The Board of Trustees of the Leland Stanford Junior University

Patent Trials and Appeals Board

Nov 25, 2020

2020001151 (P.T.A.B. Nov. 25, 2020)

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.
15/447,019 03/01/2017 Karl Deisseroth STAN-912CON4 8430
77974 7590 11/25/2020
STANFORD UNIVERSITY OFFICE OF TECHNOLOGY LICENSING
BOZICEVIC, FIELD & FRANCIS LLP
201 REDWOOD SHORES PARKWAY
SUITE 200
REDWOOD CITY, CA 94065
EXAMINER
WEHBE, ANNE MARIE SABRINA
ART UNIT PAPER NUMBER
1633
NOTIFICATION DATE DELIVERY MODE
11/25/2020 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 KARL DEISSEROTH,
FENG ZHANG,
and VIVIANA GRADINARU
____________

Appeal 2020-001151
Application 15/447,019
Technology Center 1600
____________

Before ANTON W. FETTING, ULRIKE W. JENKS, and
RACHEL H. TOWNSEND, Administrative Patent Judges.

FETTING, Administrative Patent Judge.

DECISION ON APPEAL

Appeal 2020-001151
Application 15/447,019

2

STATEMENT OF THE CASE1
Karl Deisseroth, Feng Zhang, and Viviana Gradinaru (Appellant2)
seeks review under 35 U.S.C. § 134 of a final rejection of claims 78 and 81–
95, the only claims pending in the application on appeal. We have
jurisdiction over the appeal pursuant to 35 U.S.C. § 6(b).
The Appellant invented a way of stimulating target cells, and more
particularly of using optics to stimulate the target cells. Spec. 1:10–11. An
understanding of the invention can be derived from a reading of exemplary
claim 78, which is reproduced below (bracketed matter and some
paragraphing added).
78. A light-activated protein comprising:
a) a core polypeptide comprising
an amino acid sequence at least 90% identical to
the sequence shown in SEQ ID NO:3, SEQ ID
NO:1, SEQ ID NO:2, or SEQ ID NO:4;
and,
C-terminal to the core polypeptide:
b) an endoplasmic reticulum (ER) export signal; and
c) a membrane trafficking signal.

1 Our decision will make reference to the Appellant’s Appeal Brief (“Appeal
Br.,” filed October 4, 2018) and Reply Brief (“Reply Br.,” filed November
26, 2019), and the Examiner’s Answer (“Ans.,” mailed October 9, 2019),
and Final Action (“Final Act.,” mailed January 8, 2018). Note that page
numbering in the Reply Brief is in Roman numeral format.
2 We use the word “Appellant” to refer to “applicant” as defined in
37 C.F.R. § 1.42. Appellant identifies the real party in interest as The Board
of Trustees of the Leland Stanford Junior University (Appeal Br. 3).
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PRIOR ART
The Examiner relies upon the following prior art:
Name Reference Date
Deisseroth US 9,365,628 B2 June 14, 2016
Gradinaru et al., Brain Cell Biology, vol. 36, 129–139 (2008)
Lanyi et al., J. Biol. Chem., vol. 265(3), 1253–1260 (1990)
Hofherr et al., “Selective Golgi export of Kir2.1 controls the
stoichiometry of functional Kir2.1 channel heteromers,” Journal of Cell
Science, vol. 118, 1935–1943 (2005)
Uniprot Accession Number P02945, integrated into the database on
7/21/86
Zhang et al., “Multimodal fast optical interrogation of neural circuitry,”
Nature, vol. 446, 633–641 (2007)
Aravanis et al., “An optical neural interface: in vivo control of rodent
motor cortex with integrated fiberoptic and optogenetic technology,”
J. Neural Eng. 4, S143–S156 (2007)
REJECTIONS
Claims 78, 81–84, 86–88, 90–92, 94, and 95 stand rejected under 35
U.S.C. § 103(a) as unpatentable over Gradinaru, Lanyi, and Hofherr.3
Claim 85 stands rejected under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Uniprot Accession Number P02945.
Claim 89 stands rejected under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Zhang.

