix, Appeal Br. 7.)
Claims 1 and 2 read as follows:
1. An isolated polypeptide consisting essentially of the amino
acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO:2.
2. An isolated polypeptide consisting of the amino acid
sequence set forth in SEQ ID NO: 1.
Examiner’s Rejections
1. Claims 1 and 2 stand rejected under 35 U.S.C. § 101 as directed to
non-statutory subject matter of natural products, as evidenced by Chang.3
(Ans. 6—7.)4
2. Claims 1 and 2 stand rejection under 35 U.S.C. § 102(b) as anticipated
by Alsobrook,5 as evidenced by Chang. (Id. at 2—3.)
3. Claims 1 and 2 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over Alsobrook and Kozian.6 (Id. at 4—5.)
2 Claims 3, 4, 6, and 9-16 are cancelled and claims 5, 7, and 8 are
withdrawn. (See Amendment dated July 7, 2014.)
3 Chang et al., Adaptive selection of an incretin gene in Eurasian
populations, Genome Research 21, 21—32 (2011) (“Chang”). Chang is a
post-filing publication of “the work by Appellants.” (Appeal Br. 4.)
4 This is a new ground of rejection in the Answer that Appellant responds to
in the Reply Brief dated Oct. 10, 2014.
5 Alsobrook, II et al., US 2004/0002453 Al, published Jan. 1, 2004
(“Alsobrook”).
6 Kozian et al., WO 2006/119905 Al, published Nov. 16, 2006 (“Kozian”).
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Application 13/387,931
FINDINGS OF FACT
The following findings are included for emphasis and reference
convenience.
FF 1. The Specification states that “[gjastric inhibitory polypeptide (GIP)
. . . circulates as a biologically active 42-amino acid peptide.” (Spec. 131.)
FF 2. The Specification states that “[hjuman GIP alleles encode an extended
peptide, referred to herein as GIP55S or GIP55G.” (Spec. 1 8.)
FF 3. The Specification states “[t]he GIP propeptide is 57 amino acids in
length, which is processed to a mature peptide of 42 amino acids in length.
GIP55S and GIP55G are 55 amino acids in length and are active forms
without further processing.” (Spec. 141.) The Specification illustrates this
as follows:
, GIP55G and GIP55S1 55
YAEGTFiSDYSIAMDKIHQQDFVNWLLAGKGKKNDWKHNITQREARALELASQAN
“O' G
Posttranslational processing
55-amino-acid<--------------- ---------------- ►
RXXR RK
V VV
s N-propeptide GIP C-propeptide
RXXR RXXR
<------------------------>
A 42-amino-acid A
Posttranslationa! processing
1 "O' 42
YAEGTFiSDYSiAMDKIHGQDFVNWLLAGKGKKNDWKHNITQ
GiP
(Spec. Fig. 4a., described at 121.)
FF 4. Chang states that “[a]n extended GIP peptide is expressed in human
gut cells . . . Alternative post-translational processing of proGIP could lead
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Application 13/387,931
to the generation of a 42-amino-acid mature GIP and an extended 55-amino-
acid isoform (GIP55G or GIP55S) that differ at position 52.” (Chang 26,
Fig. 3.)
FF 5. Chang states that the “GIP [gene] encodes a GIP peptide containing
the variable residue (Serl03 or Glyl03) at rs2291725.” (Chang 26.)
FF 6. Figure 1 of the Specification is described as a “[differential
distribution of alleles at rs2291725 . . . Pie charts represent the proportion of
each genotype by the geographic region.” (Spec. 118.)
FF 7. Chang states that “we found GIP55 is present in human serum and
constitutes ~ l%-3% of the total GIP after a meal. . . Thus, depending on
the genotype, humans could contain two (GIPmT/T: GIP+GIP55S;
GIpmac. GIP+GIP55G) or three GIP isoforms (G/P103T/C:
GIP+GIP55S+GIP55G).” (Chang 27.)
FF 8. GIP55S is identical to claimed SEQ ID NO:l and GIP55G is identical
to claimed SEQ ID NO:2. (See Sequence Listing filed January 30, 2012,
page 1, and Spec. 141.)
FF 9. The Examiner finds that Alsobrook discloses an isolated polypeptide
of SEQ ID NO: 18 consisting essentially of the claimed SEQ ID NO: 1
(amino acids 15—69 of SEQ ID NO: 18), reading on the limitation of claim 1.
(Ans. 2.)
