Ex Parte Tamburini

Patent Trial and Appeal Board

Mar 26, 2018

12820654 (P.T.A.B. Mar. 26, 2018)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR
12/820,654 06/22/2010
133485 7590 03/28/2018
Nelson Mullins Riley & Scarborough LLP/Alexion
One Post Office Square
30th Floor
Boston, MA 02109-2127
Paul P. Tamburini
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.
AXJ-149RCE 2533
EXAMINER
GAMBEL, PHILLIP
ART UNIT PAPER NUMBER
1644
NOTIFICATION DATE DELIVERY MODE
03/28/2018 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):
ipbos ton.docketing@nelsonmullins.com
chris.schlauch@nelsonmullins.com
ipqualityassuranceboston@nelsonmullins.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Exparte PAUL P. TAMBURINI 1
Appeal2016-001572
Application 12/820,654
Technology Center 1600
Before RICHARD M. LEBOVITZ, TA WEN CHANG, and
RYAN H. FLAX, Administrative Patent Judges.
CHANG, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134(a) involving claims to a
bispecific antibody, which have been rejected as obvious. We have
jurisdiction under 35 U.S.C. § 6(b ).
We AFFIRM.
STATEMENT OF THE CASE
"The complement system acts in conjunction with other
immunological systems of the body to defend against intrusion of cellular
and viral pathogens." (Spec. 1:20-21.) "Complement components achieve
their immune defensive functions by interacting in a series of intricate but
1 Appellant identifies the Real Party in Interest as Alexion Pharmaceuticals,
Inc. (Br. 2.)
Appeal2016-001572
Application 12/820,654
precise enzymatic cleavage and membrane binding events. The resulting
complement cascade leads to the production of products with opsonic,
immunoregulatory, and lytic functions." (Id. at 1:24--27.) "While a properly
functioning complement system provides a robust defense against infecting
microbes, inappropriate regulation or activation of the complement pathways
has been implicated in the pathogenesis of a variety of disorders," and "[t ]he
down regulation of complement activation has been demonstrated to be
effective in treating several disease indications in a variety of animal
models." (Id. at 3:26-28, 4:6-7.)
In the complement cascade, C5 convertases cleave complement
protein C5 into C5a, "a potent anaphylatoxin and chemotactic factor," and
C5b, "which allows for the formation of the lytic terminal complement
complex [(TCC)], C5b-9." (Id. at 3:18-20.) According to the Specification,
the present invention relates to "bispecific antibodies that bind to human
complement component proteins," in particular bispecific antibodies that can
bind to two or more different proteins including, e.g., C5a and C5b. (Id. at
4: 18-25.) The Specification states that such bispecific antibodies are useful
for "inhibiting terminal complement (e.g., the assembly and/or activity of the
C5b-9 TCC) and/or C5a anaphylatoxin-mediated inflammation" and can
thus be used to treat a variety of complement pathway-associated disorders.
(Id. at 4:27-30.)
Further according to the Specification, such bispecific antibodies have
certain advantages over antibodies that bind to and inhibit cleavage of full-
length or mature C5: "Unlike C5, fragments C5a and C5b are present in
blood at much lower concentrations and are often restricted to specific areas
of local complement activation," and the bispecific antibodies are also "very
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likely to have a longer half-life [in blood] as compared to anti-CS antibodies
... due to a reduced ... antigen-mediated antibody clearance"; thus, lower
dose and/or less frequent administration of the bispecific antibodies are
needed to effectively inhibit CS as compared to an anti-CS antibody. (Id. at
S:7---6: 1.) Likewise, the Specification states that the bispecific antibodies are
also advantageous over the use of a combination of two different antibodies
because of, e.g., simplified process development and clinical evaluation as
well as decreased likelihood that clearance of the antibodies would be
"significantly influenced by normal clearance or turnover of a native, highly
abundant plasma CS protein." (Id. at 6:6-19.)
Claims 1-3, 6-9, and l S-31 are on appeal. Claim 1 is illustrative of
the appealed claims and reproduced below:
1. A bispecific antibody that binds to CSa and CSb.
(Br. 11 (Claims App.).)
