THE BOARD OF REGENTS OF THE UNIVERSITY OF OKLAHOMA

Patent Trials and Appeals Board

May 26, 2020

13859811 - (D) (P.T.A.B. May. 26, 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.
13/859,811 04/10/2013 William H. Hildebrand OAKU.004P13C1 4149
20995 7590 05/26/2020
KNOBBE MARTENS OLSON & BEAR LLP
2040 MAIN STREET
FOURTEENTH FLOOR
IRVINE, CA 92614
EXAMINER
DIBRINO, MARIANNE
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
05/26/2020 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):
efiling@knobbe.com
jayna.cartee@knobbe.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
__________

Ex parte WILLIAM H. HILDEBRAND and STEVEN CATE
__________

Appeal 2019-006632
Application 13/859,811
Technology Center 1600
__________

Before FRANCISCO C. PRATS, TAWEN CHANG, and
DAVID COTTA, Administrative Patent Judges.

PRATS, Administrative Patent Judge.

DECISION ON APPEAL

Pursuant to 35 U.S.C. § 134(a), Appellant1 appeals from the
Examiner’s decision to finally reject claims 1, 3, 5, 7, and 12–21. 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 states that the real parties in interest “include the
assignee of the patent application, The Board of Regents of the University of
Oklahoma; as well as the exclusive licensee of the patent application, Pure
Transplant Solutions, LLC.” Appeal Br. 2.
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STATEMENT OF THE CASE
The following rejections are before us for review:
(1) Claims 1, 3, 5, 7, 12, 13, and 18–21, under 35 U.S.C. § 103(a) as
being unpatentable over Hildebrand2 and Kalandadze3 (Final Act. 2–4;4 Ans.
3–9);
(2) Claims 14 and 15, under 35 U.S.C. § 103(a) as being unpatentable
over Hildebrand, Kalandadze, and Rhode5 (Final Act. 6; Ans. 9–10); and
(3) Claims 14–17, under 35 U.S.C. § 103(a) as being unpatentable
over Hildebrand, Kalandadze, and Prilliman6 (Final Act. 7; Ans. 10–11).
Claim 1 is representative and reads as follows:
1. A method of producing isolated, HLA class II
trimolecular complexes, wherein the isolated, HLA class II
trimolecular complexes comprise a soluble, glycosylated alpha
chain, a soluble, glycosylated beta chain, and a non-covalently
associated, endogenously produced peptide ligand, the method
comprising the steps of:
culturing a recombinant immortalized mouse
antigen-presenting cell line selected from the
group consisting of dendritic cells, macrophages,
and B cells and further comprising a first isolated
nucleic acid segment encoding a soluble form of
an alpha chain of a HLA class II molecule, the
alpha chain comprising a first leucine zipper
domain, and a second isolated nucleic acid

2 US 2008/0145872 A1 (published June 19, 2008).
3 Avtandil Kalandadze et al., Expression of Recombinant HLA-DR2
Molecules, 271 J. BIOL. CHEM. 20156–20162 (1996).
4 Final Action entered December 20, 2018.
5 US 6,232,445 B1 (issued May 15, 2001).
6 Kiley Prilliman et al., Large-scale production of class I bound peptides:
assigning a signature to HLA-B* 1501, 45 IMMUNOGENETICS 379–385
(1997).
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segment encoding a soluble form of a beta chain of
the HLA class II molecule, the beta chain
comprising a second leucine zipper domain,
wherein the recombinant immortalized mouse
antigen-presenting cell line is cultured under
conditions that allow for expression of the soluble
class II alpha and beta chains, association of the
soluble class II alpha and beta chains,
glycosylation of the soluble class II alpha and beta
chains, and loading of an antigen binding groove
formed from the soluble class II alpha and beta
chains with an endogenously produced, non-
covalently associated peptide ligand, thereby
producing soluble class II trimolecular complexes;
and
isolating the soluble class II trimolecular complexes
secreted from the recombinant immortalized
mouse cell line, whereby each trimolecular
complex so isolated comprises identical
recombinant, individual soluble alpha and beta
chain molecules of the HLA class II.