FF 10. SEQ ID NO: 18 of Alsobrook is set forth below:
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Application 13/387,931
<400> SEQUENCE I 13
Thr Gly Ser Lys Val Ser Ser Pro Gin Pro Arg Gly Pro Arg Tyr Ala
1 5 10 IS
Gill Gly Thr Ph e lie Ser Asp Tyr Ser lie Ala Met Asp Lys lie ills
20 23 -f -\
Gin Gin Asp
35
Phe Val Asn Trp Lsu
40
Lbs Ala Gin Lys Gly
4.5
Lys Lys As El
Asp Trp- Lys His Asn lie Thr Gin Arg Gl U Ala Arg Ala Leu Glu Leu
50 55 60
Ala Ser Gin Ala A an Asrg Lys Glu Gin Glu Ala Val Glu Pro Gl n Ser
§5 70 75 SO
Ser PiCO Ala Lya Asa Pro Ser Asp Glu Asp Leu Leu Arg Asp Leu Leu
85 30 35
lie Gltl Cj X 'Ll Leu Leu Ala Cys Leu Leu Asp Gau Thr Asti Leu Cys Arg
ICO 105 US
Leu Arg Ser Arq Val Asp Gly
115
(Alsobrook 79.)
DISCUSSION
Rejection No. 1—Non-statutory subject matter
Issue
Whether a preponderance of evidence of record supports the
Examiner’s conclusion that claims 1 and 2 are directed to non-statutory
subject matter.
Principles of Law
On issues of patent eligibility, we “first determine whether the claims
at issue are directed to a patent-ineligible concept,” such as laws of nature,
natural phenomena, or abstract ideas. Alice Corp. Pty Ltd. v. CLS Banklnt'l,
134 S. Ct. 2347, 2355 (2014) (“Alice”). If this threshold is met, we move to
the second step of the inquiry and “consider the elements of each claim both
individually and ‘as an ordered combination’ to determine whether the
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Application 13/387,931
additional elements ‘transform the nature of the claim’ into a patent-eligible
application.” Id. (quoting Mayo Collaborative Services v. Prometheus
Laboratories, Inc., 132 S.Ct. 1289, 1297—98 (2012) (“Mayo”)).
Analysis
The Examiner rejected claims 1 and 2 because they are “directed to
non-statutory subject matter of natural products,” as evidenced by Chang.
(Ans. 6.) The Examiner points to Chang as “showing GIP55G and GIP55S
related to [a] single nucleotide polymorphism” (SNP ID no: rs2291725) and
“produced by [alternative] post-translation processing.” {Id., citing Chang
26, Fig. 3 ; see FF 4—7.) In particular, the Examiner states that
Claims 1 and 2 are directed to natural product claims reciting
SEQ ID NO: 1 and SEQ ID NO: 2 that are a fragment of gastric
inhibitory peptides with identical amino acid sequence derived
from the naturally occurring products of a gastric inhibitory
peptide and its natural variant as a result of single nucleotide
polymorphism (SNP) [SNP ID no: rs2291725].
(Ans. 6.)
Appellant argues that the claimed invention meets the requirements of
35 U.S.C. § 101 based on the Supreme Court decision in Association for
Molecular Pathology v. Myriad Genetics, Inc., 133 S.Ct. 2107 (2013)
(“Myriad”). (Reply Br. 2.) In particular, Appellant argues that, similar to
the patent eligible cDNA in Myriad, “the amino acid sequence of the
presently claimed polypeptide may be dictated by nature, but the inventors
have selectively removed specific portions of the amino acid sequence to
create a novel composition that is not found in nature.” (Id.) In further
support of that argument, Appellant asserts that the polypeptide of the
present claims is “distinct in both size, sequence and function from the
naturally occurring unprocessed and inactive precursor protein; or from the
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Application 13/387,931
known 42 amino acid mature protein.” (Id.) Appellant also points to Chang
to argue that “[t]he 55 amino acid protein of the present claims . . . was
synthetically produced.” (Id. at 3, citing to Chang 29, bottom of right
column.)
Pursuant to the first step of the Alice patent-eligibility framework, we
find on this record that the claims are directed to a patent-ineligible product
of nature. (FF 1—8.) In particular, SEQ ID NO: 1 and SEQ ID NO:2
correspond to the naturally occurring polypeptides GIP55S and GIP55G,
respectively. (FF 8.) Moreover, unlike the cDNA in Myriad, the claimed
polypeptides are naturally occurring.
In the second step of the Alice framework, we review the claims to
ascertain whether the product of nature has been sufficiently transformed so
as to become patent eligible. See Alice, 134 S. Ct. at 2355. Here, the
claimed polypeptides are “isolated.” (Appeal Br. 7.) Furthermore,
Appellant contends that the claimed polypeptides are distinct from the
precursor protein and “the known 42 amino acid mature protein,” and that
the claimed polypeptides were “synthetically produced.” (Reply Br. 2—3.)