The Examiner rejects claims 1-3, 6-9, and lS-31under3S U.S.C.
§ 103(a) as obvious over Guild, 2 Evans, 3 Rother '992, 4 Bansal, 5 Strom, 6
Rother 'OS6,7 and Goldenberg. 8 (Final Act. 9.)
2 Guild et al., US 2010/0166748 Al, published July 1, 2010.
3 Evans et al., US 6,3SS,24S Bl, issued Mar. 12, 2002.
4 Rother et al., US 2010/013S992 Al, published June 3, 2010.
5 Bansal, US 2008/0233113 Al, published Sept. 2S, 2008.
6 Terry B. Strom et al., Therapeutic Approach to Organ Transplantation, in
THERAPEUTIC IMMUNOLOGY (K. Frank Austen et al. ed. 1996).
7 Rother et al., US 2012/022SOS6 Al, published Sept. 6, 2012.
8 Goldenberg et al., US 2006/0140936 Al, published Jun. 29, 2006.
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DISCUSSION
Issue
The Examiner finds that Guild teaches "making and using antibodies
that reduce directly or indirectly ... the conversion of complement
component CS into complement components CSa[]and CSb," including
bispecific molecules. (June 6, 2012 Non-Final Act. S.) The Examiner finds
that Guild further teaches "the importance of CSa and CSb as pro[-
] inflammatory mediators." (Id.)
The Examiner finds that, while Guild teaches anti-CS bispecific
antibodies, it does not explicitly teach that "the bispecific antibody binds
CSa and CSb per se" as required by rejected claim 1. (Id.) However, the
Examiner finds that Evans teaches "anti-CS antibodies, including ...
antibodies that bind CSa/CSb but not CS." (Id.) The Examiner also finds
that Rother '992 teaches "antibody inhibitors of ... CSa and CSb" and also
teaches that "blocking both CSa and CSb-9 generation may be required for
the optimal inhibition of complement-mediated inflammatory responses."
(Id. at 6.) The Examiner further finds that Bansal teaches inhibiting
complement activation using multispecific I bispecific antibodies, including
blocking both CS a and CSb, where "activation of the complement system
has been implicated in the pathogenesis of a variety of diseases." (Id.)
The Examiner also adds Rother 'OS6 and Goldenberg to provide
further teachings regarding, respectively, "antibodies that bind to CSa and
CSb ... and ... divalent, bivalent antibodies that bind to two binding sites
on CS ... for a variety of therapeutic utilities" and "inhibitors of CS,
including anti-CS antibodies, that bind CSa or CSb, including multispecific
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antibodies that target complement factors, including C5a and C5b ... for a
variety [of] therapeutic utilities." (Oct. 7, 2013 Non-Final Act. 7.)
The Examiner concludes that it would have been obvious for a skilled
artisan to arrive at the claimed "bispecific antibody that binds to C5a and
C5b" because the claimed invention involved no more than the combination
of familiar elements according to known methods to yield predictable
results. (June 6, 2012 Non-Final Act. 6-7.) The Examiner further concludes
that a skilled artisan would have reason to make the combination "in order to
increase the efficacy of targeting the contribution of both C5a and C5b to
complement activation and its ill effects in various inflammatory
conditions." (Id. at 7 .) Citing Strom, the Examiner further finds that a
skilled artisan would have reason to pursue bispecific inhibition of C5a and
C5b because it is known that "a multi[-]tiered approach to
immunosuppressive therapy," wherein several agents are used
simultaneously, may "limit[] the toxicity of each individual agent while
increasing the total immunosuppressive effect." (Id. at 8.)
Appellant contends that Appellant recognized "a new problem in the
art, i.e., that there are certain limitations of antagonist anti-CS antibodies"
and further contends that, "absent knowledge of the problem and the
guidance provided in the instant specification, there simply would have been
no apparent reason for one of ordinary skill in the art to arrive at the
presently claimed antibodies." (Br. 9.)