Appeal Br. 11.
OBVIOUSNESS—
HILDEBRAND AND KALANDADZE
The Examiner’s Prima Facie Case
In rejecting claims 1, 3, 5, 7, 12, 13, and 18–21, the Examiner cited
Hildebrand as describing a process of producing isolated HLA class II
trimolecular complexes from a recombinant immortalized mouse antigen
presenting cell line, Hildebrand’s process having nearly all of the steps and
features recited in the rejected claims. Ans. 4–7.
The Examiner found that Hildebrand’s process differed from the
process recited in the rejected claims in that Hildebrand “does not disclose
wherein each chain of the HLA class II trimolecular complex also comprises
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a leucine zipper motif capable of tethering the alpha and beta chains.” Ans.
7.
The Examiner cited Kalandadze as evidence that, despite the
difference between the process of the rejected claims and Hildebrand, the
claimed process would have been obvious to a skilled artisan. See Ans. 7–8.
In particular, the Examiner cited Kalandadze as disclosing that, when yeast
and mammalian cells were engineered to express a construct in which
leucine zipper motifs replaced the transmembrane domains of each of the
alpha and beta subunits of an HLA class II molecule (HLA-DR2), the cells
were capable of secreting the HLA-DR2 alpha/beta dimers in a form that
was stable in solution. Id.
Based on references’ combined teachings, the Examiner reasoned that
a skilled artisan would have considered it obvious to replace the
transmembrane portions of the alpha and beta subunits of the HLA class II
molecules produced by Hildebrand’s cultured mouse cells with the leucine
zipper motifs taught by Kalandadze. Ans. 8. The Examiner determined that
the posited modification of Hildebrand according to Kalandadze’s teachings
would result in trimolecular complexes composed of the leucine
zipper-modified alpha/beta subunits and an endogenous peptide ligand, that
would be secreted in soluble form by the cultured mouse cells, as recited in
the rejected claims. See id.
As to motivation for the asserted combination, the Examiner reasoned
as follows:
One or ordinary skill in the art would have been motivated to
do this in order to continuously produce large quantities of
stably associated, soluble HLA-DR/endogenous peptide
complexes (of higher purity in initial non-downstream
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processing) than can be produced by detergent solubilization of
HLA from cells, for use in applications disclosed or taught by
the art references such as for removal of anti-HLA class II
antibodies from a patient as is taught by [Hildebrand] (which
would require larger amounts of HLA molecules than for an
immunoassay) while avoiding contamination with human shed
HLA molecules by use of mouse APCs for expression of the
complexes.
Ans. 8.
Analysis
As stated in In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992):
[T]he examiner bears the initial burden . . . of presenting a
prima facie case of unpatentability. . . .
After evidence or argument is submitted by the applicant in
response, patentability is determined on the totality of the
record, by a preponderance of evidence with due consideration
to persuasiveness of argument.
Claim 1 is representative of the claims subject to this ground of
rejection. Having carefully considered the evidence and arguments
presented by Appellant and the Examiner, Appellant does not persuade us
that the Examiner’s conclusion of obviousness as to claim 1 is not supported
by a preponderance of the evidence.
Hildebrand discloses that “[b]ecause HLA molecules mediate most, if
not all, adaptive immune responses, and because of their tremendous
diversity, large quantities of individual HLA proteins are required in order to
effectively study transplantation, autoimmunity disorders, and for vaccine
development.” Hildebrand ¶ 11.
Pursuant to that objective, as the Examiner found, and Appellant does
not dispute, Hildebrand discloses a process in which a mouse antigen
presenting cell line, transformed with a nucleic acid vector encoding human
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HLA class II alpha and beta chains, is cultured to express trimolecular
complexes composed of the vector-encoded alpha and beta chains and an
associated endogenous antigen in properly glycosylated form, as recited in
Appellant’s representative claim 1. See Hildebrand ¶¶ 53–57 (describing
general process); id. ¶¶ 80–87 (Examples 1–3 describing expression of HLA
class II in mouse NS-1 cells).
Hildebrand explains that expressing human HLA proteins in mouse
cells simplifies the purification procedure. See Hildebrand ¶ 56 (“The
purification of HLA extracted from non-human cells will be much less
complex and require fewer purification steps because other competing
HLA/human proteins will not need to be subtracted or otherwise selected out
during the purification process. Purification of the selected HLA protein
will be simplified.”).
As to representative claim 1’s requirement for the trimolecular
complexes to be in soluble form, the Examiner finds that an application (US
11/591,118) incorporated by reference in Hildebrand describes preparing
HLA proteins in soluble form to avoid issues associated with detergent-
based methods of isolating the proteins from cell membranes. See Ans. 5–7.
Appellant did not enter a Reply Brief disputing the Examiner’s
findings as to Hildebrand’s incorporated disclosure of the desirability of
obtaining soluble HLA class II trimolecular complexes, nor does Appellant
otherwise assert error in the Examiner’s findings as to Hildebrand’s
incorporated disclosures. We note, moreover, that Hildebrand discloses that
it was desirable to isolate the expressed trimolecular complexes away from
the cells that produced them. See, e.g., Hildebrand ¶ 69 (“HLA trimolecular
complexes purified away from the non-human cells may be utilized.”); id. ¶
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72 (describing detection or removal of anti-HLA antibodies using
“functionally active, individual HLA trimolecular complex . . . directly or
indirectly linked to [a] substrate”).
Given Hildebrand’s teaching that it was desirable to isolate the
expressed trimolecular complexes away from the cells that produced them,
we agree with the Examiner that a skilled artisan had a good reason for
preparing Hildebrand’s trimolecular complexes in a soluble form, as recited
in Appellant’s representative claim 1. As to the other disputed limitation of
