Ex Parte Marletta et al

Patent Trial and Appeal Board

Feb 27, 2017

13077686 (P.T.A.B. Feb. 27, 2017)

United States Patent and Trademark Office
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
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APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/077,686 03/31/2011 Michael A. Marietta BERK-135 6006
84220 7590 03/01/2017
UC Berkeley - OTL
Bozicevic, Field & Francis LLP
201 REDWOOD SHORES PARKWAY
SUITE 200
REDWOOD CITY, CA 94065
EXAMINER
GAR YU, LIANKO G
ART UNIT PAPER NUMBER
1676
NOTIFICATION DATE DELIVERY MODE
03/01/2017 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
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PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte MICHAEL A. MARLETTA, MICHAEL B. WINTER,
EMILY J. MCLAURIN, STEVEN Y. REECE, CHARLES OLEA JR.,
and DANIEL G. NOCERA1
Appeal 2015-004849
Application 13/077,686
Technology Center 1600
Before JOHN G. NEW, RICHARD J. SMITH, and TAWEN CHANG,
Administrative Patent Judges.
SMITH, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35U.S.C. § 134 involving claims to a non-
naturally occurring photoactive polypeptide. We have jurisdiction under
35 U.S.C. § 6(b).
We affirm.
1 According to Appellants, the real parties in interest are: a) The
Massachusetts Institute of Technology; and b) The Regents of the University
of California. (Br. 3.)
Appeal 2015-004849
Application 13/077,686
STATEMENT OF THE CASE
Claims on Appeal
Claims 1—5, 7, 11—14, 35, and 36 are on appeal.2 (Claims Appendix,
Br. i—ii.) Claim 1 is illustrative and reads as follows:
1. A non-naturally occurring photoactive polypeptide
comprising:
a) an H-NOX3 domain-containing heme binding polypeptide
comprising a heme-binding fragment of the Tar4H protein from
Thermoanaerobacter tengcongensis; and
b) a prosthetic group other than heme, wherein the prosthetic
group is bound to the heme-binding polypeptide, wherein the
photoactivity of the photoactive polypeptide is altered upon
exposure to oxygen.
Examiner’s Rejection
Claims 1—5, 7, 11—14, 35, and 36 stand rejected under pre-AIA
35 U.S.C. § 103(a) as unpatentable over Cary4 and Paulson.5 (Final Act. 8—
12.)
FINDINGS OF FACT
We adopt as our own the Examiner’s findings regarding the scope and
content of the prior art, and reasons to combine the cited references. The
following findings are included for emphasis and reference convenience.
2 Claims 6, 10, and 15—34 are withdrawn from consideration. (Final Act.
dated October 25, 2013, at 2.)
3 The Specification states that H-NOX stands for “(Heme Nitric
oxide/OXygen binding).” (Spec. 137.)
4 Cary et al., WO 2007/139767 A2, published Dec. 6, 2007 (“Cary”).
5 Paulson et al., Preparation of Ruthenium(II) and Ruthenium(III) Myoglobin
and the Reaction of Dioxygen, and Carbon Monoxide, with Ruthenium(II)
Myoglobin, 254 The Journal of Biological Chemistry 15, 7002-06
(1979) (“Paulson”).
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Application 13/077,686
FF 1. The Examiner finds that Cary teaches H-NOX proteins derived
from bacterial protein such as [T. Tengcongenisis] (the heme-binding
polypeptide is an H-NOX domain containing polypeptide (elected species)
other than soluble guanylate cyclase) bound to heme (prosthetic group).
(Final Act. 9, citing Cary H 17, 36, 54, 59, and Figure IB.)
FF 2. Cary states that “[h]eme may or may not be bound to the H-
NOX protein. In some embodiments of the isolated H-NOX proteins, NO is
bound to the H-NOX protein.” (Cary 117.)
FF 3. Cary states that
The H-NOX proteins and compositions described herein
can also be used for a number of in vitro or industrial applications
.... Particular H-NOX proteins can be selected for such
applications based on the desired NO dissociation constant....
Moreover, the H-NOX proteins can be used to remove NO from
solutions requiring the removal of NO. For example, the H-NOX
proteins may be used to absorb or remove NO in bioreactors
where NO is an inhibitor of cellular proliferation and/or
mitochondrial function.
(Cary 11 137-138.)
FF 4. The Examiner finds that “Paulson [] teach[es] reconstituting
myoglobin (heme-binding polypeptide) with ruthenium porphyrins to form
ruthenium(II) (prosthetic group other than heme) substituted Myoglobin
(heme-binding polypeptide), RuMb, and ruthenium(Ill) mesoporphyrin
(prosthetic group other than heme) substituted Myoglobin (heme-binding
polypeptide), RuMb+.” (Final Act. 9, citing Paulson Abstract; 7003 rt. col,
par. 2; 7004 rt. col., par. 1—3; Figures 3—6.)
FF 5. The Examiner finds that one of ordinary skill in the art would
have been motivated to substitute the heme of Cary with ruthenium (II)
mesoporphyrin, or ruthenium (III) mesoporphyrin, of Paulson, with a
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Application 13/077,686