The issue with respect to this rejection is whether a preponderance of
evidence supports the Examiner's conclusion that the cited prior art renders
obvious a bispecific antibody that binds to C5a and C5b.
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Findings of Fact (FF)
1. Guild teaches that
[ c ]omplement component CS is the major component of the
final pathway common to the lectin, classical and alternative
pathways in the complement cascade. The cleavage of CS by
the CS convertases of the alternative and classical pathways
yields CSb and CSa fragments. Both CSa and CSb are
proinflammatory molecules. CSa is a powerful anaphylotoxin.
. . . CSb serves as the nucleation site for the assembly of CSb-9
(CSb, C6, C7, CS and C9) also as known as the terminal
complement complex or the membrane attack complex (MAC)
that penetrates cell membranes forming a pore, which at
sublytic concentrations can contribute to proinflammatory cell
activation while at lytic concentrations it leads to cell death.
Reducing the formation of CSb-9 (MAC) and the generation of
CS a may be required for the inhibition of inflammatory
responses contributing to [age-related macular degeneration
(AMD)].
(Guild ii 4.)
2. Guild teaches "a method of treating or preventing ocular
diseases or disorders ... comprising administering an effective amount of
antibodies which specifically bind to one or more epitopes of CS to thereby
inhibit CS protein function in the complement pathway systems of a subject
in need of such treatment." (Id. ii 9.)
3. Guild teaches that the preferred anti-CS antibodies for its
invention bind to "CS or fragments thereof, e.g., CS a or CSb." (Id. ii 117 .)
4. Guild teaches that,
[i]n another aspect, [its] invention features bispecific molecules
comprising a CS binding molecule (e.g., an anti-CS antibody, or
a fragment thereof), of the invention. A CS binding molecule
of the invention can be derivatized or linked to another
functional molecule, e.g., another peptide or protein (e.g.,
another antibody or ligand for a receptor) to generate a
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bispecific molecule that binds to at least two different binding
sites or target molecules. . .. To create a bispecific molecule
of the invention, an antibody of the invention can be
functionally linked (e.g., by chemical coupling, genetic fusion,
noncovalent association or otherwise) to one or more other
binding molecules, such as another antibody, antibody
fragment, peptide or binding mimetic, such that a bispecific
molecule results.
(Id. ii 192.)
S. Guild teaches that "bispecific molecules of [its] invention can
be prepared by conjugating the constituent binding specificities using
methods known in the art." (Id. ii 19S.)
6. Evans teaches anti-CS antibodies "useful in the treatment of
[glomerulonephritis (GN)] and other inflammatory conditions involving
pathologic activation of the complement system." (Evans Abstract.)
7. In particular, Evans teaches "anti-CS antibodies that bind to
complement component CS or active fragments thereof. Preferably, the
antibodies block the generation and/or activity of complement components
CSa and CSb." (Id. at 7:8-12.; see also id. at 8:SS-S7, 18:61-62 (stating that
"[t]he anti-CS antibodies used in the practice of the invention bind to CS or
fragments thereof, e.g., CSa or CSb"), 19:31-33 (stating that "complement
component CS or CSb is preferably used as the immunogen"), claim 3
(method for treatment of GN comprising using an antibody that binds to
CSb ). ) Evans suggests that "[ t ]hrough this blocking effect, the antibodies
inhibit the proinflammatory ( anaphylatoxic) effects of CS a and the
generation of the CSb-9 membrane attack complex (MAC)." (Id. at 7:31-
33; see also id. at 8:S7---60.)
8. Rother '992 teaches administering an inhibitor of complement
activity, particularly an inhibitor of complement CS cleavage, together with
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one or more immunosuppressants and/or immunosuppressive methods, to
prolong survival of allotransplanted cells. (Rother '992 Abstract, i-f 2; see
also, e.g., id. i-fi-114, 22, 24, 31, 33, 39, 41, 48, 104, claims 7, 10, 16, 96, 99,
1 OS (generally discussing inhibiting formation of CSb or CS a, including by
inhibiting cleavage of CS); i-fi-160, 137, 1S4, 168, 172 (effect of using anti-CS
antibody in combination with other therapy in prolonging graft survival).)
