Ex Parte Valenta et al

Patent Trial and Appeal Board

Oct 25, 2012

11933498 (P.T.A.B. Oct. 25, 2012)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte RUDOLF VALENTA, SUSANNE VRTALA,
SABINE STUMVOLL, HANS GRONLUND, MONIKA GROTE,
LUCA VANGELISTA, ANNALISA PASTORE, WOLFGANG R. SPERR,
PETER VALENT, and DIETRICH KRAFT
____________

Appeal 2010-012465
Application 11/933,498
Technology Center 1600
____________

Before TONI R. SCHEINER, DONALD E. ADAMS, and
DEMETRA J. MILLS, Administrative Patent Judges.

ADAMS, Administrative Patent Judge.

DECISION ON APPEAL
This appeal under 35 U.S.C. § 134 involves claims 18-31 (App. Br. 2;
Ans. 2). We have jurisdiction under 35 U.S.C. § 6(b).
STATEMENT OF THE CASE
The claims are directed to a method for desensitization of a mammal
suffering from IgE mediated allergy (18-31). Claim 18 is representative and
is reproduced in the Claims Appendix of Appellants’ Brief.
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Claims 18-31 stand rejected under the written description provision of
35 U.S.C. § 112, first paragraph.
Claims 18-20 stand rejected under 35 U.S.C. § 102(a) as being
anticipated by Larché.
1

We reverse the written description rejection and affirm the
anticipation rejection.

Written Description:
ISSUE
Does the preponderance of evidence on this record support
Examiner’s conclusion that Appellants’ Specification fails to provide written
descriptive support for the claimed invention?
FACTUAL FINDINGS (FF)
FF 1. Appellants disclose a 138 amino acid sequence having the sequence
set forth in Appellants’ SEQ ID NO: 15 (see generally Ans. 5).
FF 2. Appellants disclose a modified Ph1 p 6 molecule having the
sequence set forth in Appellants’ SEQ ID NO: 18, which corresponds to a
N-terminal truncation (i.e. amino acids 59-138) of the Ph1 p 6 polypeptide
consisting of amino acids 29-138 of SEQ ID NO: 15 (id.).
FF 3. Appellants disclose a modified Ph1 p 6 molecule having the
sequence set forth in Appellants’ SEQ ID NO: 19, which corresponds to a
N-terminal truncation (i.e. amino acids 82-138) of the Ph1 p 6 polypeptide
consisting of amino acids 29-138 of SEQ ID NO: 15 (id.).
FF 4. Appellants disclose a modified Ph1 p 6 molecule having the
sequence set forth in Appellants’ SEQ ID NO: 20, which corresponds to a