Appellant’s argument that the claimed polypeptides are different or
distinct from the “unprocessed and inactive precursor protein” or “the
known 42 amino acid mature protein” (Reply Br. 2) is unpersuasive because
the claimed polypeptides are naturally occurring. (FF 1—8.) Likewise,
Appellant’s claims are not saved by the fact that the claimed sequences are
isolated or synthetically produced. Our reviewing court has stated
(regarding gene sequences) that “it makes no difference that the identified
gene sequences are synthetically replicated. As the Supreme Court made
clear, neither naturally occurring compositions of matter, nor synthetically
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created compositions that are structurally identical to the naturally occurring
compositions, are patent eligible.” In re BRCAl-and BRCA2-Based
Hereditary Cancer Test Patent Litigation, 774 F.3d 755, 760 (Fed. Cir.
2014) (citing Myriad, 133 S.Ct. at 2117.); see also Myriad, 133 S.Ct. at 2118
(“Nor are Myriad’s claims saved by the fact that isolating DNA from the
human genome severs chemical bonds and thereby creates a nonnaturally
occurring molecule.”). A similar analysis and conclusion applies to the
claimed amino acid sequences.
On the record before us, we find that SEQ ID NO: 1, recited in both
claims 1 and 2, is a naturally occurring product of nature. Moreover, neither
the existence of different products of nature, nor the fact that the claimed
SEQ ID NO: 1 is isolated or synthetically produced, saves SEQ ID NO: 1 as
claimed from being patent-ineligible subject matter. Accordingly, rejection
no. 1 is affirmed.
Conclusion
A preponderance of evidence of record supports the Examiner’s
conclusion that claims 1 and 2 are directed to non-statutory subject matter.
Rejection No. 2—Anticipation
Issue
Whether a preponderance of evidence of record supports the
Examiner’s finding of anticipation under 35 U.S.C. § 102(b).
Principles of Law
A claim is anticipated if a prior art reference discloses every limitation
of the claimed invention, either explicitly or inherently. In re Schreiber, 128
F.3d 1473, 1477 (Fed. Cir. 1997).
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Application 13/387,931
Analysis
Claim 1
Appellant challenges the Examiner’s finding that claim 1 is
anticipated by Alsobrook with the following arguments.
Consisting Essentially Of
Appellant points to the transitional phrase in claim 1 (“consisting
essentially of’) and states that SEQ ID NO:l or SEQ ID NO:2 “may be
flanked with one or more amino acid or other residues that do not materially
affect any basic characteristics of the polypeptide.”7 (Appeal Br. 4.)
Appellant argues further that the 119 amino acids sequence of Alsobrook
(FF 10) “corresponds to a portion of the GIP preproprotein” and that “[t]he
preproprotein does not have the biological activity of the mature protein in
the absence of processing.” (Id.) As such, according to Appellant, “the
additional amino acid residues present in the Alsobrook protein materially
affect the basic characteristics of the protein” because “these residues result
in a protein that does not have the biological activity of the processed
protein.” (Id.)
We are not persuaded. The Examiner set forth a prima facie case of
anticipation; namely, that Alsobrook discloses an isolated polypeptide
consisting essentially of SEQ ID NO:l. (FF 9, 10.) Appellant’s argument
that the additional residues in the Alsobrook protein “materially affect the
basic characteristics of the protein” is mere argument, unsupported by
7 Appellant’s usage of “consisting essentially of’ (Spec. 1 50) is similar to
the generally accepted usage of that transitional phrase. See In re Herz, 537
F.2d 549, 551-52 (CCPA 1976).
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Application 13/387,931
evidence.8 See Estee Lauder Inc. v. L’Oreal, S.A., 129 F.3d 588, 595 (Fed.
Cir. 1997) (attorney argument cannot take the place of evidence).
Accordingly, on this record, we are not persuaded that the additional
residues in Alsobrook would “materially affect any basic characteristics of
the polypeptide.” (Spec. 1 50.)
Bioactivity of GIP isoforms
Appellant argues that “the polypeptide of the present claims is distinct
in both size, sequence and function from the unprocessed and inactive
precursor protein; or from the known 42 amino acid mature protein.”
(Appeal Br. 3.) In support of that argument, Appellant refers to
“[functional testing of Appellant[’s] synthetic GIP isoforms (GIP, GIP55G,
and GIP55S).” (Id.) For example, Appellant states that “[sjurprisingly, it
was found that both GIP55G and GIP55S are significantly more resistant to
degradation by either pooled normal human serum [] or pooled complement-
preserved human serum.” (Id. at 4.)
We are not persuaded. Alsobrook discloses the isolated polypeptide
as recited in claim 1. (FF 9, 10.) Moreover, the fact that Appellant may
have discovered a property of SEQ ID NO: 1 or SEQ ID NO:2 does not
overcome an anticipation finding. See In re Spada, 911 F.2d 705, 708 (Fed.
