Anja C. Gemperli et al.

Patent Trials and Appeals Board

Jan 2, 2020

14787941 - (D) (P.T.A.B. Jan. 2, 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.
14/787,941 10/29/2015 Anja C. Gemperli 153-003 1089
36844 7590 01/02/2020
Cermak Nakajima & McGowan LLP
127 S. Peyton Street, Suite 200
Alexandria, VA 22314
EXAMINER
BRADLEY, CHRISTINA
ART UNIT PAPER NUMBER
1654
NOTIFICATION DATE DELIVERY MODE
01/02/2020 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):
ACERMAK@cnmiplaw.com
IP@cnmiplaw.com
USPTO@dockettrak.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte ANJA C. GEMPERLI and OLEH ANDRUKHOV1
Appeal 2018-004488
Application 14/787,941
Technology Center 1600
Before ERIC B. GRIMES, JOHN G. NEW, and JAMIE T. WISZ,
Administrative Patent Judges.
GRIMES, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134(a) involving claims to a
wound-healing composition, which have been rejected as lacking adequate
written description and as obvious. We have jurisdiction under
35 U.S.C. § 6(b).
We REVERSE.

1 Appellant identifies the real party in interest as Straumann Holding AG.
Appeal Br. 2. We use the word Appellant to refer to “applicant” as defined
in 37 C.F.R. § 1.42(a).
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Application 14/787,941

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STATEMENT OF THE CASE
“The present invention relates to the field of enamel matrix proteins
and to the use of them in wound healing. In particular, the invention relates
to the disclosure of a new active amelogenin polypeptide ((SEQ.ID.NO: 1)
TRAP 63) that in particular stimulates the tissue formation phase of a wound
healing process.” Spec. 1:3–6.
Claims 1, 3, 4, and 8–14 are on appeal. Claims 1 and 4 are illustrative
and reproduced below (emphasis added):
1. A pharmaceutical composition which stimulates the tissue
formation phase of a wound healing process, said composition
comprising a mixture of enamel matrix polypeptides and/or
proteins with a molecular weight < 8 kDa, wherein said mixture
is free of enamel matrix polypeptides and/or proteins with a
molecular weight > 8 kDa, and a suitable pharmaceutical
carrier, wherein said mixture comprises the enamel matrix
polypeptide of SEQ ID NO: 1 (TRAP63).

4. A pharmaceutical composition which stimulates the tissue
formation phase of a wound healing process, said composition
comprising an acid-extraction of enamel proteins and/or
polypeptides derived from developing mammalian tooth buds,
which is at least 2x enriched in an enamel matrix polypeptide
which has the amino acid sequence as shown in SEQ ID NO: 1
(TRAP63), or a pharmaceutically acceptable salt thereof.

The claims stand rejected as follows:
Claims 1, 3, and 8–14 under 35 U.S.C. § 112(a) as failing to comply
with the written description requirement (Ans. 3) and
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Claim 4 under 35 U.S.C. § 102(a)(1) as anticipated by, or alternatively
under 35 U.S.C. § 103 as obvious based on, Gestrelius2 as evidenced by
UniProt3 (Ans. 5).
OPINION
Written Description
The Examiner finds that claim 1 “has been amended to exclude all
enamel matrix polypeptides and/or proteins having a molecular weight
above 8 kDa,” and “the issue is whether or not the original disclosure
provided support specifically for mixtures that are completely free of all
enamel matrix polypeptides and/or proteins having a molecular weight
above 8 kDa.” Ans. 3–4.
The Examiner finds that “the amended claim scope is not supported
by express disclosure” because “the specification does not include the actual
language ‘free of enamel matrix polypeptides and/or proteins with a
molecular weight > 8 kDa’, the term ‘free’ in the context of protein
components, or terms equivalent to ‘free’ in the context of protein
components.” Id. at 4.
The Examiner also finds that the Specification exemplifies an “LMW
fraction,” which includes proteins with molecular weights below 8 kDa, but
“the specification presents data that suggests that proteins with a molecular
weight above 8 kDa are in fact present in the LMW fraction.” Id. The
Examiner points to Figures 9 and 10 as “clearly show[ing] that Fraction
LMW comprises polypeptides with molecular weights of approximately 12,