reasonable expectation of success, “because Paulson [] states that ruthenium,
the second row transition metal analogue of iron, is an obvious choice for
further studies on metal ion substitution in heme proteins.” (Final Act. 10,
citing Paulson 7002, left col., par. 2.)
DISCUSSION
We adopt, and agree with, the Examiner’s findings, analysis, and
conclusions, as set forth in the Final Action (Final Act. 8—12), Advisory
Action dated Feb. 10, 2014 (Adv. Act. 2—4), and Answer (Ans. 2—4).
We discern no error in the Examiner’s rejection of claims 1—5, 7, 11—
14, 35, and 36 as obvious. (FF 1—5.) The claims are not separately argued,
and we therefore limit our discussion to claim 1.
Issue
Whether a preponderance of evidence of record supports the
Examiner’s rejection for obviousness under 35 U.S.C. § 103(a).
Analysis
Appellants contest the motivation to combine the teachings of Cary
and Paulson by arguing that
substitution of heme from the H-NOX protein (from Cary) with
a ruthenium (II) mesoporphyrin or ruthenium (III)
mesoporphyrin from Paulson, would render the H-NOX protein
of Cary unsatisfactory for its intended purpose. The intended
purpose of the Cary is to use an H-NOX protein as a
physiologically compatible mammalian blood nitric oxide (NO)
gas carrier that can deliver NO to tissues of the body (i.e., “for
blood gas NO delivery”) (see e.g., the abstract of Cary). In order
achieve this goal, Cary describes the generation of mutations of
the polypeptide that alter the binding affinity (and/or binding
kinetics) of the protein complex (polypeptide plus heme) so that
NO can be released to tissues.
(Br. 5.)
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Application 13/077,686
In support of that argument, Appellants refer to several articles for the
proposition that “it was known in the art at the time of filing that ruthenium
could be used as an NO scavenger in biological systems (precisely because
Ruthenium binds NO with high affinity).” (Id. at 5—6.) Thus, according to
Appellants, “one of ordinary skill in the art would readily recognize that an
H-NOX protein of Cary with an incorporated [ruthenium mesoporphyrin]
from Paulson (instead of heme) would bind to NO with much too high an
affinity to be used to deliver NO to tissues.” (Id. at 5.)
Appellants thus argue that the substitution of heme from the H-NOX
protein of Cary with a ruthenium (II/III) mesoporphyrin of Paulson would
render Cary unsatisfactory for its intended purpose or change its mode of
operation. (Br. 4—6.) As so argued, the question to address is: What is the
intended purpose or overall principle of operation of Cary? See In re
Mouttet, 686 F.3d 1322, 1331-33 (Fed. Cir. 2012).
As an initial matter, a reference (e.g., Cary) “may be read for all that it
teaches, including uses beyond its primary purpose.” See Mouttet, 686 F.3d
at 1331. While Cary may well teach the use of its H-NOX proteins for
delivery of NO to body tissues, even as a preferred or primary use, Cary also
teaches other uses of its H-NOX proteins, including for absorption or
removal of NO in bioreactors where a high binding affinity would be
desirable. (Ans. 3^4; FF 3.) Accordingly, for purposes of this appeal, we
find that the intended purpose, or overall principal of operation, of Cary is
the in vivo or in vitro or industrial use of the disclosed H-NOX proteins for
the delivery or absorption/removal of NO. (See, e.g., Cary Abstract and
10, 12, 17, 137, and 138; FF 3.)
Based on the forgoing, we do not find that the substitution of
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Application 13/077,686
ruthenium (II/III) mesoporphyrin in place of the heme from the H-NOX
protein of Cary would render Cary unsatisfactory for its intended purpose or
change its overall principle of operation. Rather, it would be consistent with
Cary’s intended purpose of using its H-NOX proteins for absorbing or
removing NO. (Cary || 137, 138; Ans. 4.) Thus, unlike the facts in In re
Gordon cited by Appellants, the prior art suggests the desirability of the
modification. (FF 1—5.) See In re Gordon, 733 F.2d 900, 902 (Fed. Cir.
1984) (“The mere fact that the prior art could be so modified would not have
made the modification obvious unless the prior art suggested the desirability
of the modification.”) (citing cases); see also Allied Erecting v. Genesis, 825
F.3d 1373, 1380-81 (Fed. Cir. 2016); In reNuVasive, 841 F.3d 966, 973-74
(Fed. Cir. 2016).
Accordingly, the rejection of claim 1 is affirmed.
Conclusion of Law
A preponderance of evidence of record supports the Examiner’s
rejection of claim 1 under 35 U.S.C. § 103(a). Claims 2—5, 7, 11—14, 35,
and 36 were not argued separately and fall with claim 1.
SUMMARY
We affirm the rejection of all claims on appeal.
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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