3 The rejection preface omits dependent claim 83. Final Act. 3. There is no
separate discussion of claim 83 by either Examiner or Appellant in the Final
Action, Briefs, and Answer. In light of the absence of this being an issue
before us, the omission is taken to be an inadvertent clerical error and claim
83 is taken as being within in the scope of the first rejection.
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Claim 93 stands rejected under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Aravanis.
Claims 78, 82–83, 86–87, 90–92, and 94 stand rejected under the
judicially created doctrine of obviousness type double patenting as claiming
the patentably indistinguishable subject matter as U.S. Patent
No. 9,365,628.4
ISSUES
The issues of obviousness turn primarily on whether the references
describe the limitations in the claims.
The issues of obviousness type double patenting turn primarily on
whether the claims recite patentably indistinguishable subject matter from
another U.S. Patent.
FACTS PERTINENT TO THE ISSUES
The following enumerated Findings of Fact (FF) are believed to be
supported by a preponderance of the evidence.
Facts Related to the Prior Art
Gradinaru
01. Gradinaru is directed to eNpHR: a Natronomonas
halorhodopsin enhanced for optogenetic applications. Gradinaru
Title.
02. Viviana Gradinaru and Karl Deisseroth, two of the authors, are
also two of the inventors named in the instant appeal.

4 This rejection was newly added in the Answer. Ans. 9.
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03. Temporally precise inhibition of distinct cell types in the intact
nervous system has been enabled by the microbial halorhodopsin
NpHR, a fast light-activated electrogenic Cl− pump. While
neurons can be optically hyperpolarized and inhibited from firing
action potentials at moderate NpHR expression levels, there are
challenges with pushing expression to extremely high levels,
including apparent intracellular accumulations. The authors
sought to molecularly engineer NpHR to achieve strong
expression without these cellular side effects, and found that high
expression correlated with endoplasmic reticulum (ER)
accumulation, and that under these conditions NpHR colocalized
with ER proteins containing the KDEL ER retention sequence.
The authors screened a number of different putative modulators of
membrane trafficking and identified a combination of two motifs,
an N-terminal signal peptide and a C-terminal ER export
sequence, that markedly promoted membrane localization and ER
export defined by confocal microscopy and whole-cell patch
clamp. The modified NpHR displayed increased peak
photocurrent in the absence of aggregations or toxicity, and potent
optical inhibition was observed not only in vitro but also in vivo
with thalamic single-unit recording. The new enhanced NpHR
(eNpHR) allows safe, high-level expression in mammalian
neurons, without toxicity and with augmented inhibitory function,
in vitro and in vivo. Gradinaru Abstract.
04. Gradinaru describes neurons targeted to express the light-
activated chloride pumping halorhodopsin from Natronomonas
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pharaonis (NpHR) which can be hyperpolarized and inhibited
from firing action potentials when exposed to yellow light.
Gradinaru 130.
05. Gradinaru describes transport along the secretory pathway,
with ER export being the first step in the pathway, as crucial for
surface expression of integral membrane proteins. Although some
proteins can exit the ER by bulk flow, ER export of membrane
proteins can be impaired if the protein is either misfolded or lacks
specific export signals. Because NpHR is functional in
mammalian neurons even in vivo, aggregate formation might be
due to lack of an ER export signal rather than misfolding.
Gradinaru describes determining if adding different ER export
signals to the NpHR sequence would abolish aggregate formation.
C-terminal ER export signals have been shown to be important for
efficient processing and surface expression of many membrane
proteins. Gradinaru 130–131.
06. Gradinaru describes the ER export signal peptide as
FCYENEV derived from Kir2.1. Adding FCYENEV to the
NpHR C-terminus along with the signal peptide from the β
subunit of the nAChR to the NpHR N-terminus prevented
aggregate formation, and the result was referred to as eNpHR.
Gradinaru 131–132.
07. Gradinaru explicitly cites Hofherr. “First, we found that in
contrast to NpHR, eNpHR did not colocalize with ER proteins
