Olivier Kitten

Patent Trials and Appeals Board

Jul 17, 2019

14786287 - (D) (P.T.A.B. Jul. 17, 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.
14/786,287 10/22/2015 Olivier Kitten 085416-546576 6253
23416 7590 07/17/2019
POLSINELLI PC
(DE OFFICE)
1000 Louisiana Street
Fifty-Third Floor
HOUSTON, TX 77002
EXAMINER
BRADLEY, CHRISTINA
ART UNIT PAPER NUMBER
1654
NOTIFICATION DATE DELIVERY MODE
07/17/2019 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):
DC-IPdocketing@polsinelli.com
uspt@polsinelli.com
PTOL-90A (Rev. 04/07)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte OLIVIER KITTEN
(APPLICANTS: AFFILOGIC)
____________

Appeal 2019-002105
Application 14/786,2871
Technology Center 1600
____________

Before DONALD E. ADAMS, DEBORAH KATZ, and
JOHN E. SCHNEIDER, Administrative Patent Judges.

ADAMS, Administrative Patent Judge.

DECISION ON APPEAL
This Appeal under 35 U.S.C. § 134(a) involves claims 1, 3, 4, and 7–
16 (Final Act.2 2; App. Br. 2). Examiner entered a rejections under the
written description provision of 35 U.S.C. § 112(a) and 35 U.S.C. § 103.
We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.

1 Appellant identifies “AFFILOGIC” as the real party in interest
(Appellant’s July 27, 2018 Appeal Brief (App. Br.) 2 (emphasis omitted)).
2 Examiner’s March 28, 2018 Final Office Action.
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STATEMENT OF THE CASE
Appellant’s disclosure “relates to the field of the preparation of topical
compositions for cosmetic or therapeutic use, containing active ingredients
which bind to targets of interest” (Spec.3 1:3–6). Claim 1 is representative
and reproduced below:
1. A dermatological composition comprising a variant of a
wild-type OB-fold protein, said variant having between 5 and
20 mutated residues in the interface of binding of said wild-type
OB-fold protein to its natural ligand, wherein said wild-type
OB-fold protein is selected from the group consisting of Sac7d
or Sac7e derived from Sulfolobus acidocaldarius, Ss07d
derived from Sulfolobus solfataricus, DBP 7 derived from
Sulfolobus tokodaii, Ssh7b derived from Sulfolobus shibatae,
Ssh7a derived from Sulfolobus shibatae, and p7ss derived from
Sulfolobus solfataricus, and wherein said mutated residues are
selected from the group consisting of V2, K3, K5, K7, Y8, K9,
G10, E14, T17, K21, K22, W24, V26, G27, K28, M29, S31,
T33, D36, N37, G38, K39, T40, R42, A44, S46, E47, K48,
D49, A50 and P51 of Sac7d.
(App. Br. 18.)

Grounds of rejection before this Panel for review:
Claims 1, 3, 4, and 7–16 stand rejected under the written description
provision of 35 U.S.C. § 112(a).
Claims 1, 3, 4, and 7–16 stand rejected under 35 U.S.C. § 103 as
unpatentable over the combination of Binz4 and Pecorari.5

3 Appellant’s October 22, 2015 Specification.
4 Binz et al., US 2011/0207668 A1, published Aug. 25, 2011.
5 Pecorari et al., US 2010/0145008 A1, published June 10, 2010.
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WRITTEN DESCRIPTION:
ISSUE
Does the preponderance of evidence on this record support
Examiner’s finding that Appellant’s Specification fails to provide written
descriptive support for the claimed invention?
FACTUAL FINDINGS (FF)
FF 1. Examiner finds that Appellant’s “claims are . . . very broad and
encompass several wild-type OB-fold protein sequences, which are in turn
mutated at 5 to 20 positions [in] the binding interface” (Final Act. 4).
FF 2. Examiner finds that “[a]lthough a claim limitation requiring 5 to 20
mutations out of 66 may appear limited, the actual number of amino acid
sequences meeting this requirement is enormous, even considering that the
mutations must occur at the binding interface and not simply at any of the 66
residues” (Final Act. 4; see generally id. at 4–6).
FF 3. Examiner finds that “[t]he prior art teaches that there is a high degree
of unpredictability associated with skin permeability of proteins” (Final Act.
9 (citing Huang6 and Kalluri7)).
FF 4. Huang discloses that “[p]rotein drugs, due to their large size and
hydrophilic nature, are normally precluded from effective delivery such as
cell entry or tissue diffusion” and “naturally occurring proteins with skin
penetrating ability rarely exist” (Huang, Abstract; see generally Final Act.
9–10).