1
Larché et al., WO 99/34826, published July 15, 1999.
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N-terminal truncation (i.e. amino acids 86-138) of the Ph1 p 6 polypeptide
consisting of amino acids 29-138 of SEQ ID NO: 15 (id. at 6).
FF 5. Appellants disclose a modified Ph1 p 6 molecule having the
sequence set forth in Appellants’ SEQ ID NO: 21, which corresponds to a C-
terminal truncation (i.e. amino acids 1-57) of the Ph1 p 6 polypeptide having
SEQ ID NO: 15 (id.).
FF 6. Appellants disclose a modified Ph1 p 6 molecule having the
sequence set forth in Appellants’ SEQ ID NO: 22, which corresponds to a C-
terminal truncation (i.e. amino acids 29-85) of the Ph1 p 6 polypeptide
consisting of amino acids 29-138 of SEQ ID NO: 15 (id.).
FF 7. Examiner finds that Appellants’ “C-terminally truncated Ph1 p 6 aa
1-57 corresponding to SEQ ID NO: 22 and amino acids 29-85 of SEQ ID
NO: 15) exhibits reduced IgE binding and does not induce histamine
release” (id. at 7).
FF 8. Examiner finds that Appellants’ N-terminal truncated Ph1 p 6
polypeptide having SEQ ID NO: 18 “exhibits reduced IgE binding[ and]
does not induce histamine release” (id. at 7-8).
FF 9. Examiner finds that Appellants’ N-terminal truncated Ph1 p 6
polypeptides having SEQ ID NOs: 19 and 20 that fall within the amino acid
range of Appellants’ SEQ ID NO: 18 “exhibit reduced IgE binding” (id. at
8).
FF 10. Examiner finds that Appellants “ha[ve] not adequately described a
correlation between the structure of the truncated Ph1 p 6 allergen and IgE
binding, IgG induction or histamine release” (id. at 9).
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FF 11. Examiner finds that Appellants disclose one example of a N-terminal
truncated Ph1 p 6 polypeptide, the polypeptide having SEQ ID NO: 18, “that
induces an IgG1 response in mice” (id.).
FF 12. Examiner finds that Appellants’ Specification fails to exemplify “a
C-terminally truncated or N- and C- terminally truncated Ph1 p 6
[polypeptide] that induces IgG in any mammal” (id.).
ANALYSIS
We recognize, but are not persuaded by Examiner’s intimation that
Appellants’ claimed invention lacks written descriptive support, because
Appellants’ Specification fails to establish the exact number of amino acids
that could be removed from the N- and/or C- terminus of a Ph1 p 6
polypeptide consisting of amino acids 29-138 of SEQ ID NO: 15 and still
meet the requirements of Appellants’ claimed invention (see Ans. 14-15; FF
10).
As Appellants explain, the Ph1 p 6 polypeptide of their claimed
invention “consists of 110 amino acids” and therefore, “the recited truncated
structures define a closed group of truncated molecules of defined structure”
(Reply Br. 4). Appellants further explain that they “have disclosed the
functions which must be exhibited by the claimed structures” and that they
“have correlated these functions to structure, namely the N-terminal
truncation and/or the C-terminal truncation” (id.; see also FF 1-9). “That
Appellants have not individually listed and tested each truncated molecule in
the finite set of molecules that satisfies … [their claims] does not mean that
the requirements of 35 U.S.C. § 112, first paragraph have not been met” (id.
at 5). We agree.
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“[E]xamples are not necessary to support the adequacy of a written
description[;] . . . the written description standard may be met . . . even
where actual reduction to practice of an invention is absent.” Falkner v.
Inglis, 448 F.3d 1357, 1366 (Fed. Cir. 2006). Examiner failed to provide
persuasive reasoning and/or an evidentiary basis on this record to support a
conclusion that Appellants’ Specification fails to provide written descriptive
support for the full scope of their claimed invention.
The same is true of Examiner’s concern that Appellants’ Specification
exemplifies only one modified Ph 1 p 6 polypeptide within the scope of
Appellants’ claimed invention “that induces IgG in any mammal” (FF 11-
12). Examiner does not dispute that Appellants’ Specification discloses
modified Ph1 p 6 molecules that (1) exhibit reduced IgE binding capacity as
compared with the Ph1 p 6 polypeptide and (2) are capable of raising an IgG
immune response in a mammal are required by Appellants’ claimed
invention (see, e.g., Appellants’ claim 18). Thus, it appears that Examiner’s
concern is that one example is not sufficient to support the genus that falls
within the scope of Appellants’ claimed invention. Examiner failed,
however, to provide persuasive reasoning and/or an evidentiary basis on this
record to support a conclusion that more than one example is necessary on
this record.
CONCLUSION OF LAW
The preponderance of evidence on this record fails to support
Examiner’s conclusion that Appellants’ Specification fails to provide written
descriptive support for the claimed invention. The rejection of claims 18-31
under the written description provision of 35 U.S.C. § 112, first paragraph is
reversed.
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Anticipation:
Does the preponderance of evidence on this record support
Examiner’s finding that Larché teaches Appellants’ claimed invention?
FACTUAL FINDINGS (FF)
FF 13. Larché “teaches a method of desensitization of a mammal …
suffering from IgE mediated allergy … using hypoallergenic immunogenic
molecules derived from … Ph1 p6” (Ans. 11).
FF 14. Larché’s desensitization methods do “not invoke IgE responses and
do[es] not lead to the release of histamine from basophils … [of] sensitize[d]
individuals” (id. at 11-12).
FF 15. Larché teaches the use of “Ph1 p6 molecules hav[ing] an N-terminal
deletion” (id. at 11).
FF 16. Larché teaches a sequence of Ph1 p 6 that is “100% identical to
[Appellants’] SEQ ID NO: 18[,] which corresponds to [amino acids] 59-138
of SEQ ID NO: 15” and therefore Larché teaches a sequence of Ph1 p 6 that
is a N-terminal truncated form of Ph1 p 6 polypeptide as required by
Appellants’ claim 18 (id.; Larché 65: 24-26).
ANALYSIS
The claims have not been argued separately and therefore stand or fall
together. 37 C.F.R. § 41.37(c)(1)(iv). Claim 18 is representative.
We are not persuaded by Appellants’ contentions that Larché
“provides no specific teaching relating to any Ph1 p 6 polypeptide
modification and particularly provides no teaching of how any of the Ph1 p 6
polypeptides set forth at pages 65-66 should be modified” and that Larché’s
“sequences at pages 65-66 … are disclosed only as starting points to identify
desired undisclosed peptides which may be arrived at by unspecified amino
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acid deletions, additions or substitutions, or other modifications” (App. Br.
20-21; Reply Br. 6-7). Larché’s Ph1 p 6 polypeptide consists of amino acids
59-138 of Appellants’ SEQ ID NO: 15; therefore, it is a N-terminal
truncation of the Ph1 p 6 polypeptide, as it is defined by Appellants’ claim
18 (i.e. a “polypeptide consisting of amino acids 29-138 of SEQ ID NO:
15”); and is encompassed by Larché’s disclosure of a modified peptide
antigen useful in “a method of desensitization of a mammal … suffering
from IgE mediated allergy … using hypoallergenic immunogenic molecules
derived from … Ph1 p6” (FF 13-16; Appellants’ claim 18).
For the foregoing reason we are not persuaded by Appellants’
contentions that their “claimed invention is not specifically disclosed in”
Larché or that Larché “employs a different mechanistic approach towards
desensitization and immunotherapy” (App. Br. 21-22; Reply Br. 6-8; Cf. FF
16 and FF 13-15). Notwithstanding Appellants’ unsupported contention to
the contrary, utilizing Larché sequence that corresponds to amino acids 59-
138 of Appellants’ SEQ ID NO: 15, in Larché’s method will result in the
desensitization of a mammal suffering from IgE mediated allergy by raising
an IgG immune response in the mammal. Appellants fail to establish an
evidentiary basis on this record to support a contrary conclusion.
CONCLUSION OF LAW
The preponderance of evidence on this record supports Examiner’s
finding that Larché teaches Appellants’ claimed invention. The rejection of
claim 18 under 35 U.S.C. § 102(b) as being anticipated by Larché is
affirmed. Claims 19 and 20 are not separately argued and fall together with
claim 18. 37 C.F.R. § 41.37(c)(1)(iv).
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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-IN-PART

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