Ex Parte Raats et al

Patent Trial and Appeal Board

Sep 26, 2016

12737075 (P.T.A.B. Sep. 26, 2016)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR
121737,075 12/01/2010 Jozef Maria Hendrik Raats
24247 7590 09/28/2016
TRASKBRITT, P,C
P.O. BOX 2550
SALT LAKE CITY, UT 84110
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
ATTORNEY DOCKET NO. CONFIRMATION NO.
3403-Pl0291US 7095
EXAMINER
EWOLDT, GERALD R
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
09/28/2016 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):
USPTOMail@traskbritt.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte JOZEF MARIA HENDRIK RAATS and
RENATO GERARDUS SILVANO CHIRIVI1
Appeal2014-002022
Application 12/737,075
Technology Center 1600
Before JEFFREY N. FREDMAN, ULRIKE W. JENKS, and
JACQUELINE T. HARLOW, Administrative Patent Judges.
JENKS, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims directed to a
method of treating arthritis. The Examiner rejects the claims as lacking
enablement. We have jurisdiction under 35 U.S.C. § 6(b).
We affirm.
1 According to Appellants, the Real Party in Interest is MODIQUEST B.V.
(Br. 2.)
Appeal2014-002022
Application 12/737,075
STATEMENT OF THE CASE
Claims 1, 5, 6, and 33-35 are on appeal, and can be found in the
Claims Appendix of the Appeal Brief (Br. 14). Claim 1 is representative of
the claims on appeal, and reads as follows:
1. A method of treating arthritis in a subject diagnosed with
arthritis, the method comprising:
administering to the subject an antibody that binds a
citrullinated epitope on a peptide selected from the group
consisting of SEQ ID N0:21, SEQ ID N0:24, SEQ ID
N0:26. [sic] SEQ ID N0:37, and SEQ ID N0:38.
Appellants request review of the Examiner's rejection of claims 1, 5,
6, and 33-35 under 35 U.S.C. § 112, first paragraph as lacking an enabling
disclosure for the full breadth of the claims.
Issue
The Examiner rejected the claims because the Specification provides
insufficient guidance to enable a person of ordinary skill in the art to practice
the full scope of the claimed invention without undue experimentation. The
Examiner has conceded that the Specification discloses methods of treating
rheumatoid arthritis (RA) using the RhmAb2.102 antibody (Ans. 9; see infra
FF2-FF5). However, the Examiner notes that the Specification "provides no
evidence that even the entire intact RhmAb2 .102 antibody would effectively
bind the unrelated peptides of SEQ ID NOs: 21, 24, 26, 3 7, and 3 8 and
effectively treat all types of unrelated arthritidae" (Ans. 8-9; see infra FF2
and FF3). The Examiner concludes that the Specification is not enabling for
the full scope of the claims because its guidance is limited to the
RhmAb2.102 antibody (Ans. 9; see infra FF3 and FF4).
2
Appeal2014-002022
Application 12/737,075
Appellants contend that "the skilled artisan has multiple years of
experience in creating antibodies and testing their functionality" (Br. 10),
that the Specification "provide[ s] guidelines for the creation of antibodies
useful in the claimed methods" (id.), that multiple antibodies were indeed
generated (id.), and that Appellants have shown that antibody RhmAb2.102
abolished clinical signs of arthritis when administered (id. at 11 ).
The issue is: Does the preponderance of evidence of record support
the Examiner's conclusion that the Specification lacks an enabling
disclosure for using the claimed genus of antibodies for treating arthritis?
Findings of Fact
FF 1. The Specification provides that "citrullinated peptides were
immunoprecipitable from the inflamed forepaws of affected mice
using human monoclonal antibody 102 (RhmAb2.102)" (Spec. iJ 102).
"Citrulline is an amino acid that is not incorporated into proteins
during translation, however, it can be generated by post-translational
modification of an arginine residue by peptidylarginine deiminase
(PAD)" (Spec.2 iJ 37).
FF2. Antibody RhmAb2. l 02 recognizes both the fibrinogen B peptide
(SEQ ID N0:37; see Ans. 5); mouse vimentin peptide (Spec. iii! 100
and 101); human plasma fibrinogen (Spec. iJ 157; see Ans. 5); SEQ ID
N0:2 l (Spec. iJ 96; Ans. 5), histone cluster 2, H4b, alpha 2 actin,
junction plakoglobin, beta actin, desmoplakin isoform I, homerin,
heterogeneous nuclear ribonucleoprotein U isoform a, heat shock
70kDa protein 6 (HSP70B '), annexin A2 isoform 1, cell surface
2 All references are made to the Substitute Specification submitted May 24,
2013 (see Br. 6).