6 Dr. Yongzhuo Huang et al., Synthetic Skin-Permeable Proteins Enabling
Needleless Immunization, 49 ANGEW CHEM INT ED ENGL. 2724–27 (2010).
7 Haripriya Kalluri et al., Transdermal Delivery of Proteins, 12 AAPS
PARMSCITECH 431–41 (2011).
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FF 5. Kalluri discloses that because “proteins have a large size and are
hydrophilic in nature, they cannot permeate passively across the skin due to
the stratum corneum which allows the transport of only small lipophilic drug
molecules” (Kalluri, Abstract; see generally Final Act. 10).
FF 6. Examiner finds that “with respect to molecular weight and size, the
species reduced to practice [in Appellant’s Specification] are representative
of the genus” (Ans. 17).
ANALYSIS
Examiner finds that “Appellant . . . failed to disclose the amino acid
sequence of the species reduced to practice” and, therefore, “it is impossible
to know whether the species have a wide range of hydrophilicities, or
whether the species have similar hydrophilicities” (Ans. 17–18; see also
Final Act. 10 (Appellant’s Specification does not “disclose the degree of
hydrophilicity of the species reduced to practice” therein)). In this regard,
Examiner asserts that although “Appellant has evidenced that the species
reduced to practice can cross the skin barrier . . ., and that the genus
maintains the OB-fold topology even when mutate,” Appellant “has not
provided facts or data to demonstrate that this function is necessarily
attributable to the conserved fold[ing]” of the OB-protein (Ans. 18).
Therefore, Examiner finds that given “the enormous scope of sequences
included in [Appellant’s] claims, it is not reasonable to expect that all
species that meet the structural requirements of the claims will be permeable
to the skin or cornea” and Appellant’s Specification “fails to fill the gap
between permeability and structure in part because it does not describe the
physical and chemical properties of OB-fold variants that possess this
function and which could be used to distinguish OB-fold variants capable of
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being administered topically from those that are [skin] impermeable” (Final
Act. 10; see id. at 11 (Appellant’s Specification “does not describe a general
correlation between structure and function for the claimed genus”).
We are not persuaded.
Kitten declares that although “[t]he paradigm in the art is that
molecules of a size larger than 500 Da are not able to cross the skin barrier,”
“the Sac7d variant proteins [within the scope of Appellant’s claims] are able
to cross the skin barrier despite their large size due to their specific compact
folding” and this was confirmed by the examples presented in Appellant’s
Specification, which were “personally supervised” by Kitten (see First
Kitten Decl.8 ¶¶ 9–10). In this regard, Kitten explains that the modifications
required by Appellant’s claims “are located in the binding site of the
proteins” and “[c]onsequently, even though there might be many possible
variants, these [variants] would all present the same configuration [because]
the amino acids that determine the scaffold configuration remain
unchanged” (First Kitten Decl. ¶ 11; see id. (Kitten declares “what is
important is not the amino acids that have changed, but the amino acids that
remain unchanged and are responsible for the topology of the protein.
Consequently, the variants shall all present the same topology”); see also id.
¶ 12 (“the fact that a few variants of Sac7d proteins were able to cross the
skin barrier indicates that all proteins that share sequence and topology
homology would be able to cross the skin barrier”); Second Kitten Decl.9
¶¶ 11–12).

