Ex Parte Carmeliet et al

Patent Trial and Appeal Board

Mar 24, 2017

13785559 (P.T.A.B. Mar. 24, 2017)

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.
13/785,559 03/05/2013 Peter CARMELIET BJS-5117-35 3858
23117 7590 03/28/2017
NIXON & VANDERHYE, PC
901 NORTH GLEBE ROAD, 11TH FLOOR
ARLINGTON, VA 22203
EXAMINER
GAMBEL, PHILLIP
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
03/28/2017 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):
PTOMAIL@nixonvan.com
pair_nixon @ firsttofile. com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte PETER CARMELIET, DESIRE COLLEN,
SANDRO De FALCO, and RUVO MENOTTI1
Appeal 2016-000703
Application 13/785,559
Technology Center 1600
Before JEFFREY N. FREDMAN, JOHN G. NEW, and RYAN H. FLAX,
Administrative Patent Judges.
Opinion for the Board filed by New,
Administrative Patent Judge.
Opinion Concurring-in-Part, Dissenting-in-Part, filed by FREDMAN,
Administrative Patent Judge.
NEW, Administrative Patent Judge.
1 Appellants state the real parties-in-interest are Life Sciences Research
Partners VZW and Vlaams Interuniversitair Instituut Voor Biotechnologie
VZW. App. Br. 3.
Appeal 2016-000703
Application 13/785,559
DECISION ON APPEAL
Appellants file this appeal under 35 U.S.C. § 134(a) from the
Examiner’s Non-Final Rejection of claims 1—17.
Specifically, the claims stand rejected as unpatentable under 35
U.S.C. § 112, first paragraph, as lacking sufficient written descriptive
support.
Claims 1—17 also stand rejected as unpatentable under 35 U.S.C.
§ 112, first paragraph, as lacking enablement.
Claims 1—17 stand further rejected under 35 U.S.C. § 102(b) as being
anticipated by Boulton et al. (WO 99/24056, May 20, 1999) (“Boulton”).
Claims 1—17 also stand rejected as unpatentable under 35 U.S.C.
§ 103(a) as being obvious over the combination of Boulton, M.J. Bottomley
et al., Placenta growth factor (PIGF) induces vascular endothelial growth
factor (VEGF) secretion from mononuclear cells and is co-expressed with
VEGF in synovial fluid, 119 Clin. Exp. Immunol. 182-88 (2000)
(“Bottomley”), Shitara et al. (US 6,986,890 Bl, January 17, 2006)
(“Shitara”), Tchistiakova et al. (US 6,733,755 B2, May 11, 2004)
(“Tchistiakova”), and Ferrara et al. (US 6,455,283 Bl, September 24, 2002)
(“Ferrara”).
We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.
NATURE OF THE CLAIMED INVENTION
Appellants’ invention is directed to molecules that can inhibit the
binding of PIGF to its receptor (VEGFR-1), such as monoclonal antibodies
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and tetrameric peptides, and to the use of these molecules to treat
pathological processes. Abstract.
REPRESENTATIVE CLAIM
Claim 1 is representative of the claims on appeal and recites:
1. A method of suppressing pathological angiogenesis or
pathological arteriogenesis in an eye of a mammal, by
administering to said mammal an antibody or fragment thereof
that specifically binds to placental growth factor, that has no
cross-reactivity to other proteins, and that neutralizes the activity
of placental growth factor, thereby suppressing pathological
angiogenesis or pathological arteriogenesis in said eye of said
mammal, said antibody being a monoclonal antibody, a human
antibody, a human monoclonal antibody, a humanized antibody,
or a humanized monoclonal antibody; and said antibody
fragment being a Fab, F(ab)'2 or scFv fragment.
App. Br. 25.
ISSUES AND ANALYSES
We do not agree with the Examiner’s findings and conclusions that
the appealed claims lack written descriptive support and are anticipated by,
or obvious over, the combined cited prior art under 35 U.S.C. §§ 102(b) and
103(a). We agree with, and adopt, the Examiner’s findings and conclusion
that the appealed claims lack enablement. We address the arguments raised
by Appellants below.