9. Rother '992 teaches that the CS component of the complement
system is cleaved to form "products with multiple proinflammatory effects."
(Id. i-f 88.) In particular, Rother teaches that CSa is an anaphylatoxin and
that CSb combines with C6, C7, C8, and C9 molecules to form membrane
attack complex (MAC) that may lead to proinflammatory cell activation or
cell lysis. (Id. i-fi-184, 88.) Rother '992 teaches that, "blocking both CSa and
CSb-9 generation may be required for the optimal inhibition of complement-
mediated inflammatory response following transplantation." (Id. i-f 88; see
also id. i-f 97 (suggesting that "inhibiting the formation of CSa and CSb-9 or
inhibiting CSa and CSb-9 which was present would aid in preventing graft
failure").)
10. Rother '992 teaches that "antibodies can be made to individual
components of activated complement, e.g., antibodies to CSa, C7, C9, etc."
(Id. i-f 94.) Rother '992 also teaches that "beneficial effect of anti-CS mAb
has previously been reported in several experimental models." (Id. i-f 89; see
also id. i-f 99 (discussing known anti-CS antibodies).)
11. Rother 'OS6 teaches that cleavage of CS releases CS and leads
to the formation of CSb-9, which among other things amplify the release of
downstream inflammatory factors. (Rother 'OS6 i-f 13; see also id. i-f lS.)
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12. Rother '056 teaches using "compositions containing an
inhibitor of human complement ... for treating or preventing complement-
associated disorders." (Id. at Abstract, i-fi-f 18-19.) In particular, Rother '056
teaches embodiments wherein the inhibitor inhibits "the cleavage of human
complement component C5 into fragments C5a and C5b" as well as
embodiments wherein "the inhibitor binds to, and inhibits, one or both of
C5a and C5b." (Id. i-fi-122-23.) Rother '056 also teaches compositions
including two or more inhibitors of C5. (Id. i-f 147.)
13. Rother '056 teaches that "[t]he inhibitor can be, e.g., an
antibody that binds to C5a or C5b." (Id. i123; see also, e.g., id. i-fi-f 18
(describing embodiments wherein the compositions contain an antibody that
binds to C5, C5a, or C5b ), 59 (inhibitor can be antibody that binds to C5 or
C5a or C5b ), 89 (inhibitor of C5 may be "an antibody that binds to a ... C5
protein or a biologically-active fragment thereof such as C5a and C5b"), 94,
120 (anti-C5a antibody), 122, 124, 125 (anti-C5b antibody), 130, 179.)
14. Rother '056 teaches that antibodies that bind to C5a or C5b,
and the methods for making such antibodies, are known in the prior art. (Id.
,-r,-r 122, 127, 148.)
15. Rother '056 teaches that,
[i]n the therapeutic embodiments of the present disclosure,
bispecific antibodies are contemplated. Bispecific antibodies
are monoclonal, preferably human or humanized, antibodies
that have binding specificities for at least two different antigens.
In the present case, one of the binding specificities is for the
human complement component C5 antigen the other one is for
any other antigen.
Methods for making bispecific antibodies are within the
purview of those skilled in the art.
(Id. at i-fi-f 180-183.)
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16. Goldenberg teaches
a multispecific antagonist that reacts specifically with at least
two different targets. The targets are selected from the group
consisting of (A) pro inflammatory effectors of the innate
immune system, (B) coagulation factors, (C) complement
factors and complement regulatory proteins, and (D) targets
specifically associated with an inflammatory or immune-
dysregulatory disorder or with a pathologic angiogenesis or
cancer, wherein the latter target is not (A), (B), or (C)." At
least one of the targets is (A), (B) or (C).
(Goldenberg i-f 33; see also id at Abstract.)
17. Goldenberg teaches that in the complement cascade "a specific
complement protein, C5, forms two highly active, inflammatory byproducts,
C5a and C5b." (Id. i-f 110.) Goldenberg teaches that,
[ w ]hile any of these components of the complement system can
be targeted by a multispecific antagonist according to the
invention, certain of the complement components are preferred.