8 Declaration of Olivier Kitten, signed January 24, 2018 (“First Kitten
Decl.”).
9 Declaration of Olivier Kitten, signed July 5, 2017 (“Second Kitten Decl.”).
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Examiner’s assertion that Appellant “has not provided facts or data to
demonstrate that [skin permeation] is necessarily attributable to the
conserved fold[ing]” of the OB-protein is not persuasive in view of
Appellant’s declaratory evidence (see Ans. 18). In addition, for the reasons
set forth in the Kitten declarations, we are not persuaded that Examiner’s
reliance on Huang and Kalluri supports a finding that the modifications to
wild-type OB-fold protein that are required by Appellant’s claimed
invention will necessarily result in a protein that will be incapable of
permeating skin (FF 3–5).
CONCLUSION
The preponderance of evidence on this record fails to support
Examiner’s finding that Appellant’s Specification fails to provide written
descriptive support for the claimed invention. The rejection of claims 1, 3,
4, and 7–16 under the written description provision of 35 U.S.C. § 112(a) is
reversed.

OBVIOUSNESS:
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness?
FACTUAL FINDINGS (FF)
FF 7. Pecorari discloses
the use of an OB-fold protein, as a starting molecule for
obtaining, through a combinatorial mutation/selection approach,
a molecule specifically binding to a target, especially to a target
to which the starting OB-fold protein does not bind, i.e., to a

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target different form the target of the OB-fold protein used as
the starting molecule.
(Pecorari ¶ 7; see generally Final Act. 17; Ans. 13.)
FF 8. Pecorari discloses that Sac7d as an example of an OB-fold protein
within the scope of its invention (Pecorari ¶ 8; see also id. ¶ 11; see
generally Final Act. 17).
FF 9. Pecorari discloses a protein comprising modifications to 5 to 32,
preferably 8 to 20, and more preferably 11 to 16 residues of the binding
interface of an OB-fold protein (Pecorari ¶ 10; see general Final Act. 17;
Ans. 13).
FF 10. Using the sequence of Sac7d, as disclosed in Pecorari’s SEQ ID No:
1 as a reference, Pecorari discloses the specific amino acid residues of OB-
fold protein that “can be randomized are . . .: V2, K3, KS, K7, Y8, K9, G10,
E14, T17, K21, K22, W24, V26, G27, K28, M29, S31, T33, D36, N37, G38,
K39, T40, R42, A44, S46, E47, K48, D49, A50 and P51” (Pecorari ¶ 12; see
also id. ¶¶ 62–79 (disclosing, inter alia, the production, analysis, screening
and purification of mutated Sac7d OB-fold protein); id. ¶ 99 (discloses the
design of a Sac7d OB-fold protein, wherein “the substitution strategy
focused on the eleven residues in . . . [the binding surface] of Sac7d (K7,
Y8, K9, W24, V26, M29, S31, T33, R42, A44, S46)”); see generally Final
Act. 17–18; Ans. 13).
FF 11. Pecorari discloses that purified proteins can “be concentrated up to
60 mg/ml in a standard TBS buffer with no sign of precipitation and
remained soluble over several months at 4º C (Pecorari ¶ 109; see generally
Final Act. 17–18; Ans. 13; see generally Spec. 8: 34 – 9: 1 (Appellant
discloses that “[t]he for of the topical composition according to the invention
is conventional” and “may be in a liquid form”)).
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ANALYSIS
The dermatological composition of Appellant’s claim 1 comprises a
variant of a wild-type OB-fold protein, such as Sac7d, that has between 5
and 20 mutated residues in the binding interface, relative to the wild-type
OB-fold protein, wherein the mutated residues are selected from the group
consisting of V2, K3, K5, K7, Y8, K9, G10, E14, T17, K21, K22, W24,
V26, G27, K28, M29, S31, T33, D36, N37, G38, K39, T40, R42, A44, S46,
E47, K48, D49, A50, and P51 of Sac7d (see App. Br. 18).
Pecorari discloses a mutated OB-fold protein, such as Sac7d, that
comprises modifications to 5 to 32 residues of the binding interface of an
OB-fold protein (see FF 7–9). In addition, Pecorari discloses that the
residues of Sac7d that are available for modification are the same residues
set forth in Appellant’s claim 1 (see FF 10; cf. App. Br. 18). Pecorari further
discloses compositions comprising purified proteins in buffer (FF 11).
Absent evidence to the contrary, a mutated Sac7d OB-fold protein within the
scope of Pecorari’s disclosure that is in buffer reads on a dermatological
composition, i.e. a composition that may be applied topically to skin.
Therefore, we find no error in Examiner’s conclusion that a person of
ordinary skill in this art, at the time Appellant’s invention was made, would
have found the dermatological composition of Appellant’s claim 1, prima
facie obvious in view of the combination of Binz and Pecorari.10
As discussed above, Pecorari discloses purified proteins in buffer (FF
11). In addition, we find no administration step in Appellant’s claim 1.