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A. Rejection of claims 1—17 under 35 U.S.C. $ 112, first paragraph for
lack of written descriptive support
Issue
Appellants argue the Examiner erred because the language of the
claims is supported by sufficient written descriptive support in Appellants’
Specification. App. Br. 13.
Analysis
The Examiner finds the limitation of claim 1 reciting “an antibody or
fragment thereof... that has no cross-reactivity to other proteins” does not
receive adequate written descriptive support in Appellants’ Specification.
Non-Final Act. 3. The Examiner finds the only reference to this limitation is
in paragraph [0018] of the Specification, which recites:
The terms “antibody” or “antibodies” relate to an antibody
characterized as being specifically directed against P1GF or
VEGFR-1 or any functional derivative thereof, with the
antibodies being preferably monoclonal antibodies, or an
antigen-binding fragment thereof, of the F(ab')2, F(ab) or single
chain Fv type, or any type of recombinant antibody derived
thereof. These antibodies of the invention, including specific
polyclonal antisera prepared against PIGF or VEGFR-1 or any
functional derivative thereof have no cross-reactivity to other
proteins. The monoclonal antibodies of the invention can, for
instance, be produced by any hybridoma liable to be formed
according to classical methods from splenic cells of an animal,
particularly of a mouse or rat immunized against PIGF or
VEGFR- 1 or any functional derivative thereof, and of cells of a
myeloma cell line, and to be selected by the ability of the
hybridoma to produce the monoclonal antibodies recognizing
PIGF or VEGFR-1 or any functional derivative thereof that have
been initially used for the immunization of the animals.
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(emphasis added). The Examiner thus finds Appellants’ Specification does
not:
provide sufficient written description showing possession of the
necessary functional characteristics coupled with a known or
disclosed correlation between function and structure, or by a
combination of such identifying characteristics, sufficient to
show the applicant was in possession of a species or a genus of
anti-placental growth factor antibodies having the binding,
inhibiting and treating functions and including no cross­
reactivity to other proteins, broadly encompassed by the claimed
invention.
Non-Final Act. 3 (emphasis added).
The Examiner finds further that the recitation of no cross-reactivity to
other proteins, by the plain language of the Specification, is interpreted to
mean “no cross-reactivity to any other protein.” Non-Final Act. 4. The
Examiner points to several prior art references that teach that antibodies,
including anti-human P1GF antibodies, can routinely be expected to have a
degree of cross-reactivity with other proteins.2 Id. at 4—5. The Examiner
therefore finds that Appellants’ Specification fails to provide a disclosure of
an anti-PIGF antibody having the claimed functional characteristics of
2 The Examiner cites, e.g., G. Kijanka et al., Rapid Characterization of
Binding Specificity and Cross-Reactivity of Antibodies Using Recombinant
Human Protein Arrays, 340(2) J. Immunol. Methods 132—37 (2009); J.A.
Berzovsky and I.J. Berkower, Antibody-Antigen Interactions and
Monoclonal Antibodies, in Antigen-Antibody Interactions and
Monoclonal Antibodies in Fundamental Immunology, Sixth Edition,
152—91 (W. Paul, ed., 2008); J.E. Park et al., Placenta Growth Factor.
Potentiation of Vascular Endothelial Growth Factor Bioactivity, in vitro and
in vivo, and High Affinity Binding to Flt-1 but not to Flk-l/KDR, 269(41) J.
Biol. Chem. 25646—54 (1994); ThermoFisher Product Data Sheet for PLGF
Antibody.
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binding, inhibiting and treating and that has no cross-reactivity to any other
protein, as claimed. Id. at 6. The Examiner concludes that an artisan of
ordinary skill would not be able to visualize or recognize the identity of the
members of the genus that exhibit this functional property. Id.
Appellants argue that their Specification discloses antibodies and
antibody fragments. App. Br. 13 (citing Spec. H 8, 13, 14, 16, 18).