claim 1, we also agree with the Examiner that a skilled artisan would have
considered it obvious to configure the vectors encoding the alpha and beta
chains of the HLA II complexes to express leucine zipper domains.
Specifically, Kalandadze discloses that when expressing recombinant
HLA class II molecules (HLA-DR2) in host cells, expression of leucine
zipper domains on each of the alpha and beta chains, as recited in
Appellant’s claim 1, allows the alpha/beta dimers to be secreted in soluble
form. See Kalandadze 20161 (“Replacement of the hydrophobic
transmembrane regions by the Fos and Jun leucine zipper dimerization
motifs resulted in the assembly and secretion of αβ heterodimers, both in
Chinese hamster ovary [(CHO)] cells and in yeast [(Pichia pastoris)].”).
Kalandadze discloses, moreover, that the secreted alpha/beta dimers
efficiently incorporate antigenic peptides. See id. 20156 (“Kinetic and
quantitative peptide binding experiments demonstrated that recombinant
DR2 molecules [produced in P. pastoris] were efficiently loaded with an
antigenic peptide.”).
Thus, to summarize, Hildebrand taught that it was desirable to isolate
its expressed HLA class II trimolecular complexes away from the mouse
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cells that produced them, and Kalandadze taught that expression of leucine
zipper domains on each of the alpha and beta chains of HLA class II proteins
allowed the HLA II proteins to be secreted away from two species of host
cells, in a dimerized form capable of loading antigenic peptides. Given
these teachings, we agree with the Examiner that a skilled artisan had a good
reason for, and a reasonable expectation of success in, modifying the vector
encoding the alpha and beta chains of Hildebrand’s HLA II trimolecular
complexes to include a leucine zipper motif, as taught by Kalandadze. We
therefore also agree with the Examiner that the process recited in
Appellant’s representative claim 1 would have been prima facie obvious to a
skilled artisan.
Appellant’s arguments do not persuade us to the contrary. Appellant
contends that a skilled artisan would have lacked a no reasonable
expectation of combining Hildebrand and Kalandadze because Kalandadze
expressed empty alpha/beta heterodimers in yeast, which were loaded with
antigenic peptides after expression, whereas Hildebrand’s methods, like the
process of representative claim 1, require the alpha/beta heterodimers to be
loaded with an endogenous peptide when expressed. Appeal Br. 6.
Therefore, Appellant contends, a skilled artisan “would expect that
expressing the same leucine zipper-modified soluble HLA complexes in
another cell type, APCs [(antigen presenting cells)], would also express
empty HLA complexes, without loaded endogenous peptides.” Id.
The Examiner responds that, in addition to yeast, Kalandadze reported
producing secreted, leucine zipper-modified, alpha/beta heterodimers in
CHO cells, which are mammalian cells. Ans. 12. The Examiner reasoned,
moreover, that a skilled artisan would not have interpreted Kalandadze as
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describing expression of empty alpha/beta heterodimers as argued by
Appellant, but instead would have viewed Kalandadze’s secreted alpha/beta
heterodimers as being associated with lower affinity endogenous peptides.
See id. at 12–13.
Specifically, the Examiner reasoned that a skilled artisan would have
viewed Kalandadze’s secreted alpha/beta heterodimers as being associated
with endogenous peptides based on Kalandadze’s disclosure that lower
affinity peptides present in the yeast cell secretory pathway could readily be
exchanged for a higher affinity peptide. Ans. 13 (citing Kalandadze 20162).
The portion of Kalandadze cited by the Examiner reads as follows:
Availability of (low affinity) peptides in the secretory pathway
may be the limiting factor in the assembly of αβ heterodimers;
this may be overcome by coexpressing a DR-binding peptide in
the secretory pathway (under the control of the AOX1 promoter
as fusion with the α-mating factor secretion signal). The
invariant chain peptide (CLIP) may be suitable for this purpose
since it could be later exchanged with other DR2 binding
peptide(s).
Kalandadze 20162 (citation omitted)
Appellant did not enter a Reply Brief asserting error in the Examiner’s
interpretation of Kalandadze’s page 20162 as describing its secreted
alpha/beta heterodimers as being associated with endogenous peptides.
Therefore, the Examiner’s assertion in that regard is undisputed. Moreover,
given Kalandadze’s disclosure on page 20162 that its alpha/beta
heterodimers can be coexpressed with a heterodimer-binding peptide that
can later be exchanged with a higher affinity peptide, we discern no error in
the Examiner’s finding that Kalandadze suggests that, when making the
leucine zipper modification to alpha and beta chains of HLA class II
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molecules, the resulting secreted alpha/beta heterodimers are associated with
endogenously coexpressed antigenic peptides.
Thus, to summarize, Kalandadze suggests that when making the
leucine zipper modification to alpha and beta chains of HLA class II
molecules, the resulting secreted alpha/beta heterodimers are associated with
coexpressed antigenic peptides. Appellant does not persuade us, therefore,
that making the leucine zipper modification to Hildebrand’s HLA-encoding
vector as posited by the Examiner would have been expected to result in a
trimolecular complex lacking the endogenously produced peptide antigen
required by Hildebrand, and recited in Appellant’s representative claim 1.
Appellant also does not persuade us that the Wettstein7 reference
demonstrates that a skilled artisan would have lacked a reasonable
expectation in making Kalandadze’s leucine zipper modification to
Hildebrand’s HLA-encoding vector. See Appeal Br. 6–7 (citing Wettstein
220, 221, 225).
As the Examiner found, Wettstein describes a very different alteration
than Kalandadze’s leucine zipper modification; Wettstein modifies the alpha
and beta chains of the HLA molecule to include enzymatically cleavable
regions allowing release of the molecule in soluble form from the cell
surface. See Wettstein 219 (abstract). Appellant, moreover, identifies no
specific teaching in Wettstein relating to Kalandadze’s leucine zipper
modification, nor does Appellant identify in Wettstein any teaching that