10 The Board may rely upon less than all the references cited by the
Examiner. See In re May, 574 F.2d 1082, 1090 (CCPA 1978); In re Kronig,
539 F.2d 1300, 1304 (CCPA 1976).
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Therefore, absent evidence to the contrary, a composition comprising a
mutated Sac7d OB-fold protein within the scope of Pecorari’s disclosure in
buffer reads on a dermatological composition, i.e. a composition that may be
applied topically to skin, with the scope of Appellant’s claimed invention
(see generally FF 11). Therefore, we are not persuaded by Appellant’s
contention that the prior art relied upon by Examiner “does not properly
account for a dermatological composition” (App. Br. 12; see also id. at 13
(“Pecorari does not teach or suggest that the OB-fold proteins can (or
should) be administered topically, let alone dermatologically”); see
generally id. at 14).
Appellant’s claim 1 does not require a protein to penetrate skin (see
id. at 18). Therefore, we are not persuaded by Appellant’s contentions
regarding skin penetration (see id. (citing Huang and Kalluri); see also
Reply Br. 2–3). Appellant’s contention is also not persuasive because
Pecorari suggests compositions within the scope of Appellant’s claim 1,
such as a Sac7d OB-fold protein that has been modified at 5 residues
selected from the group consisting of V2, K3, K5, K7, Y8, K9, G10, E14,
T17, K21, K22, W24, V26, G27, K28, M29, S31, T33, D36, N37, G38,
K39, T40, R42, A44, S46, E47, K48, D49, A50, and P51 of Sac7d (see FF
7–11). “From the standpoint of patent law, a compound and all of its
properties are inseparable; they are one and the same thing.” In re Papesch,
315 F.2d 381, 391 (CCPA 1963). Thus, absent evidence to the contrary,
Pecorari’s composition will exhibit the same properties as Appellant’s
claimed composition.
For the foregoing reasons, we are not persuaded that Kitten’s
statement “that molecules of a size larger than 500 Da are not able to cross
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the skin barrier,” but “Sac7d variant proteins are able to cross the skin
barrier despite their large size due to their specific compact folding”
supports a conclusion of non-obviousness (see First Kitten Decl. ¶ 10; see
also App. Br. 14–15). For the same reasons, we are not persuaded that
Kitten’s statement that “[t]he fact that the claimed variants of Sac7d are able
to cross the skin could not have been expected or predicted based on the data
reported in Binz and in Pecorari” supports a conclusion of non-obviousness
(see Second Kitten Decl. ¶ 13; see also App. Br. 15). To be clear, the “mere
recognition of . . . latent properties [of a prior art composition] does not
render the otherwise obvious [invention] unobvious.” In re Prindle, 297
F.2d 251, 254 (CCPA 1962); see also Ex parte Obiaya, 227 USPQ 58, 60
(BPAI 1985) (“The fact that appellant has recognized another advantage
which would flow naturally from following the suggestion of the prior art
cannot be the basis for patentability when the differences would otherwise
be obvious”).
For the foregoing reasons, we are not persuaded by Appellant’s
contention that because the protein within Appellant’s claimed
dermatological composition is able to penetrate skin, the claimed
dermatological composition exhibits an unexpected result (see App. Br. 15–
16; see also Reply Br. 2–3).
CONCLUSION
The preponderance of evidence relied upon by Examiner supports a
conclusion of obviousness. The rejection of claim 1 under 35 U.S.C. § 103
as unpatentable over the combination of Binz and Pecorari is affirmed.
Claims 3, 4, and 7–16 are not separately argued and fall with claim 1.

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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