Appellants argue that the Specification further discloses murine monoclonal
antibody MabPL5Dl 1 against P1GF; production of monoclonal antibodies
against murine PIGF-2; and subcloning of the five positive clones with
subsequent production of monoclonal antibodies that were again tested for
inhibition of binding of m-PIGF-2 to Flt-1/Fc. App. Br. 14—15 (citing Spec.
1175—80). Appellants therefore argue that a person of ordinary skill would
understand from the whole of the Specification that Appellants were in
possession of the claimed invention at the time the application was filed.
App. Br. 15.
We do not agree with the Examiner’s findings. “[T]he test for
sufficiency 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.” Ariad
Pharms., Inc. v. Eli Lilly and Co., 598 F.3d 1336, 1351 (Fed. Cir. 2010).
Appellants’ Specification discloses: “These antibodies of the invention,
including specific polyclonal antisera prepared against P1GF or VEGFR-1 or
any functional derivative thereof, have no cross-reactivity to other proteins.”
Spec. 118. Although we find Appellants’ Specification presents a de
minimis written description, we find it just sufficient to reasonably convey to
a person of ordinary skill in the art of immunology an understanding that
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Appellants’ had possession of “an antibody or fragment thereof... that has
no cross-reactivity to other proteins,” as recited in the claims. We
consequently reverse the Examiner’s rejection on this ground.
B. Rejection of claims 1—17 under 35 U.S.C. $ 112, first paragraph for
lack of enablement
The Examiner repeats his findings in support of his conclusion that
Appellants’ claims on appeal are not enabled. Non-Final Act. 6—11. Again,
Appellants do not directly address the Examiner’s conclusion that
Appellants’ Specification does not enable the limitation of claim 1 reciting
“an antibody or fragment thereof... that has no cross-reactivity to other
proteins.”
We find the Examiner has the better position on this issue. Section
112 requires that the patent specification enable “those skilled in the art to
make and use the full scope of the claimed invention without ‘undue
experimentation’” in order to extract meaningful disclosure of the invention
and, by this disclosure, advance the technical arts. Invitrogen Corp. v.
Clontech Labs. Inc., 429 F.3d 1052, 1070-71 (Fed. Cir. 2005). Furthermore,
the specification must teach those of skill in the art “how to make and how
to use the invention as broadly as it is claimed.” In re Goodman, 11 F.3d
1046, 1050 (Fed. Cir. 1993).
We agree with the Examiner that Appellants’ Specification lacks a
sufficient disclosure to enable a person of ordinary skill to make and use the
full scope of an antibody or fragment thereof that has no cross-reactivity to
any other proteins, as required by the claims. This is particularly so in view
of the prior art with respect to the well-known cross-reactivity of
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monoclonal antibodies in the art, as cited by the Examiner in the findings
concerning Appellants’ written description arguments, discussed supra. We
consequently affirm the Examiner’s rejection of the claims.
C. Rejection of claims 1—17 as anticipated and/or obvious
Issue
Appellants argue the Examiner erred in finding Boulton discloses the
limitation of claim 1 reciting “an antibody which is a monoclonal antibody, a
human antibody, a human monoclonal antibody, a humanized antibody, or a
humanized monoclonal antibody or an antibody fragment that is a Fab,
F(ab)'2 or scFv fragment.” App. Br. 18.
Analysis
Appellants argue the Examiner has ignored the claims, as amended, to
include the disputed limitation, and contend that Boulton fails to disclose
each and every aspect of the claimed invention. App. Br. 18.
Furthermore, Appellants argue Boulton fails to establish a causative
relationship between P1GF and proliferative diabetic retinopathy (PDR). Id.
at 19. Appellants contend that it would not have been clear to a person of
ordinary skill in the art whether P1GF is a resultant consequence of PDR or
one of the many possible causes of PDR. Id. According to Appellants, in
the absence of such causal relationship, there would have been no
expectation of success in treating PDR by blocking P1GF. Id.