7 Daniel A. Wettstein et al., Expression of a Class II Major
Histocompatibility Complex (MHC) Heterodimer in a Lipid-linked Form
with Enhanced Peptide/Soluble MHC Complex Formation at Low pH, 174 J.
EXP. MED. 219–228 (1991).
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explains specifically whether Kalandadze’s leucine zipper modification
would be expected to work in Hildebrand’s process. Nor does Appellant
identify any teaching in Wettstein suggest that any type of modification to
the alpha and beta chains of HLA class II molecules would eliminate loading
of endogenous peptides to recombinantly expressed alpha/beta heterodimers.
We acknowledge that, at least in one instance, Wettstein discloses that
a particular modification to the HLA molecules might affect the ability of
the expressed alpha/beta heterodimers to associate with endogenous
antigens. See Wettstein 225 (“Peptides generated by endogenous processing
of cytochrome c are available to Ek expressed in CHO cells, but not (or very
poorly) to GPI-linked Ek expressed in CHO cells, indicating that the
chimeric molecules are not treated as native molecules by the recipient
cells.”). Again, however, Wettstein’s modification is not the leucine zipper
modification described by Kalandadze and recited in Appellant’s
representative claim 1. As discussed above, Kalandadze suggests that
endogenously coexpressed peptides will be associated with leucine
zipper-modified alpha/beta heterodimers. See Kalandadze 20162.
Thus, even assuming that Wettstein somehow tangentially suggested
that Kalandadze’s leucine zipper modification might affect loading of
endogenous peptides into alpha/beta heterodimers, Kalandadze itself
provided at least a reasonable expectation that applying the leucine zipper
modification to Hildebrand’s process would result in alpha/beta
heterodimers associated with endogenous peptides as required by
Hildebrand, and as recited in Appellant’s representative claim 1. As our
reviewing court has explained, “[o]bviousness does not require absolute
predictability of success. . . . For obviousness under § 103, all that is
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required is a reasonable expectation of success.” In re Kubin, 561 F.3d
1351, 1360 (Fed. Cir. 2009) (quoting In re O’Farrell, 853 F.2d 894, 903–04
(Fed. Cir. 1988) (emphasis removed).
In sum, for the reasons discussed, Appellant does not persuade us that
a skilled artisan would have lacked a reasonable expectation of success in
combining Hildebrand and Kalandadze in the manner posited by the
Examiner. Appellant also does not persuade us that a skilled artisan would
have lacked motivation for combining Hildebrand and Kalandadze.
Specifically, Appellant does not persuade us that, because Hildebrand
described its process as successfully producing isolated HLA class II
trimolecular complexes, a skilled artisan would have lacked motivation for
modifying Hildebrand’s process to produce isolated trimolecular complexes.
See Appeal Br. 7 (asserting that evaluation of MHC/peptide/TCR interaction
and associated induced signals posited by Examiner as providing motivation
for making soluble complexes “could have been studied by analyzing the
HLA complexes expressed on the surface of the APCs as taught by
Hildebrand without introducing modified HLA complexes which may or
may not reflect what actually occurred with normal complexes”); see also id.
(“Hildebrand ’872 teaches that trimolecular complexes could be used to
successfully detect specific anti-HLA class II antibodies, and points to no
need for making the trimolecular complexes soluble as argued by the
Examiner. See Hildebrand ’872, at ¶¶ [0090]-[0095].”); id. at 8 (“[T]he
work was considered a success, and there would have been no need to go to
all the extra work of making the HLA molecules soluble when the current
process was already successful.” (citing Hildebrand ¶¶ 88-94)).
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We acknowledge Hildebrand’s disclosure in its examples of preparing
HLA class II trimolecular complexes on the surface of mouse NS-1 cells,
and then using the complexes isolated from the cells to screen for anti-HLA
antibodies. See Hildebrand ¶¶ 80–95.
At best, however, Appellant has shown only that Hildebrand’s process
differs from the process of Appellant’s representative claim 1 in that
Hildebrand does not employ the claimed leucine zipper modification. It is
well settled, however, that “the mere existence of differences between the
prior art and an invention does not establish the invention’s
