Zurawski, Gerard et al.

Patent Trials and Appeals Board

Oct 23, 2019

14887151 - (D) (P.T.A.B. Oct. 23, 2019)

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.
14/887,151 10/19/2015 Gerard Zurawski BHCS.P0036C1D1/1000205590 1064
32425 7590 10/23/2019
NORTON ROSE FULBRIGHT US LLP
98 SAN JACINTO BOULEVARD
SUITE 1100
AUSTIN, TX 78701-4255
EXAMINER
HUYNH, PHUONG N
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
10/23/2019 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):
aoipdocket@nortonrosefulbright.com
PTOL-90A (Rev. 04/07)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte GERARD ZURAWSKI, ANNE-LAURE FLAMAR, and
EYNAV KLECHEVSKY
____________

Appeal 2019-003621
Application 14/887,151
Technology Center 1600
____________

Before JEFFREY N. FREDMAN, DEBORAH KATZ, and JOHN G. NEW,
Administrative Patent Judges.

KATZ, Administrative Patent Judge.

DECISION ON APPEAL

Appellant1 seeks our review, under 35 U.S.C. § 134(a), of the
Examiner’s decision to reject claims 39–47, 49–53, 59, and 60. (Appeal
Brief filed July 2, 2018 (“Br.”) 1–4.)2
We have jurisdiction under 35 U.S.C. § 6(b). We AFFIRM.

1 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 Baylor
Research Institute. (See Br. 1.)
2 Claims 48, 61, and 62 are withdrawn.
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Application 14/887,151

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INTRODUCTION
Appellant’s Specification provides a method of assembling antibody-
antigen complexes by simply mixing components. (Specification dated
October 3, 2017 (“Spec.”) ¶ 6.) The Specification discloses that cohesin
and dockerin protein domains, which are derived from bacterial cellulosome,
can be used to produce fusion proteins in mammalian cells because they
form high affinity protein-protein complexes. (Id. ¶¶ 8–10.) The
Specification exemplifies the use of cohesion-dockerin binding pairs in a
modular rodent monoclonal antibody (rAb) carrier that includes at least a
portion of an antibody linked to one half of a cohesin-dockerin binding pair
and an antigen linked to the other half of the cohesin-dockerin binding pair.
(Id. ¶ 12, Fig. 1.)
Appellant’s claim 39 is representative of the subject matter on appeal
and recites:
A method of making a complex comprising

combining an antigen-specific binding domain with one
or more antigen carrier domain(s),

wherein the antigen-specific binding domain comprises
one of a cohesin or dockerin binding pair and

the antigen carrier domain comprises a peptide antigen
and the other of a cohesin dockerin binding pair.

(Br. 5.)
The Examiner rejected the claims as follows:
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Claims
Rejected
35 U.S.C. § Basis Final Office
Action
39–43, 45–46,
49–51, 60
103(a)(pre-AIA) Bayer3 and
Bozzacco4
4–9
44, 47, 52, 53 103(a) Bayer, Bozzacco,
Hawiger,5 and
Ninomiya6
9–13
59 103(a) Bayer, Bozzacco,
and Bates7
13–14

ANALYSIS
The Examiner finds that Bayer teaches the strong interaction between
cohesion and dockerin forms an affinity complex. (Final Action dated
December 12, 2017 (“Final Act.”) 4, citing Bayer 384.) The Examiner finds
that Bayer teaches hybrid biomolecules of dockerins or cohesins fused to
protein A, antibodies, lectins, or DNA. (Id., citing Bayer 384–385.) The
Examiner finds “[f]or example, a dockerin-antibody hybrid can be mixed

