Ex Parte Lambowitz et al

Patent Trial and Appeal Board

Mar 12, 2018

13254223 (P.T.A.B. Mar. 12, 2018)

United States Patent and Trademark Office
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
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APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/254,223 09/01/2011 Alan M. Lambowitz UTX-021743-U S-PCT-1 7473
26294 7590 03/14/2018
TAROLLI, SUNDHEIM, COVELL & TUMMINO L.L.P.
1300 EAST NINTH STREET, SUITE 1700
CLEVELAND, OH 44114
EXAMINER
HUTSON, RICHARD G
ART UNIT PAPER NUMBER
1652
NOTIFICATION DATE DELIVERY MODE
03/14/2018 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):
rkline @ tarolli. com
docketing@tarolli.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte ALAN M. LAMBOWITZ, SABINE MOHR, GEORG MOHR, and
EMAM GHANEM
Appeal 2017-006588
Application 13/254,2231
Technology Center 1600
Before DEMETRA J. MILLS, ELIZABETH A. LaVIER, and
TAWEN CHANG, Administrative Patent Judges.
LaVIER, Administrative Patent Judge.
DECISION ON APPEAL
Pursuant to 35 U.S.C. § 134(a), Appellants seek review of the
rejections maintained on appeal by the Examiner of claims 1, 4-7, 10-14,
16, 26, and 27. We have jurisdiction under 35 U.S.C. § 6(b). For the
reasons set forth below, we REVERSE.
BACKGROUND
The Specification discusses a need for reverse transcriptase (RT)
enzymes that can function well at high temperatures, and describes a fusion
protein including a thermostable RT connected to a stabilizer protein. See
Spec. 4-5. Claim 1 is illustrative:
1 Appellants state the real party in interest is the Board of Regents, the
University of Texas System. Appeal Br. 3.
Appeal 2017-006588
Application 13/254,223
1. A stabilized reverse transcriptase fusion protein comprising
a thermostable group-II intron reverse transcriptase connected
at its N-terminus by a linker peptide to the C-terminus of a
stabilizer protein including 50 or more amino acids, wherein the
fusion protein exhibits increased solubility and stability in
solution.
Appeal Br. 23 (Claims Appendix).
REJECTIONS MAINTAINED ON APPEAL
1. Claims 1, 4-6, 10-14, 16, 26, and 27 stand rejected under
35 U.S.C. § 103(a) as unpatentable over Lampson2 and Wang.3
Ans. 3.
2. Claims 1, 4-7, 10-14, 16, 26, and 27 stand rejected under 35
U.S.C. § 103(a) as unpatentable over Lampson and Kapust.4 Ans.
4-5.
DISCUSSION
The rejections rely on Lampson to teach a thermostable group-II
intron reverse transcriptase and either Wang or Kapust to teach fusion to a
stabilizer protein. See generally Final Action 6-7, 12-13. Appellants argue
“those skilled in the art at the time of filing believed proteolytic removal of
large tags was necessary to avoid interfering with the activity of the
passenger protein.” Appeal Br. 14 (citing Declaration of Alan M.
Lambowitz, Ph.D., dated June 24, 2016 (Appeal Br. Exhibit C)
(“Declaration”)). The Examiner expressly agrees with this statement. Ans.
2 Lampson et al., WO 2005/084409 A2, published Sept. 15, 2005.
3 Wang, US 6,627,424 Bl, issued Sept. 30, 2003.
4 Kapust et al., Escherichia coli maltose-binding protein is uncommonly
effective at promoting the solubility ofpeptides to which it is fused, 8
Protein Science 1668 (1999).
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Appeal 2017-006588
Application 13/254,223
9. However, the Examiner maintains that this general expectation of
impaired activity “does not override the motivation” to combine Lampson
with Wang relied on by the Examiner, i.e., “increasing the processivity and
stability of the reverse transcriptase.” Id. Similarly, the Examiner points to
“increasing the solubility” as motivation to combine Lampson with Kapust.
Ans. 14.
In light of the evidence, Appellants have the better position. The issue
with the rejections is not the Examiner’s rationale for combining, per se (at
least as to increased solubility5), but rather that the state of the prior art
taught away from making such a combination for a different, very
significant, reason, i.e., loss of function. Although the Examiner is correct
that claim 1 does not require permanent fusion of the RT and the stabilizer
protein (see Ans. 13), we discern no analysis in the rejections demonstrating
that the cited prior art combinations teach or suggest subsequent cleavage of
the fusion protein to yield an active enzyme.
The undisputed evidence that the ordinarily skilled artisan would have
expected combining the prior art to impair the activity of the passenger
protein (here, the group-II intron RT) amounts to a strong teaching away
from making either of the combinations posited in the rejections. There is
no finding of record that improved solubility would have motivated the
5 As to the combination with Wang, the Examiner’s reliance on increased
“processivity” as part of the rationale is directly at odds with the undisputed
Declaration evidence, because processivity (i.e., “the ability of a nucleic acid
modifying enzyme to remain attached to the template or substrate and
perform multiple modification reactions” (Wang 3:56-58)) presupposes
activity.
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Application 13/254,223
ordinarily skilled artisan to make a group-II intron RT fusion protein despite
the predicted loss of function of the RT, for example. In the absence of such
a finding (or of evidence or analysis in support thereof), we conclude the
ordinarily skilled artisan would have been dissuaded from combining the
references as claimed. Cf. Ormco Corp. v. Align Tech., Inc., 463 F.3d 1299,
1308 (Fed. Cir. 2006) (“However, a reference that ‘teaches away’ from a
given combination may negate a motivation to modify the prior art to meet
the claimed invention.” (citation omitted)).
CONCLUSION
The rejections of claims 1, 4-7, 10-14, 16, 26, and 27 are reversed.
REVERSED
4