(Fig. 2B), or show evidence of toxicity even at high expression
levels. eNpHR appeared to be present in somatic Golgi structures,
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typical for transmembrane proteins as they are packaged for
transport.” Gradinaru 132 (citing Hofherr). “The altered
properties of eNpHR as described here clearly do not simply
represent a subtle quantitative change in performance, but rather a
distinct step in the development of this optogenetic technology.
Future improvements could incrementally further advance eNpHR
function, perhaps including the Golgi export signals from Kir2.1.”
Gradinaru 135 (citing Hofherr).
08. Gradinaru describes mammalian cells expressing the
halorhodopsin and contact of the cells with light which result in a
modification of the cells function. Gradinaru 132–133.
Lanyi
09. Lanyi is directed to describing the structure of a halorhodopsin
from Natronobacterium pharaonis. Lanyi Title.
10. Lanyi describes the amino acid sequence of bacterial NpHR.
Lanyi Fig. 1. This is 100% identical to SEQ ID NO:3. Final Act.
4.
11. Lanyi describes nucleic acid encoding NpHR. Lanyi 1255.
Hofherr
12. Hofherr is directed to describing how selective Golgi export of
Kir 2.1 (Potassium inward rectifier channel 2.1) controls the
stoichiometry of functional Kir2.x channel heteromers. Hofherr
Title.
13. Hofherr describes the Kir2.1 protein as comprising both a
peptide for membrane insertion with the sequence
KSRITSEGEYIPLDQIDINV and an ER export signal peptide
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with the sequence FCYENEV, both located in the C terminus of
the protein. Hofherr 1937, Fig. 1, and 1940, Fig. 4.
14. Hofherr describes results that strongly suggest that the
different levels of surface expression of GFPKir2.1 and GFPKir2.4
are due to less efficient anterograde transport of GFPKir2.4 to the
plasma membrane. Hofherr 1937, right column. (GFP refers to
green fluorescent protein. Hofherr 1936, left column.)
15. Hofherr describes designing chimeras of Kir2.l and Kir2.4 by
swapping their cytoplasmic N- and C- terminal domains to
identify the difference in sequence responsible for the distinct
trafficking patterns. Hofherr 1937, right column.
16. Hofherr describes a first set of experiments, in which the C-
terminal domain of Kir2.1was found to contain the critical
targeting information for efficient plasma membrane expression.
A more detailed analysis of the surface expression of further C-
terminal chimeras revealed that a stretch of 20 amino acids within
the Kir2.1 C-terminus was necessary for efficient plasma
membrane targeting and was sufficient to increase surface
expression of GFPKir2.4 by approximately 4-fold. Hofherr 1937,
right column.
17. Hofherr describes test result data that argue in favor of an
active forward trafficking signal in the Kir2.l C-terminus. Hofherr
1938, left column.
18. Hofherr describes an anterograde trafficking motif in the
cytoplasmic C-terminus of Kir2.1 channels that is not only
necessary to promote its Golgi-to-plasma membrane transport in
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both epithelial cells and neurons, but is also sufficient to increase
surface expression of Kir2.4 when inserted at the homologous
position. Hofherr 1939, right column.
19. Hofherr describes Golgi trafficking sequence,
KSRITSEGEYIPLDQIDINV, as amino acids 233-252 of the Kir
2.1 protein. Hofherr Fig. 4A. This is at the C terminus. The
Figure legend of Figure 4 refers to this sequence as the Golgi to
plasma membrane trafficking determinant.
Deisseroth
20. Deisseroth is entitled “OPSIN POLYPEPTIDES AND
METHODS OF USE THEREOF.” Deisseroth Title.
21. Deisseroth’s inventors include two of the instant application’s
inventors. Deisseroth Inventors.
22. Deisseroth’s claim 1 includes “[a]n isolated fusion polypeptide
comprising an amino acid sequence having at least 85% amino
acid sequence identity to the amino acid sequence set forth in SEQ
ID NO: 22.” Deisseroth Claim 1.
23. SEQ ID NO:2 of the instant application is a subset of, and
wholly contained within, Deisseroth’s SEQ ID NO: 22. Ans. 9.
24. Deisseroth’s claim 1 recites that “said polypeptide is fused to
an endoplasmic reticulum (ER) export sequence and/or a
trafficking sequence.”
25. Deisseroth’s Specification recites that “[i]n some
embodiments, a subject DChR1 opsin comprises, in order from
amino terminus to carboxyl terminus, a DChR1 opsin; a
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trafficking sequence; and an ER export sequence.” Deisseroth
5:49–52.