2 Gestrelius et al., US 2002/0169105 A1, published Nov. 14, 2002.
3 UniProt database, entry Q9TQY2_PIG (2000).
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15, and 20 kDa.” Id. The Examiner also points to the Specification’s
statements that the LMW fraction contained “significantly less” or
“insignificant amounts” of 20 kDa amelogenin protein, both of which
indicate that the LMW fraction is not “‘free of’ components with a
molecular weight above 8 kDa.” Id. at 4–5.
Appellant argues that, “although actual reduction to practice may
serve as evidence of possession, actual reduction to practice is not required.”
Appeal Br. 5. Appellant argues that, “[e]ssentially, the Examiner’s argument
is that the Examples in the specification do not evidence an actual reduction
to practice of the claimed invention. But this is not the standard. See, e.g.,
Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 926 (Fed. Cir.
2004).” Reply Br. 3. “Working examples are explicitly not required.” Id. at
4 (citing Falkner v. Inglis, 448 F.3d 1357 (Fed. Cir. 2006).)
Appellant also argues that “the specification as filed . . . describe[s] a
process for producing a composition that includes the step of ‘removing any
protein with a molecular weight (M.W.) ≥ 8 kDa from’ a preparation of
isolated enamel proteins.” Appeal Br. 7. Appellant argues that a composition
“from which proteins with a molecular weight ≥ 8 kDa have been removed,
is a literal description of a composition that does not include proteins with a
molecular weight > 8 kDa.” Id. at 7–8. Appellant thus argues that “the
inventors, at the time the application was filed, were in possession of the
claimed invention, if not in actual physical possession, then at least by
providing sufficient ‘[w]ords, structures, figures, diagrams, formulas, etc.,
that fully set forth the claimed invention.’ Lockwood v. American Airlines,
Inc., 107 F .3d 1565, 1572 (Fed. Cir. 1997).” Reply Br. 4–5.
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We agree with Appellant that the Specification satisfies the 35 U.S.C.
§ 112(a) requirement that the “description must ‘clearly allow persons of
ordinary skill in the art to recognize that [the inventor] invented what is
claimed.’” Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1351 (Fed.
Cir. 2010) (alteration in original). “In other words, the test for sufficiency [of
the written description] is whether the disclosure of the application relied
upon reasonably conveys to those skilled in the art that the inventor had
possession of the claimed subject matter as of the filing date.” Id.
“The term ‘possession,’ however, has never been very enlightening.”
Id. “[T]he written description requirement does not demand either examples
or an actual reduction to practice; a constructive reduction to practice that in
a definite way identifies the claimed invention can satisfy the written
description requirement.” Id. at 1352 (emphasis added). That is, based on
“the perspective of a person of ordinary skill in the art . . . the specification
must describe an invention understandable to that skilled artisan and show
that the inventor actually invented the invention claimed.” Id. at 1351.
Here, the Specification states that “[t]he enamel matrix is composed
of a number of proteins,” and “[e]namel matrix proteins and enamel matrix
derivatives (EMD) have previously been described in the patent literature to
be able to . . . promote open wound healing.” Spec. 2:5–8, 2:17. The
Specification describes Appellant’s invention as follows:
The present invention now for the first time discloses all
components of a newly identified low molecular weight
fraction of isolated enamel matrix derivatives that can clearly
be shown to be more effective in reducing the inflammatory
response in a targeted soft tissue than the complete enamel
matrix extract (EMD).
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Id. at 4:13–16. The Specification also states that “the invention relates to the
disclosure of a new active amelogenin polypeptide ((SEQ.ID.NO: 1) TRAP
63) that in particular stimulates the tissue formation phase of a wound
healing process.” Id. at 1:4–6. These passages identify Appellant’s invention
as being low molecular weight enamel matrix proteins, including TRAP 63,
that reduce inflammation and stimulate wound healing, as recited in claim 1.
The Specification also states that an aspect of the disclosed invention
is a process for producing a pharmaceutical composition, comprising
isolating enamel proteins from developing animal tooth buds, and “removing
any protein with a molecular weight (M.W.) ≥ 8 kDa from said isolate,” thus
producing “a pharmaceutical composition comprising proteins with a
molecular weight (M.W.) < 8 kDa, such as ≤ 7 kDa.” Id. at 6:24 to 7:2. This
passage identifies a molecular weight of 8 kDa, as recited in claim 1, as a
threshold for the “low molecular weight” enamel matrix proteins described
as part of the disclosed composition.
In our view, the Specification adequately describes the composition
defined by claim 1 in a manner that is understandable to a skilled artisan and
demonstrates that Appellant invented what is claimed. No more is required
to satisfy the written description requirement of 35 U.S.C. § 112(a). See
Ariad, 598 F.3d at 1351.
It is true, as the Examiner has pointed out, that the “LMW” fraction
characterized in the Specification’s working examples is not completely free
of proteins with molecular weights above 8 kDa. Figure 10, for example,
identifies one of the proteins in Fraction LMW as “Amelogenin (20 kDa).”
Claim 1, however, is not directed to “Fraction LMW,” or limited to
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compositions made by the same process. Claim 1 simply requires that the
composition be free of proteins above a molecular weight of 8 kDa, and the