3
Appeal2014-002022
Application 12/737,075
heparin-binding protein HIP, heterogeneous nuclear ribonucleoprotein
C isofonn b, neurofilament, heavy polypeptide 200kDa, ribosomal
protein L29, heat shock 70kDa protein 8 isoform 1, eukaryotic
translation elongation factor 1 alpha 1, dermcidin preproprotein,
albumin precursor, nuclease sensitive element binding protein 1
(Spec. ii 174, table 7; see Ans. 5).
FF3. According to the Specification, "human monoclonal antibodies
RhmAb2. l 04 and RhmAb2. l 05 reduced the clinical signs of arthritis
in the experimental CAIA [(collagen antibody induced arthritis)]
model, whereas RhmAb2.103, RhmAb2.102 and RhmAb2.107 even
abolished the clinical signs of arthritis in the experimental CAIA
model" (Spec. ii 68; see ii 135).
FF4. According to the Specification, "RhmAb2.103 and RhmAb2.102
performed identical" (Spec. ii 69). "RhmAb2. l 02 resulted in highest
anti-inflammatory effect. When examining the mean arthritis score of
hind paws only, RhmAb2. l 02, RhmAb2. l 05 and RhmAb2. l 07 all
performed similar in respect to anti-inflammatory effect" (Spec. ii 24).
FF5. RhmAb2.102 contains
[t]he immunoglobulin heavy chain encoded by SEQ ID N0:8
comprises a mouse leader globulin according to SEQ ID
NO: 12, followed by the variable antibody heavy chain
according to SEQ ID NO: 13, followed by the immunoglobulin
constant domain human IgG 1 according to SEQ ID NO: 14.
The immunoglobulin light chain encoded by SEQ ID N0:9,
comprises a mouse leader globulin according to SEQ ID NO:
12, followed by the variable antibody light chain according to
SEQ ID NO: 15 followed by the immunoglobulin human
lambda constant domain according to SEQ ID NO: 16
(Spec. ii 128).
4
Appeal2014-002022
Application 12/737,075
Analysis
After considering the evidence and the arguments, we conclude the
weight of the evidence favors the Examiner's conclusion that the
Specification lacks an enabling disclosure for the full breadth of the claims
as currently presented. Accordingly, we adopt the Examiner's reasoning
(see Grounds of Rejection, Ans. 3-6), and agree that the Examiner properly
found Appellants' arguments unpersuasive (see Response to Argument, Ans.
6-9). We provide the following points for emphasis.
A rejection for lack of enablement is appropriate when either the
written description does not enable the full scope of the claims, or where the
description does not enable any subject matter with the claim scope. In re
Cortright, 165 F.3d 1353, 1356 (Fed. Cir. 1999). Here, the Examiner rejects
the claims as lacking support for (1) the full scope of arthritidae claimed and
(2) as lacking sufficient "evidence that even the entire intact RhmAb2.102
antibody would effectively bind the unrelated peptides of SEQ ID N Os:2 l,
24, 26, 37, and 38 and effectively treat all types of unrelated arthritidae"
(Ans. 8-9). "While every aspect of a generic claim certainly need not have
been carried out by an inventor, or exemplified in the specification,
reasonable detail must be provided in order to enable members of the public
to understand and carry out the invention. That requirement has not been
met in this specification" with regard to treating the genus of arthritidae
claimed (see Br. 14, claim 1 ), based on the claimed citrullinated epitopes of
SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 37, and
SEQ ID NO: 38 (id.) See Genentech, Inc. v. Novo NordiskA/S, 108 F.3d
1361, 1366 (Fed. Cir. 1997).
5
Appeal2014-002022
Application 12/737,075
Appellants contend that "the skilled artisan has multiple years of
experience in creating antibodies and testing their functionality" (Br. 10),
and that the Specification "provide[ s] guidelines for the creation of
antibodies useful in the claimed methods" (id.).