3 Bayer, E. A. et al., The Cellulosome - A Treasure-trove for Biotechnology,
12 Trends in Biotechnology 379–386 (1994).
4 Bozzacco, L. et al., DEC-205 Receptor on Dendritic Cells Mediates
Presentation of HIV Gag Protein to CD8+ T cells in a Spectrum of Human
MHC I Haplotypes, 104 Proc. Nat’l Acad. Sci. 1289–1294 (2007).
5 Hawiger et al., US 2004/0258668 A1, published December 23, 2004.
6 Ninomiya, A. et al., Intranasal Administration of A Synthetic Peptide
Vaccine Encapsulated in Liposome Together With an anti-CD40 Antibody
Induces Protective Immunity Against Influenza A Virus In Mice, 20 Vaccine
3123–3129 (2002).
7 Bates, E. E. M. et al., APCs Express DCIR, a Novel C-Type Lectin Surface
Receptor Containing an Immunoreceptor Tyrosine-Based Inhibitory Motif,
163 J. Immunol. 1973–1983 (1999).
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with cohesin-lectin hybrid in order to couple to a desired antigen or
glycoprotein.” (Id., citing Bayer 385.) The Examiner finds further that
Bayer teaches advantages using a cohesion-dockerin affinity complex to
provide numerous advantages, for example that the 1:1 binding ratio of
dockerin to cohesin enables better control of the coupling component and
that multi-component complexes can contain a series of different cohesins
complexing with multiple dockerins. (Final Act. 4–5, citing Bayer 385.)
Because Bayer does not teach a peptide antigen, the Examiner cites
Bozzacco for its teaching to link a monoclonal antibody that binds to a
human receptor with a viral antigen to improve presentation of the antigen
and increase vaccine efficacy. (Final Act. 5, citing Bozzacco 1292.) More
specifically, the Examiner finds Bozzacco teaches a monoclonal antibody
that binds to dendritic cell receptor DEC-205 fused to an HIV antigen gag
p24 peptide. (Id.) The Examiner finds one of ordinary skill in the art would
have been motivated modify Bayer’s hybrid biomolecule complex with
Bozzacco’s antibody-antigen pair by attaching an anti-DEC-205 antibody to
cohesin or dockerin and a viral peptide antigen to the complementary
dockerin or cohesin in order to delivery viral antigens to dendritic cells.
(Final Act. 5–6.) The reason to do so would be to take advantage of the
flexibility and high affinity of dockerin-cohesin 1:1 binding complex. (Id. at
6.)
Appellant argues that there is no reason “to modify the complex of
Bozzacco to employ the cohesin and dockerin molecules described in Bayer,
and one would not have a reasonable expectation of success for performing
the methods described in Bozzacco with such modifications.” (Br. 2.)
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Appellant further argues that the Examiner’s proposed modification would
change the principle of operation of the references. (Id.)
Appellant contends that Bozzacco teaches a fusion protein of an
antibody covalently attached to an HIV antigen. (Br. 2, citing Bozzacco
1293.) Appellant argues there is no reason to modify Bozzacco’s fusion
protein with Bayer’s non-covalent affinity complex. (Id.) Appellant argues
that covalent bonds are metastable and typically require a catalyst to break
the bond. (Id. at 3, citing Mathews.8) Appellant further argues that
Bozzacco requires internalization of the fusion protein for effective cross-
presentation, and that there is no evidence that a molecular complex would
function similarly to a covalent bond attachment. (Id. at 2–3.) Appellant
contends that “although the claims are not drawn to a method of antigen
presentation, the proposed modifications to the complex of Bozzacco cannot
render the complex unsatisfactory and/or change the principle of operation
of the complex for use in the methods described in Bozzacco.” (Id. at 3.)
We are not persuaded by Appellant’s arguments that there would not
have been a reason to combine the prior art. Appellant argues against
modifying Bozzacco’s antibody-antigen fusion protein with Bayer’s
cohesin-dockerin affinity complex. However, the Examiner’s rejection
modifies Bayer’s dockerin-antibody cohesin-hybrid affinity complex with
Bozzacco’s specific DEC-205 antibody and HIV peptide antigen. Therefore,
Appellant does not address the Examiner’s rejection.

8 Mathews C., and Van Hold, K., Biochemistry, The Benjamin/Cummings
Publishing Company at 25 (1996), submitted October 3, 2017.
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Bayer teaches hybrid biomolecules including fusion proteins
incorporating cohesin and dockerin. (Bayer 384–385.) Bayer teaches a
dockerin-antibody hybrid can be mixed with a cohesin-hybrid (e.g., lectin,
toxin, protein) to couple a desired antigen. Id. The Examiner cites
Bozzacco for identifying a specific peptide antigen to be combined with a
specific antibody in a cohesin-dockerin affinity system in order to deliver
viral antigens to dendritic cells. “The combination of familiar elements
according to known methods is likely to be obvious when it does no more
than yield predictable results.” KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398,
416 (2007). Because the Examiner articulated a reason from the prior art to
combine the references, we are not persuaded that the Examiner erred.
We are not persuaded by Appellant’s arguments there would not have
been a reasonable expectation of success in the claimed method. (See Br. 3.)
Obviousness does not require absolute predictability of success. . . . [A]ll
that is required is a reasonable expectation of success. Medichem, S.A. v.
Rolabo, S.L., 437 F.3d 1157, 1165 (Fed. Cir. 2006). The combined prior art
cited by the Examiner provides more than a general approach in a promising
field of experimentation; the prior art provides specific guidance as to the
particular form of the claimed invention and how to achieve it. (See id.) In
particular, Bayer teaches the specific advantages of using a cohesin-dockerin
affinity complex, as well as specific examples of fusion proteins, including
dockerin-antibody and cohesin-antigen that would have been obvious to
combine with Bozzacco’s preferred antibody and peptide antigen.
Moreover, the modification does not change the operation of Bayer, it
merely selects a specific antigen as taught by Bozzacco. Although the
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affinity complex may function differently from a covalent bond, “a given
course of action often has simultaneous advantages and disadvantages, and
this does not necessarily obviate motivation to combine.” (Id.) Because the
prior art establishes a reasonable expectation of success in modifying Bayer
with the specific antibody and peptide antigen of Bozzacco, we are not
persuaded that the Examiner erred.
Accordingly, we affirm the Examiner’s rejection of claim 39.
Appellant does not present separate arguments against the rejection of
claims 41–43. Appellant argues that the Examiner erred in rejecting claims
44, 47, 52, 53, and 59 for the same reasons argued against the rejection of
claim 39. (See Br. 4.) Because, as discussed above, we are not persuaded
by Appellant’s arguments we affirm the Examiner’s rejections of all of
Appellant’s pending claims as being obvious under 35 U.S.C. § 103(a).

CONCLUSION
In summary:
Claims
Rejected
35 U.S.C. § References/
Basis
Affirmed Reversed
39–43, 45–46,
49–51, 60
103(a) Bayer and
Bozzacco
39–43, 45–46,
49–51, 60

44, 47, 52, 53 103(a) Bayer, Bozzacco,
Hawiger, and
Ninomiya
44, 47, 52, 53
59 103(a) Bayer, Bozzacco,
and Bates
59
Overall
Outcome
39–47, 49–53,
59, 60

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Application 14/887,151

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No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136.

AFFIRMED