Appellants also point to Boulton’s disclosures: (1) “that inhibitors of
P1GF ... are able to reduce, prevent or regress ocular angiogenesis”; and (2)
that “P1GF and functional derivatives or fragment thereof may also be used
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to prevent ocular revascularization in conditions such as the PDRs.” App.
Br. 19 (citing Boulton 3—4). Appellants therefore contend Boulton discloses
contradictory teachings with respect to whether P1GF activity should be
decreased or increased in order to prevent ocular angiogenesis, which,
Appellants contend, would have confused a person of ordinary skill in the art
as to whether there existed any reasonable expectation of therapeutic success
in modulating (positive or negative) P1GF in the treatment of any eye
disorder. Id.
The Examiner responds that Boulton explicitly discloses inhibitors of
P1GF in treating pathological conditions encompassed by the claimed
methods and described in Appellants’ Specification, including
“angiogenesis, proliferative diabetic retinopathies for the reduction,
prevention or regression of subretinal neovascularization, iris
neovascularization resulting in glaucoma, rubeosis, comeal/retinal
vascularization.” Ans. 9 (citing Boulton 3, 4, Examples 1, 2). The
Examiner finds Boulton also discloses using anti-PIGF antibodies as
inhibitors of P1GF. Id. (citing Boulton 3—10, claim 10).
With respect to Appellants’ arguments that the disclosures of Boulton
are contradictory, the Examiner finds Boulton discloses P1GF or functional
derivatives I fragments may be used to stimulate or inhibit angiogenesis
depending upon the specific condition to be treated. Ans. 10 (citing Boulton
4). The Examiner finds no contradiction in neutralizing antibodies against
P1GF as inhibitors of various pathological conditions, including regulation of
ocular angiogenesis and the proliferative diabetic retinopathies recited by
Appellants’ claims on appeal. Id.
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We are not persuaded by the Examiner’s findings and conclusions.
As we have explained supra, with respect to Appellants’ enablement
arguments, we are not persuaded that Appellants have provided an enabling
disclosure of the limitation reciting “an antibody ... that has no cross­
reactivity to other proteins.” However, in the Non-Final Rejection, the
Examiner does not cite to any of the prior art references as disclosing this
particular limitation, nor can we find any disclosures in the prior art that
teach or suggest such a limitation. Indeed, the Examiner does not identity a
teaching in Boulton for a monoclonal antibody with narrow specificity and
high affinity limited to the P1GF target. Because the Examiner does not
adduce any evidence disclosing this limitation of the claims on appeal, we
reverse the Examiner’s rejection on this ground. Furthermore, and for the
same reasons, we reverse the Examiner’s rejection of the claims as being
obvious under 35 U.S.C. § 103(a).
DECISION
The Examiner’s rejection of claims 1—17 as unpatentable under
35 U.S.C. § 112, first paragraph, for lack of written description is reversed.
The Examiner’s rejection of claims 1—17 as unpatentable under
35 U.S.C. § 112, first paragraph, for lack of enablement is affirmed.
The Examiner’s rejection of claims 1—17 as unpatentable under
35 U.S.C. § 102(b) is reversed.
The Examiner’s rejection of claims 1—17 as unpatentable under
35 U.S.C. § 103(a) is reversed.
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No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a)(1). See 37 C.F.R.
§ 1.136(a)(l)(iv).
AFFIRMED
CONCURRING-IN-PART, DISSENTING-IN-PART OPINION
FREDMAN,
Administrative Patent Judge.
I fully concur with the opinion of the Majority regarding affirmance
of the enablement rejection and reversal of the anticipation and obviousness
rejections.
I respectfully dissent from the Majority’s result reversing the written
description rejection. In my opinion, the Examiner’s rejection is consistent
with the reasoning of Centocor Ortho Biotech, Inc. v. Abbott Laboratories,
636 F.3d 1341, 1351 (Fed. Cir. 2011) and AbbVie Deutschland GmbH &
Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285 (Fed. Cir. 2014).