C3a, C4a and C5a cause mast cells to release chemotactic
factors such as histamine and serotonin, which attract
phagocytes, antibodies and complement, etc. These form one
group of preferred targets according to the invention. Another
group of preferred targets includes C3b, C4b and C5b, which
enhance phagocytosis of foreign cells. Another preferred group
of targets are the predecessor components for these two groups,
i.e., C3, C4 and C5. C5b, C6, C7, CS and C9 induce lysis of
foreign cells (membrane attack complex) and form yet another
preferred group of targets.
(Id. i-f 112; see also id. i-fi-137 (stating that "[i]n preferred embodiments, the
complement factor is selected from the group consisting of C3, C5, C3a, and
C5a"), 104 ("another group of targets is the group consisting of C5a, LPS,
IFNy and B7''), 113, 121, 123 (preferred target combinations having
complement factor, especially C3, C5, C2a, or C5a, as one of the targets).)
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18. Goldenberg teaches that, "[i]n some embodiments, the
multispecific antagonist is a combination of two separate antibodies. In
other embodiments, it is a multispecific antibody, particularly a fusion
protein." (Id. i-f 34; see also id. i-fi-1 40, 44, 92, 126.) Goldenberg further
teaches that
[a] multispecific antibody is an antibody which can bind
simultaneously to at least two targets which are of different
structure, e.g., two different antigens, two different epitopes on
the same antigen, or a hapten and/or an antigen or epitope. Two
or more of the binding arms may be directed to the same or
different epitopes of the same antigen; thus constituting
multivalency in addition to multispecificity.
A bispecific antibody is an antibody or antibody
fragment construct which can bind simultaneously to two
targets which are of different structure.
(Id. i-fi-f 84--85, 102.)
19. Goldenberg teaches that "[t]here are certain advantages when
the multispecific antagonist is an antibody that is at least bispecific,
including rapid clearance from the blood." (Id. i-f 125.)
20. Goldenberg teaches that
[a ]ntagonists that inhibit complement activation products,
especially the anaphylatoxins, ... offer promise to decrease
sepsis mortality. C3a, C4a and C5a, appear during sepsis, and
the elevated anaphylotoxin plasma levels highly correlate with
the development of multi organ failure. In sepsis, complement
may directly promote procoagulant activity or indirectly induce
cytokine production. In vitro C5a and the terminal complex of
complement, C5b-9, induce tissue factor expression on
endothelial cells and monocytes, and assembly of C5b-9 on the
surface of platelets has been shown to stimulate prothrombinase
activity. The present invention provides improved therapeutics
for treating sepsis by providing multispecific antagonists that
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target two or more of coagulation factors, proinflammatory
cytokines and complement activations products.
(Id. if 183.)
21. Bansal teaches a method of inhibiting the formation of C3a,
C5a, and membrane attack complex (MAC). (Bansal Abstract.)
22. Bansal teaches that C5 convertase cleaves C5 to release C5a,
the most potent anaphylatoxin, and C5b, which initiates the formation of
C5b-9 known as the membrane attack complex (MAC). (Id. if 10.) Bansal
teaches that both C5a and MAC have roles in inflammation and that MAC
has role in lysing cells. (Id. at iii! 10, 53, 54.)
23. Bansal teaches that the complement system, including C5a and
C5b-9, may be implicated in the pathogenesis of a number of diseases. (See,
e.g., id. iii! 43, 46, 49, 53, 54--55, 56-57, 64, 66, 79, 81, 87-88, 94--95, 98-
99, 102, 114.)
24. Bansal teaches that administration of anti-CS monoclonal
antibodies may prevent or treat certain pathologies. (See, e.g., id. iii! 39
(attenuated infarct size, neutrophil infiltration, and apoptosis in the
myocardium), 55 (decreases symptoms in a mouse model of systemic lupus
erythematosus (SLE), an autoimmune disease), 5 8 (amelioration of
glomerulonephritis in a mouse model), 73 (prevents hyperacute rejection in
rat-to-presensitized mouse heart transplantation model).)