nonobviousness.” Dann v. Johnston, 425 U.S. 219, 230 (1976).
Moreover, because Appellant’s arguments are directed to the alleged
deficiencies in the Hildebrand viewed in isolation, rather than in the
combination with Kalandadze advanced by the Examiner, Appellant’s
arguments are insufficient to demonstrate nonobviousness. See In re Merck
& Co., Inc., 800 F.2d 1091, 1097 (Fed. Cir. 1986) (“Non-obviousness
cannot be established by attacking references individually where the
rejection is based upon the teachings of a combination of references. . . .
[The reference] must be read, not in isolation, but for what it fairly teaches
in combination with the prior art as a whole”).
In the present case, as discussed above, Hildebrand taught that it was
desirable to isolate its expressed HLA class II trimolecular complexes away
from the mouse cells that produced them (see, e.g., Hildebrand ¶ 69), and
Kalandadze taught that expression of leucine zipper domains on each of the
alpha and beta chains of HLA class II proteins allowed the HLA II proteins
to be secreted away from two species of host cells, in a dimerized form
capable of loading antigenic peptides (see, e .g., Kalandadze 20161). Given
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these teachings, Appellant does not persuade that a skilled artisan lacked
motivation for modifying the vector encoding the alpha and beta chains of
Hildebrand’s HLA II trimolecular complexes to include a leucine zipper
motif, as taught by Kalandadze. In short, Kalandadze provided a way to
make molecules having properties considered desirable by Hildebrand.
Because the motivation for making the combination posited by the Examiner
comes from the references themselves, we are not persuaded that the
Examiner’s conclusion of obviousness is based on improper hindsight.
We are also unpersuaded by Appellant’s argument that modifying
Hildebrand’s process to include Kalandadze’s leucine zipper modification
would have yielded “unnecessary complexity [that] would run counter to the
teachings of Hildebrand ’872 which alleges, for example, that the methods
taught therein will make purification of HLA much less complex, and that
purification of the selected HLA protein will be simplified.” Appeal Br. 7
(citing Hildebrand ¶ 56).
As noted above, the simplification described by Hildebrand in its
process relates to the fact that recombinant production of human HLA
proteins in mouse cells makes purifying the human protein easier. See
Hildebrand ¶ 56 (“The purification of HLA extracted from non-human cells
will be much less complex and require fewer purification steps because
other competing HLA/human proteins will not need to be subtracted or
otherwise selected out during the purification process.” (emphasis added)).
Indeed, producing secreted trimolecular complexes, which undisputedly do
not require detergent-aided purification steps, as posited by the Examiner
(see Ans. 8) is consistent with Hildebrand’s suggestion that its purification
process be simplified.
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In sum, for the reasons discussed, Appellant does not persuade us that
the Examiner erred in determining that a skilled artisan had a reasonable
expectation of success in, and ample motivation for, combining Hildebrand
and Kalandadze in the manner posited by the Examiner. We therefore agree
with the Examiner that the process recited in Appellant’s representative
claim 1 would have been prima facie obvious to a skilled artisan. Because
Appellant does not advance any specific objective evidence of
nonobviousness that might outweigh the evidence of prima facie
obviousness presented by the Examiner, we affirm the Examiner’s rejection
of claim 1 over Hildebrand and Kalandadze. Claims 3, 5, 7, 12, 13, and 18–
21 fall with claim 1.
OBVIOUSNESS—
HILDEBRAND, KALANDADZE, AND RHODE
In rejecting claims 14 and 15, which depend from claims 1 and 5
discussed above, the Examiner cited Hildebrand and Kalandadze for the
teachings discussed above, and cited Rhode as evidence that the additional
features recited dependent claims 14 and 15 would have been obvious
variations of the process suggested by Hildebrand and Kalandadze. See
Final Act. 6; Ans. 9–10.
Appellant contends only that Rhode fails to remedy the deficiencies in
the combination of Hildebrand and Kalandadze, addressed above. See
Appeal Br. 8–9. As discussed above, we do not find the combination of
Hildebrand and Kalandadze deficient. Accordingly, for the reasons
discussed above, we affirm the Examiner’s rejection of claims 14 and 15
over Hildebrand, Kalandadze, and Rhode.