Cir. 1990) (“The discovery of a new property or use of a previously known
composition . . . can not impart patentability to claims to the known
composition.”) (citing cases); see also In re Papesch, 315 F.2d 381, 391
8 To be clear, while we acknowledge Appellant’s arguments regarding
certain testing of GIP isoforms (Appeal Br. 3—4), Appellant does not point to
any evidence regarding the characteristics of Alsobrook’s SEQ ID NO: 18.
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(CCPA 1963) (“From the standpoint of patent law, a compound and all of its
properties are inseparable; they are one and the same thing.”).
Rejection No. 2 for anticipation of claim 1 by Alsobrook is affirmed.
Claim 2
Claim 2 differs from claim 1 in that it uses the transitional phrase
“consisting of’ and is limited to SEQ ID NO:l. See Vehicular Tech Corp. v.
Titan Wheel Inti, Inc., 212 F.3d 1377, 1383 (Fed. Cir. 2000) (“In simple
terms, a drafter uses the phrase ‘consisting of to mean ‘I claim what follows
and nothing else.’”).
The Examiner rejected claim 2 for anticipation based on the following
statement:
Alsobrook [] show SEQ ID NO: 18 comprises an RXXR motif
of RGPR at amino acid positions 11-14 and an RK cleavage site
at amino acid positions 70-71 inherently as a precursor to
generate the precise sequence of SEQ ID NO: 1 (GIP55S) in
patient specimens, evidenced by Chang [] showing alternatively
post-translation process generates GIP55S in mammalian cells []
reading on the limitation of claim 2.
(Ans. 3.)
Appellant argues that “it is not inherent that the prior art [Alsobrook]
sequence would be processed into the 55 amino acid protein ... it would be
inherent that the processing would result in the known 42 amino acid mature
protein.” (Appeal Br. 5; Reply Br. 3.)
“[T]he examiner bears the initial burden, on review of the prior art or
on any other ground, of presenting a prima facie case of unpatentability.” In
re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992). On this record, we find
that the Examiner has not set forth a prima facie case of anticipation of claim
2 because Alsobrook’s SEQ ID. NO: 18 does not describe a polypeptide
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“consisting of’ SEQ ID NO:l as claimed. Moreover, the Examiner’s
inherency analysis relies on what occurs in nature (“in patient specimens” or
“in mammalian cells”). (Ans. 3.) However, under that analysis, the claimed
polypeptide is no longer “isolated” as recited in claim 2. As such, the
Examiner’s position of anticipation based on inherency fails.
Rejection No. 2 for anticipation of claim 2 by Alsobrook is reversed.
Conclusion
A preponderance of evidence of record supports the Examiner’s
finding that claim 1 is anticipated under 35 U.S.C. § 102(b).
A preponderance of evidence of record fails to support the Examiner’s
finding that claim 2 is anticipated under 35 U.S.C. § 102(b).
Rejection No. 3—Obviousness
Issue
Whether a preponderance of evidence of record supports the
Examiner’s conclusion of obviousness under 35 U.S.C. § 103(a).
Analysis
Claim 1
Appellant contests the obviousness rejection by relying on the
anticipation arguments set forth above with respect to claim 1. (Appeal Br.
6.) Those arguments are unpersuasive for the reasons set forth above.
Moreover, claim 1 is anticipated, and anticipation is “epitome of
obviousness.” In re McDaniel, 293 F.3d 1379, 1385 (Fed. Cir. 2002)
(citations omitted). Accordingly, we affirm the rejection of claim 1 for
obviousness.
Claim 2
In rejecting claim 2 for obviousness, the Examiner relies on the same
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inherency position set forth above, as well as Kozian for showing that “it is
well-known that the GIP gene has an amino acid substitution variant,
Ser—>Gly, at position 103 of prepro-GIP.” (Ans. 5.) Appellant argues that
Kozian “does not teach or suggest the 55 amino acid form of GIP.” (Appeal
Br. 6.)
We find that the Examiner has not established a prima facie case of
obviousness as to claim 2. See Oetiker, 977 F.2d at 1445. In particular, we
find the Examiner’s inherency position flawed for the reasons set forth
above. In addition, the Examiner does not explain how Kozian’s disclosure
of “an amino acid substitution variant” teaches or suggests GIP55S (SEQ ID
NO:l).
Conclusion of Law
A preponderance of evidence of record supports the Examiner’s
conclusion that claim 1 is obvious under 35 U.S.C. § 103(a).
A preponderance of evidence of record fails to support the Examiner’s
conclusion that claim 2 is obvious under 35 U.S.C. § 103(a).
SUMMARY
We affirm the rejection of claims 1 and 2 under 35 U.S.C. § 101 as
directed to non-statutory subject matter.
We affirm the rejections of claim 1 under 35 U.S.C. § 102(b) and 35
U.S.C. § 103(a). We reverse the rejections of claim 2 under 35 U.S.C.
§ 102(b) and 35 U.S.C. § 103(a).
TIME PERIOD FOR RESPONSE
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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