25. Bansal teaches that antibodies to C5a is known in the prior art.
(Id. if 152.)
26. Strom teaches that antirejection therapy is organized certain
general principles, including a multi-tiered approach wherein "several agents
are used simultaneously, each of which is directed at a different molecular
target with the allograft response." (Strom 451, left column.) Strom further
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teaches that "[a ]dditive-synergistic effects are achieved through application
of each agent at a relatively low does, thereby limiting the toxicity of each
individual agent while increasing the total immunosuppressive effect." (Id.)
Analysis
Appellant does not separately argue the claims, and we limit our
analysis to claim 1 as representative. 37 C.F.R. § 41.37(c)(l)(iv).
The cited prior art shows that the functions of C5a and C5b in the
complement system are well known in the art. (FF 1, FF9, FF 11, FF 17,
FF22.) Likewise, it is well known in the art that inhibitors of C5a and C5b,
such as anti-C5a, and anti-C5b antibodies, may be used to treat complement
associated pathologies. (FF2, FF3, FF6, FF7, FF12, FF13, FF20.)
The cited prior art also shows that anti-C5a and anti-C5b antibodies,
as well methods of manufacturing such antibodies, are known in the art.
(FFlO, FF14, FF25.) Guild and Goldenberg similarly teach bispecific
antibodies and methods of manufacturing them. (FF4, FF5, FF16-FF18.)
Finally, both Guild and Goldenberg suggest C5a and/or C5b as a target for
such a bispecific antibody (FF3, FF4, FFl 7), and Rother '056 teaches an
inhibitor that "binds to, and inhibits, one or both of C5a and C5b" (FF12
(emphasis added).)
In light of the above, we agree with the Examiner that the cited prior
art combination renders claim 1 obvious, because a bispecific antibody that
binds to C5a and C5b is no more than the combination of familiar elements
according to known methods that yields predictable results. KSR Int 'l Co. v.
Teleflex Inc., 550 U.S. 398, 416 (2007) ("The combination of familiar
elements according to known methods is likely to be obvious when it does
no more than yield predictable results."). The teaching in Goldenberg of
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bispecific antibodies to complement proteins, including preferred targets
CSa and CSb (FFl 7), particularly, provides a strong reason to have made the
claimed bispecific antibody to both these targets. As the Examiner
concluded, a skilled artisan would have reason to make the claimed
combination "in order to ... target[] the contribution of both CS a and CSb to
complement activation and its ill effects in various inflammatory
conditions." (June 6, 2012 Non-Final Act. 7.)
Appellant argues that "[ n ]one of the cited references, alone, per se
teach the instantly claimed bispecific antibodies." (Br. 7-9.) We are not
persuaded. The rejection is based on obviousness, not anticipation. "Non-
obviousness cannot be established by attacking references individually
where the rejection is based upon the teachings of a combination of
references. . . . [The reference] must be read, not in isolation, but for what it
fairly teaches in combination with the prior art as a whole." In re Merck &
Co., 800 F.2d 1091, 1097 (Fed. Cir. 1986).
Appellant argues that the claimed bispecific antibody that binds to
CSa and CSb "are very likely to have a longer half-life, as compared to anti-
cs antibodies, in blood due to a reduced contribution of antigen-mediated
antibody clearance." (Br. 7 (emphasis omitted).) To the extent Appellant is
arguing that the claimed subject matter exhibits unexpected results, we are
not persuaded. Appellant has not cited persuasive evidence that the alleged
difference in antibody clearance between an anti-CS antibody and a
bispecific antibody that binds to CSa and CSb is unexpected. Pfizer, Inc. v.
Apotex, Inc., 480 F.3d 1348, 1371 (Fed. Cir. 2007) (explaining that, "by
definition, any superior property must be unexpected to be considered
evidence of non-obviousness"). Neither has Appellant shown that any
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alleged unexpected results are unexpected as compared with the closest prior
art. In re Baxter Travenol Labs., 9S2 F.2d 388, 392 (Fed. Cir. 1991) (stating
that, "when unexpected results are used as evidence of nonobviousness, the
results must be shown to be unexpected compared with the closest prior
art.").