ANALYSIS
Claims 78, 81–82, 84, 86–88, 90–92, 94, and 95 rejected under 35
U.S.C. § 103(a) as unpatentable over Gradinaru, Lanyi, and Hofherr
Initially, we determine that claim 78 is the only claim argued. The
Examiner determines that Gradinaru describes all of claim 78 except for a
membrane trafficking signal at the polypeptide C-terminal. In particular, the
Examiner determines:
Gradinaru et al. teaches a lentiviral vector comprising a
CaMKIIα promoter operatively linked to nucleic acid sequence
encoding NpHR (Natronomonas pharaonis halorhodopsin),
which is further operatively linked to a sequence encoding an
ER export signal peptide and a sequence encoding a signal
peptide for membrane insertion, and which expresses a NpHR
protein comprising an ER export signal peptide and a signal
peptide for membrane insertion (Gradinaru et al., pages 131 and
135). Gradinaru et al. further teaches that the ER export signal
peptide is FCYENEV derived from Kir 2.1 (Gradinaru et al.,
page 131-132). Gradinaru et al. also teaches mammalian cells
expressing the halorhodopsin and contact of the cells with light
which result in a modification of the cells function (Gradinaru
et al., page 132-133).
Non-Final Action mailed June 8, 2017, p. 6. The Examiner cites Lanyi only
as evidence that Gradinaru describes a core polypeptide having an amino
acid sequence 100% identical to the sequence shown in SEQ ID NO:2.
Appellant does not contest that Gradinaru and Lanyi describe claim 78
limitations (a) and (b).
As to limitation (c), the Examiner determines that:
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Hofherr et al. further supplements the teachings of Gradinaru et
al. by teaching that the Kir 2.1 protein comprises both a peptide
for membrane insertion with the sequence
KSRITSEGEYIPLDQIDINV and an ER export signal peptide
with the sequence FCYENEV both located in the C terminus of
the protein (Hofherr et al. page 1937, Figure 1, and page 1940,
Figure 4). Hofherr et al. further teaches that the
KSRITSEGEYIPLDQIDINV sequence can be fused to other
proteins to improve membrane expression (Hofherr et al. , page
1940).
Non-Final Action mailed June 8, 2017, p. 7. The Examiner then determines
the motivation to combine the references as:
it would have been prima facie obvious to the skilled artisan at
the time of filing to add both the ER export signal peptide
FCYENEV and the membrane insertion signal peptide
KSRITSEGEYIPLDQIDINV from the C-terminus of the Kir
2.1 protein to the C-terminus of NpHR with a sequence of SEQ
ID NO:3 as taught by Lanyi et al. with a reasonable expectation
of success as both sequences are derived from C-terminus of
Kir2.1 and have been demonstrated to be effective in directing
membrane trafficking of proteins to the cell surface, and both
Gradinaru et al. and Hofherr et al. provide detailed teachings for
making fusion proteins comprising heterologous trafficking
elements.
Id.
Appellant first argues that “Gradinaru does not provide any teaching
or suggestion of an NpHR with a membrane trafficking signal C-terminal to
the NpHR.” Appeal Br. 7; Reply Br. vii.
The Examiner applies Hofherr rather than Gradinaru for this
limitation. Beyond that, the Examiner answers:
Gradinaru et al. provides a specific suggestion to make
additional improvements to eNpHR and points to Hofherr et al.
as a source of potential future improvements. Hofherr et al.
teaches a number of trafficking signals from Kir 2.1, not limited
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to the Golgi export signal and there is no requirement that
Gradinaru et al. specifically point to the
KSRITSEGEYIPLDQIDINV taught by Hofherr et al. to
establish obviousness.
Ans. 11.
Appellant next argues that “Gradinaru in view of Hofherr does not
provide a predicted success of plasma membrane expression of a non-
mammalian opsin in a mammalian cell.” Appeal Br. 8; Reply Br. viii.
The Examiner answers that
Gradinaru et al. clearly demonstrates that that the addition of a
membrane trafficking peptide, specifically the ER export
peptide from the C terminus of Kir2.1 from the a mammalian
protein to the C-terminus of a bacterial opsin does in fact
improve membrane expression of the bacterial protein in
mammalian cells thus providing a reasonable expectation that
mammalian trafficking peptides can function when fused to a
bacterial opsin.
Ans. 12.
Appellant replies that the Examiner “does not take into consideration
that despite this finding in Gradinaru, Gradinaru admits that improvements