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OBVIOUSNESS—
HILDEBRAND, KALANDADZE, AND PRILLIMAN
In rejecting claims 14–17, all of which depend from either claim 1 or
5 discussed above, the Examiner cited Hildebrand and Kalandadze for the
teachings discussed above, and cited Prilliman as evidence that the
additional features recited dependent claims 14–17 would have been obvious
variations of the process suggested by Hildebrand and Kalandadze. See
Final Act. 7; Ans. 10–11.
Appellant contends only that Prilliman fails to remedy the deficiencies
in the combination of Hildebrand and Kalandadze, addressed above. See
Appeal Br. 9–10. As discussed above, we do not find the combination of
Hildebrand and Kalandadze deficient. Accordingly, for the reasons
discussed above, we affirm the Examiner’s rejection of claims 14 and 15
over Hildebrand, Kalandadze, and Prilliman.

CONCLUSION
In summary:
Claims
Rejected
35 U.S.C.
§
Reference(s)/Basis Affirmed Reversed
1, 3, 5, 7,
12, 13, 18–
21
103(a) Hildebrand,
Kalandadze
1, 3, 5, 7,
12, 13, 18–
21

14, 15 103(a) Hildebrand,
Kalandadze, Rhode
14, 15
14–17 103(a) Hildebrand,
Kalandadze,
Prilliman
14–17
Overall
Outcome
1, 3, 5, 7,
12–21

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TIME PERIOD
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