We are not persuaded by Appellants contentions and agree with the
Examiner that the guidance provided by the Specification, even when
combined with the existing knowledge of those skilled in the art, is
inadequate to enable a skilled artisan to practice the full scope of the claimed
methods without undue experimentation. There is no dispute that the artisan
would know how to make and select antibodies to a particular protein
sequence. The dispute lies in the lack of disclosure in the Specification
showing that an antibody that selectively binds any of the claimed sequences
would necessarily function to treat arthritis. As pointed out by the
Examiner, the disclosed RhmAb2.102 antibody binds to a lot of other
sequences (FF2). Thus, antibody binding to SEQ ID N0:37 is not
sufficiently informative to show that producing other antibodies that bind to
this sequence, or the other sequences listed in the claim, will have the same
effect as the RhmAb2 .102. In other words, the Specification does not
provide a sufficient teaching that correlates the RhmAb2. l 02 antibodies
reactivity to SEQ ID N0:37 to treatment of rheumatoid arthritis (RA), let
alone the genus of arthritidae.
Appellants contend that multiple antibodies were generated that were
shown to be effective at treating arthritis (Br. 10).
We are not persuaded. Even though the Specification discloses the
production of multiple antibodies that are initially derived from the
autoantibody repertoires of RA patients, the final antibodies produced by the
6
Appeal2014-002022
Application 12/737,075
method in the Specification did not all function equally (Spec. iJ 125). In
other words, not all antibodies derived using the same process as disclosed
in the Specification are effective for the claimed treatment method (see
Spec. Fig. 1 C). And, as pointed out by the Examiner, the Specification does
not establish that the "treatment was [indeed] effected through the binding of
the peptide sequences of SEQ ID NOs:21, 24, 26, 37, and 38 as claimed"
(Ans. 7). Accordingly, we agree with the Examiner's position that the
amount of experimentation required to practice the full scope of the
invention would be undue.
Additionally, the claims are directed to the use of antibodies in a
treatment method wherein the antibodies bind a peptide having the following
sequences SEQ ID N0:21, SEQ ID N0:24, SEQ ID N0:26, SEQ ID N0:37,
and SEQ ID N0:38. We agree with the Examiner's position that the
Specification does not disclose that the RhmAb2. l 02 antibodies bind to each
of the claimed sequences (Ans. 7). Thus, the disclosure of the RhmAb2.102
antibody does not provide support for the effect through the binding of
antibodies to these sequences. Even though the RhmAb2 .102 antibody is
shown to be reactive with SEQ ID N0:37, the problem is that this is not the
only protein that this antibody reacts with, therefore, there is no correlation
between the binding of the antibody with the peptide to an effect of treating
any disease (FF2).
Appellants contend that antibody "RhmAb2. l 02 abolished clinical
signs of arthritis when administered" to animals and conclude that if any
additional experimentation is required the amount of such experiments
would not be "undue" (Br. 11 ).
7
Appeal2014-002022
Application 12/737,075
We are not persuaded. The Examiner explains that the Specification
"discloses only that the administration of the RhmAb2. l 02 to experimental
animals with CAIA was 'surprisingly' effective in the treatment of CAIA"
(Ans. 7). What is not made clear in the Specification is that the treatment is
through the binding of the antibody to the recited peptides (see Ans. 7). As
explained by the Examiner, the CAIA is considered a model for rheumatoid
arthritis (RA), it is not clear how this model is "considered to b[ e] enabling
for unrelated arthitidae such as osteoarthritis," psoriatic arthritis, and
juvenile idiopathic arthritis as claimed (Ans. 6).
Appellants contend that the Examiner has recognized "that CAIA is
an art recognized model for rheumatoid arthritis" therefore claim 6 is
enabled (Br. 12). With respect to claims 34, and 35, Appellants contend that
the Specification teaches that RhmAb2. l 02 is effective for treating arthritis
and that this antibody contains "SEQ ID NO: 13 and 15" (Br. 12).
We are not persuaded. Here, claims 6, 34, and 35 each depend on
claim 1, and as discussed above claim 1 is not enabled for the use of
antibodies directed to the list of sequences as explained by the Examiner.
SUMMARY
We affirm the rejection of claim 1under35 U.S.C. § 112, first
paragraph as lacking enablement for the full scope as claimed. Claims 5, 6,
and 33-35 were not separately argued and fall with claim 1. 37 C.F.R.
§ 41.37(c)(l)(iv).
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § l.136(a).
AFFIRMED
8