were necessary to address the technical challenges with ‘expressing
heterologous membrane proteins in mammalian cells can lead to poor
folding, assembly, and trafficking.’” Reply Br. ix (citing Gradinaru 130).
Appellant omits, however, the follow on in Gradinaru’s same section that
“we report here on a strategy to increase the efficiency of NpHR membrane
targeting to maximize photocurrents without aggregations or toxicity, even
for high expression levels under strong promoters, in vitro and in vivo.”
Gradinaru 130 Gradinaru goes on in the Results section to say that “we
found that in contrast to NpHR, eNpHR did not colocalize with ER proteins,
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or show evidence of toxicity even at high expression levels.” Gradinaru 132
(citing the Hofherr reference herein applied).
Appellant goes on to argue that “the Examiner has not provided a
sufficient reason for why one of ordinary skill in the art would select the
references cited and modify them in the manner suggested to provide a light-
activated opsin that includes an ER export signal and a membrane trafficking
signal C-terminal to the light-activated opsin.” Appeal Br. 9. As determined
above, the Examiner finds that Gradinaru describes claim 78 except for
limitation (c), Hofherr describes the benefits in membrane expression arising
from locating a membrane trafficking signal on the C-terminal side as in
limitation (c), and Gradinaru explicitly cites Hofherr for potential
improvements. See FF 07, 13–19.
Appellant next argues that “[i]t was not predictable from Hofherr
which of the 3 elements discussed in Hofherr would promote expression of a
microbial opsin at the plasma membrane of a mammalian cell such as a
neuron.” Appeal Br. 9; Reply Br. x.
The Examiner answers that
Hofherr et al. clearly teaches the functionality of the
KSRITSEGEYIPLDQIDINV peptide when placed C-terminus
to a protein. Hofherr et al. teaches that the C-terminus
trafficking peptides includes an ER export signal at amino acids
374-380 and a trafficking determinant at amino acids 233-252,
KSRITSEGEYIPLDQIDINV, and that modification or removal
of this sequence substantially decreases membrane expression
(Hofherr et al., Figures 1 and 4). Thus, Hofherr et al. does in
fact teach the importance of the KSRITSEGEYIPLDQIDINV
peptide sequence and provides substantial motivation to further
add this sequence to the eNpHR comprising the C-terminus ER
export signal also from Kir 2.1 as taught by Gradinaru et al. to
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potentially improve membrane expression of the resulting
fusion protein with a reasonable expectation of success.
Ans. 12–13.
Appellant replies
one of ordinary skill in the art, based on the teachings of
Stockklausner 2001 and Stockklausner 2003, might have
concluded that both the ER export signal C-terminal to the
Kir2.1 channel and the Golgi export signal at the N-terminus of
the Kir2.1 channel are necessary in regulating surface
expression of the Kir2.1 protein.
Reply Br. x. Appellant refers to two articles by Stockklausner for the first
time in the Appeal Brief. The argument is speculative, as evidenced by the
use of the phrase “might have concluded.” Further, Appellant’s argument
regarding Stockklausner 2001 only shows that Gradinaru’s disclosed C-
terminal ER export signal is needed, and Appellant’s argument regarding
Stockklausner 2003 only shows that the information in a Golgi export signal
is needed, not that it needs to be located at the N- terminal side. In any
event, Hofherr describes the benefits of locating both signals at the C-
terminal side.
Claim 85 rejected under 35 U.S.C. § 103(a) as unpatentable over
Gradinaru, Lanyi, Hofherr, and Uniprot Accession Number P02945
Appellant relies on the arguments in support of claim 78, which are
equally unpersuasive here.
Claim 89 rejected under 35 U.S.C. § 103(a) as unpatentable over
Gradinaru, Lanyi, Hofherr, and Zhang
Appellant relies on the arguments in support of claim 78, which are
equally unpersuasive here.
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Claim 93 rejected under 35 U.S.C. § 103(a) as unpatentable over
Gradinaru, Lanyi, Hofherr, and Aravanis
Appellant relies on the arguments in support of claim 78, which are
equally unpersuasive here.
Claims 78, 82-83, 86-87, 90-92, and 94 rejected under the judicially created
doctrine of obviousness type double patenting as claiming the patentably