Principles of Law
“[T]he asserted claims constitute a wish list of properties that a fully
human, therapeutic TNF-[a] antibody should have: high affinity,
neutralizing activity, and the ability to bind in the same place as the mouse
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A2 antibody.” Centocor, 636 F.3d at 1351. “The specification at best
describes a plan for making fully-human antibodies and then identifying
those that satisfy the claim limitations. But a ‘mere wish or plan’ for
obtaining the claimed invention is not sufficient.” Id.
While our precedent suggests that written description for certain
antibody claims can be satisfied by disclosing a well-
characterized antigen, that reasoning applies to disclosure of
newly characterized antigens where creation of the claimed
antibodies is routine. . . . Claiming antibodies with specific
properties ... can result in a claim that does not meet written
description even if the [target] protein is disclosed because
antibodies with those properties have not been adequately
described.
Id. at 1352.
Functionally defined genus claims can be inherently vulnerable
to invalidity challenge for lack of written description support,
especially in technology fields that are highly unpredictable,
where it is difficult to establish a correlation between structure
and function for the whole genus or to predict what would be
covered by the functionally claimed genus.
Abbvie, 759 F.3d at 1301. “The asserted claims attempt to claim every fully
human 1L—12 antibody that would achieve a desired result, i.e., high binding
affinity and neutralizing activity, and cover an antibody as different as
Stelara, whereas the patents do not describe representative examples to
support the full scope of the claims.” Id.
Findings of Fact
1. The Specification teaches “a murine monoclonal antibody
against P1GF. In another specific embodiment, the murine monoclonal
antibody is MabPL5Dl 1” (Spec. 117).
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2. The Specification teaches the “antibodies of the invention,
including specific polyclonal antisera prepared against P1GF or VEGFR-1 or
any functional derivative thereof, have no cross-reactivity to other proteins”
(Spec. 118).
3. The Specification teaches “antibodies or functional fragments
thereof can be used for the manufacture of a medicament for the treatment of
the above-mentioned disorders” (Spec. |44), with the list of disorders
comprising “ischemic retinopathy, tumor formation, pulmonary
hypertension, edema and inflammation” (Spec. 112).
4. The Specification teaches: “Anti-PIGF antibodies, which
blocked the PIGF response of endothelial cells . . . reduced vascular leakage
in wild-type mice application of mustard oil on their ears” (Spec. 179).
5. The Specification teaches “120 hybridomas were produced, of
which showed a 50% inhibition, 38 showed 70% inhibition and five gave
complete inhibition of binding of rmPIGP-2 to its receptor (Fit-1)” (Spec. |
75).
6. Table 3 of the Specification is reproduced below:
Molar excess versus rn-HGF-2
Nr to X sx 2.5 X 1.25 X No antibody
1 MJH5G5 66 64 63 89 100
£ PL5DI1D4 10 15 22 43 100
PL5D11F10 14 10 22 35 100
3 PL13FUC8 57 70 S3 100 100
4 PL17AI0EI2 40 46 60 m 100
PL17A1GF12 41 41 53 90 100
Negative control Irrelevant antibody l C 8 100 100 100 100 100
Concentration of rn-PJGP-2 in rig/’ml 5 5 5 5 5
Concentration of antibody in ng/ml 200 100 50 25 0
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“Table 3: Inhibition by anti-murine P1GF-2 Mab of murine PIGF-2 binding
to murine Flt-1/Fc. The data represent residual m-PlGF-2 in percent” (Spec.
177).
Analysis
In my view, the central issue in this written description requirement is
the functional requirement in claim 1 that the antibody, in addition to
specifically binding P1GF, also “has no cross-reactivity to other proteins”
and functions to neutralize P1GF thereby “treating pathological angiogenesis
or arteriogenesis.” I do not dispute that two particular antibodies that inhibit
P1GF are described (FF 1, 4).
However, I conclude that the functional requirements that this peptide
also have no cross-reactivity with other proteins and the functional
requirement that the antibodies neutralize P1GF and treat pathological
angiogenesis and arteriogenesis are the sort of wish list of properties which
fails to satisfy the written description requirement since claiming “antibodies
with specific properties, e.g., an antibody that binds to human TNF-a with
A2 specificity, can result in a claim that does not meet written description
even if the human TNF-a protein is disclosed because antibodies with those
properties have not been adequately described.” Centocor, 636 F.3d at
1352.