Appellant argues that Appellant "went in a new and different direction
from [the prior art] based, at least in part, on the recognition of a new
problem in the art, i.e., that there are certain limitations of antagonist anti-CS
antibodies." (Br. 9.) Appellant argues that a patentable invention "may lie
in the discovery of the source of a problem even though the remedy may be
obvious once the source of the problem is identified." (Id. (internal
quotation marks and citation omitted).) 9
Discovery of the source of a problem may indeed result in a
patentable invention, In re Sponnoble, 40S F.2d S78, S8S (C.C.P.A. 1969);
Leo Pharm. Products., Ltd. v. Rea, 726 F.3d 1346, 13S3 (Fed. Cir. 2013).
We are not persuaded, however, that cases such as Sponnoble and Leo
Pharmaceutical apply in this instance.
In Sponnoble, the invention related to an improved center seal plug
that may be placed between the compartments in a plural compartment
mixing vial in order to temporarily isolate the compartments from each
other, wherein the plug is formed of butyl rubber and coated with a thin film
of silicone and solves the problem of an excessive amount of moisture
9 Appellant also asserts that his solution (i.e., a bispecific antibody that binds
to CSa and CSb) to the problem that had not been previously identified (i.e.,
that "there are certain limitations of antagonist anti-CS antibodies") is "novel
and non-obvious." (Br. 9.) We are not persuaded for the reasons already
discussed.
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transmitted from a liquid-containing compartment into a solids-containing
compartment. 405 F.2d at 580. The rejection was based in part on the
finding that "[prior art reference] Jensen clearly teaches in the art the use of
butyl rubber for its steam, i.e., moisture, impervious property ... and ... in
view thereof it would have been obvious ... to make the center plug ... of
[prior art reference] Bujan of butyl rubber so as to render it impervious to
moisture." Id. at 585 (internal quotation marks omitted). In reversing the
rejection, the Sponnoble court found that "[t]here is no teaching in the prior
art which would suggest the necessity of selecting a center seal plug material
which is more impervious to liquid water than [prior art references] Bujan's
or Lockhart's natural rubber." Id. at 586.
In Leo Pharmaceutical, the claim at issue recited "[a] pharmaceutical
composition for dermal use, said composition comprising
[components A, B & CJ ... wherein said pharmaceutical composition is
storage stable and nonaqueous." 726 F.3d at 1352 (first bracket added).
The Leo Pharmaceutical court found, however, that "the prior art either
discouraged combining [two recited components] in a single formulation, or
attempted the combination without recognizing or solving the storage
stability problems associated with the combination." Id. at 1353.
In contrast, as discussed above, the cited prior art in this case provides
suggestion and reason to combine the known anti-C5a antibody and anti-
C5b antibody into a bispecific antibody as required by the claims-i.e., in
order to treat various inflammatory conditionsregardless of whether there is
recognition in the prior art that antagonist anti-CS antibodies has limitations
relating to, e.g., high rate of antigen-mediated antibody clearance. The
reason to combine the prior art does not have to be the same reason that
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Appeal2016-001572
Application 12/820,654
motivated the inventors to have made the invention. Contrary to the facts in
Leo Pharmaceutical, there is explicit reason to make a bispecific antibody to
C5a and C5b (e.g., FF 17) and no evidence that such combination was
disparaged or otherwise considered inapt.
Finally, Appellant argues that, "absent knowledge of the problem and
the guidance provided in the instant specification, there simply would have
been no apparent reason for one of ordinary skill in the art to arrive at the
presently claimed antibodies." (Appeal Br. 9.) We are not persuaded for the
reasons already discussed above.
Accordingly, we affirm the Examiner's rejection of claim 1. Claims
2, 3, 6-9, and 15-31, which were not separately argued, fall with claim I.
37 C.F.R. § 41.37(c)(l)(iv).
SUMMARY
For the reasons above, we affirm the Examiner's decision rejecting
claims 1-3, 6-9, and 15-31.
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
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