indistinguishable subject matter as another U.S. Patent (9,365,628)
Claim 1 of Deisseroth reads as: “[a]n isolated fusion polypeptide
comprising an amino acid sequence having at least 85% amino acid
sequence identity to the amino acid sequence set forth in SEQID NO: 22,
wherein said polypeptide is fused to an endoplasmic reticulum (ER) export
sequence and/or a trafficking sequence.”
The Examiner determines that claim 78 in the instant application is a
partial sequence of the polypeptide disclosed in Deisseroth. Ans. 9. In
particular, SEQ ID:2 recited in claim 78 is a subset of the amino acid
sequence of SEQ ID: 22 recited in Deisseroth’s claim 1, and so is patentably
indistinct from the larger sequence claimed in Deisseroth. FF 22. If the
claimed invention is “merely an obvious variation of an invention disclosed
and claimed in the [reference] patent,” the instant claims would be invalid
for obviousness-type double patenting. See Abbvie Inc. v. Mathilda &
Terence Kennedy Inst. of Rheumatology Tr., 764 F.3d 1366, 1379 (Fed. Cir.
2014) (quoting In re Vogel, 422 F.2d 438, 441 (CCPA 1970). Although “[i]t
is well-settled that a narrow species can be non-obvious and patent eligible
despite a patent on its genus[,] . . . not every species of a patented genus is
separately patentable.” Id. (citations omitted). The present claims are
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directed to a protein that includes a core polypeptide having an at least 90%
identity to a particular amino acid sequence. SEQ ID NO:2 is 365 amino
acids in length (Spec. 10:17) while SEQ ID NO:22 of the reference patent is
720 amino acids in length (Deisseroth 59–61). One of ordinary skill in the
art could at once envision all the sequences having a length of 365 amino
acids within the 720 amino acid sequence disclosed in Deisseroth rendering
the species recited as SEQ ID NO:2 unpatentable from SEQ ID NO 22. See
Abbvie at 1379 (citing In re Petering, 301 F.2d 676, 681–82 (1962)). As to
the last two limitations in claim 78, Appellant argues that
the '628 patent does not teach or suggest the particular location
at which the ER export signal and a trafficking sequence is
located relative to the core polypeptide. . . . Furthermore, the
Examiner has not provided any reasoning or guidance in the
'628 patent as to why it would have been obvious to one of
ordinary skill in the art to place the ER export signal and
trafficking signal C- terminal to the core polypeptide.
Reply Br. iii. Appellant omits the fact that the Deisseroth claim 1 recites
that “said polypeptide is fused to an endoplasmic reticulum (ER) export
sequence and/or a trafficking sequence” and the Specification recites that
“[i]n some embodiments, a subject DChR1 opsin comprises, in order from
amino terminus to carboxyl terminus, a DChR1 opsin; a trafficking
sequence; and an ER export sequence.” FF 24 and 25. Deisseroth therefore
claims encompass the placement of the claim 78 signals, and also describes
the particular C-terminal placement as recited in claim 78.
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CONCLUSIONS OF LAW
The rejection of claims 78, 81–84, 86–88, 90–92, 94, and 95 under 35
U.S.C. § 103(a) as unpatentable over Gradinaru, Lanyi, and Hofherr is
proper.
The rejection of claim 85 under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Uniprot Accession Number P02945 is
proper.
The rejection of claim 89 under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Zhang is proper.
The rejection of claim 93 under 35 U.S.C. § 103(a) as unpatentable
over Gradinaru, Lanyi, Hofherr, and Aravanis is proper.
The rejection of claims 78, 82–83, 86–87, 90–92, and 94 under the
judicially created doctrine of obviousness type double patenting as claiming
the patentably indistinguishable subject matter as another U.S. Patent is
proper.
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CONCLUSION
The rejection of claims 78 and 81–95 is affirmed.
In summary:
Claims
Rejected
35
U.S.C.
§
Reference(s)/Basis Affirmed Reversed
78, 81–84, 86–88,
90–92, 94, 95
103 Gradinaru, Lanyi,
Hofherr
78, 81–84, 86–88,
90–92, 94, 95

85 103 Gradinaru, Lanyi,
Hofherr, Uniprot
Accession Number
P02945
85
89 103 Gradinaru, Lanyi,
Hofherr, Zhang
89
93 103 Gradinaru, Lanyi,
Hofherr, Aravanis
93
78, 82–83, 86–87,
90–92, 94
Non-Statutory
Double Patenting
78, 82–83, 86–87,
90–92, 94

Overall Outcome 78, 81–95

No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a). See 37 C.F.R.
§ 1.136(a)(1)(iv) (2011).

AFFIRMED