Examiner has not shown that a skilled artisan would not have been able to
use conventional protein purification techniques to “remov[e] any protein
with a molecular weight (M.W.) ≥ 8 kDa from [an] isolate” of enamel
proteins, as described in the Specification (page 6).
We conclude that the Specification adequately describes the
composition of claim 1. We therefore reverse the rejection of claims 1, 3,
and 8–14 under 35 U.S.C. § 112(a).
Prior Art
The Examiner rejects claim 4 as anticipated by, or obvious based on,
Gestrelius with evidence provided by UniProt. The Examiner finds that
Gestrelius discloses “a pharmaceutical composition for wound healing . . .
comprising main protein bands at 20 kDa, 12–14 kDa and around 5 kDa.”
Ans. 6. The “composition may mainly or exclusively contain up to 70–90%
amelogenins with a molecular weight (MW) between 40,000 and 5,000
Daltons.” Id.
The Examiner finds that Gestrelius teaches that “the enamel matrix
may be obtained from . . . a mammal in which teeth are under development.
A suitable source is developing teeth from slaughtered animals such as, e.g.,
calves, pigs or lambs.” Id. The Examiner cites UniProt as evidence that
“[p]orcine amelogenin comprises an amino acid sequence that is identical to
instant SEQ ID NO: 1 (TRAP63) at positions 1–63.” Id.
The Examiner finds that Gestrelius teaches preparing its composition
by scraping off enamel matrix and “extraction with aqueous solution such as
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a buffer, a dilute acid or base or a water/solvent mixture, followed by size
exclusion, desalting or other purification steps, optionally followed by
freeze-drying.” Id. The Examiner concludes that
Gestrelius et al. explicitly teaches acid extraction, and a
composition having at least 2x enrichment in an enamel matrix
polypeptide (i.e. up to 70–90% amelogenins with a molecular
weight (MW) between 40,000 and 5,000 Daltons) (¶ [0105]),
which appears to meet all of the structural requirements of and
to anticipate the instant claim.
Id. In the alternative, the Examiner concludes that
it would have been obvious to use acid extraction of . . . a
mammal in which teeth are under development as taught by
Gestrelius et al., and in doing so one of ordinary skill in the art
would prepare a composition that is at least 2x enrich[ed] in an
enamel matrix polypeptide. The reference does not name a
polypeptide TRAP63 but the compositions disclosed in or
suggested by the reference would contain TRAP63.
Id. at 6–7.
Appellant argues that “Gestrelius teaches that the . . . proteins in the
mixture prepared therein ‘typically have a molecular weight of at the most
about 120 kDa such as, e.g., at the most 100 kDa, 90 kDa, 80 kDa, 70 kDa
or 60 kDa as determined by SDS Page electrophoresis.’” Appeal Br. 8
(quoting Gestrelius ¶ 95). “Such a composition would contain both the high
and low molecular weight proteins identified by the present inventors, and
would not be relatively enriched in TRAP63.” Id. at 9.
Appellant argues that, therefore, “Gestrelius does not inherently
describe a composition which meets the limitations of the present claims.
What is more, there is no teaching or suggestion in Gestrelius to use size
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exclusion to prepare a composition which is specifically enriched in the low
molecular weight material TRAP 63.” Id.
We agree with Appellant that the Examiner has not shown that the
composition of claim 4 is either anticipated by or obvious based on
Gestrelius as evidenced by UniProt. With respect to anticipation, the
Examiner has not provided evidence or sound technical reasoning to support
the conclusion that the composition described at ¶ 105 of Gestrelius—a
composition “up to 70–90% amelogenins with a molecular weight (MW)
between 40,000 and 5,000 Daltons” (Ans. 6)—is inherently “at least 2x
enriched in” TRAP63 relative to the starting material, as required by claim
4. See In re King, 801 F.2d 1324, 1326 (Fed. Cir. 1986) (“It is axiomatic that
anticipation of a claim under § 102 can be found only if the prior art
reference discloses every element of the claim.”).
With respect to obviousness, the Examiner has not shown that acid
extraction of enamel matrix from pig teeth, as suggested by Gestrelius,
inherently results in a composition that is at least two-fold enriched in
TRAP63, as claimed. “The inherent result must inevitably result from the
disclosed steps; ‘[i]nherency . . . may not be established by probabilities or
possibilities.’” In re Montgomery, 677 F.3d 1375, 1379–80 (Fed. Cir. 2012)
(citations omitted, alterations in original).
Nor has the Examiner shown that a skilled artisan would have had a
reason, based on the prior art or the knowledge of those skilled in the art, to
use “size exclusion, desalting, or other purification steps” (Gestrelius ¶ 88)
to produce a composition at least two-fold enriched in TRAP63.
“Obviousness requires more than a mere showing that the prior art includes
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. . . each separate limitation in a claim under examination.” Unigene Labs.,
Inc. v. Apotex, Inc., 655 F.3d 1352, 1360 (Fed. Cir. 2011). “Rather,
obviousness requires the additional showing that a person of ordinary skill at
the time of the invention would have selected and combined those prior art
elements in the normal course of research and development to yield the
claimed invention.” Id.
We therefore reverse the rejection of claim 4 as anticipated by, or
obvious based on, Gestrelius with evidence provided by UniProt.
DECISION SUMMARY
In summary:
Claims
Rejected
35 U.S.C. § Reference(s)/Basis Affirmed Reversed
1, 3, 8–14 112(a) Written Description 1, 3, 8–14
4 102(a)(1) Gestrelius, UniProt 4
4 103 Gestrelius, UniProt 4
Overall
Outcome
1, 3, 4, 8–
14

REVERSED