While the Specification claims that of 120 hybridomas, 15 showed
50% inhibition, 38 showed 70% inhibition and five gave complete inhibition
(FF 5), the data in Table 3 belies that disclosure, showing no complete
inhibition for any of the tested antibodies where several of the monoclonal
antibodies substantially failed to inhibit binding at 1.25 fold molar excess,
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and PL1H5G5 and PL13F11C8 retained more than 50% activity even at 10
fold molar excess (FF 6). Moreover, the issue is not binding to P1GF but
rather the absence of description in the Specification of a routine method for
obtaining antibodies with the other functional properties of claim 1.
In particular, the Specification is entirely silent on disclosing a single
antibody that has no cross-reactivity with other proteins.
There is no disclosure in the Specification of what antibody structures,
antigens, or other information is necessary to obtain the functional result of
avoiding cross-reactivity while retaining neutralizing activity and treating
the specific pathological conditions. Consequently, the instant “claims
merely recite a description of the problem to be solved while claiming all
solutions to it and, as in Eli Lilly and Ariad’s claims, cover any compound
later actually invented and determined to fall within the claim’s functional
boundaries—leaving it to the pharmaceutical industry to complete an
unfinished invention.” Ariad Pharmaceuticals, Inc. v. Eli Lilly and Co., 598
F.3d 1336, 1353 (Fed. Cir. 2010).
In Abbvie, an antibody with a particular binding rate was found to lack
descriptive support for the entire genus even though over 200 antibodies
were disclosed because “[although the number of the described species
appears high quantitatively, the described species are all of the similar type
and do not qualitatively represent other types of antibodies encompassed by
the genus.” Abbvie, 759 F.3d at 1300.
Here, only one antibody was deposited (FF 1) and two total disclosed
with part of the functionality required by claim 1 (FF 4), with no antibody
demonstrated to have no cross reactivity with other proteins. Thus, while
there is not a bright line rule for the number of species necessary to support a
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generic claim, I would find the current Specification insufficient because the
“claims attempt to claim every . . . antibody that would achieve a desired
result, i.e., high binding affinity and neutralizing activity . . . whereas the
patents do not describe representative examples to support the full scope of
the claims.” Id. at 1301.
Appellants contend the “level of skill in the art of making antibodies
that specifically bind to a desired protein, or that are specifically directed to
a desired protein, or that do not cross-react to other proteins, or that
neutralize the activity of a desired protein are well known in the art” (App.
Br. 9).
In Ariad, where a single specific inhibitor, IeB, was taught by the
Specification, Ariad found that “a vague functional description and an
invitation for further research does not constitute written disclosure of a
specific inhibitor insufficient to satisfy the written description requirement.
Ariad, 598 F.3d at 1356. Similarly, in the instant case, the possession of a
very limited number of species of antibody that may themselves lack the
cross-reactivity requirement and without any structure or reliable
methodology to produce other antibodies which necessarily have the
functional properties of “not cross-reacting to other proteins” and “treating
pathological angiogenesis or arteriogenesis” lacks written description.
This is precisely the sort of situation where Appellants have expressed
a wish. A wish for an antibody with certain functional properties. It is a
fine, useful, and desirable wish, but a wish nonetheless. There is no
description of the antigen or process necessary to obtain this antibody.
There are, at best, two examples of such an antibody with no structural
description of the antibody itself. There is no description in the
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Specification of any method which could be reliably used to obtain this
antibody. Centocor mandates that a ‘“mere wish or plan’ for obtaining the
claimed invention is not sufficient.” Centocor, 636 F.3d at 1351. Here,
Appellants’ Specification lacks even a plan, retaining only the wish.
For these reasons, I dissent from the Decision of the Majority and
would affirm the Examiner’s written description rejection.
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