Ex Parte Bartel

Board of Patent Appeals and Interferences

Jul 2, 2008

10122573 (B.P.A.I. Jul. 2, 2008)

UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte PAUL BARTEL
__________

Appeal 2008-2711
Application 10/122,573
Technology Center 1600
__________

Decided: July 2, 2008
__________

Before DONALD E. ADAMS, DEMETRA J. MILLS, and JEFFREY N.
FREDMAN, Administrative Patent Judges.

FREDMAN, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to an
isolated protein complex, which the Examiner has rejected as lacking an
adequate description in the Specification, as failing to enable the full scope
of the claims and as inherently anticipated. We have jurisdiction under 35
U.S.C. § 6(b). We affirm.

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Application 10/122,573

Background
“In contrast with the traditional view of protein function, which
focuses on the action of a single protein molecule, a modern expanded view
of protein function defines a protein as an element in an interaction network”
(Spec. 3). The Specification discloses that by “identifying interacting
proteins, a better understanding of disease pathways and the cellular
processes that result in diseases may be achieved, and important regulators
and potential drug targets in disease pathways can be identified (Spec. 4).
The Specification separately notes that the “yeast two-hybrid system can be
employed to identify proteins that interact with a specific known protein
involved in a disease pathway” (Spec. 6).
Appellants teach that the “apoptosis regulator Bcl-XL ("BCL-XL")
interacts with translationally-controlled tumor protein 1 ("TCTP", also
known as IgE-dependent histamine-releasing factor or HRF)” (Spec. 6).
Statement of the Case
The Claims
Claims 39-48 are on appeal. We will focus on claim 39 which is
representative and reads as follows:
39. An isolated protein complex comprising a first protein
interacting with a second protein, wherein said first protein is
selected from:
(a) BCL-XL, or a fragment thereof that interacts with
TCTP;
(b) a first polypeptide having an amino acid sequence at
least 75% identical to that of (a), and that interacts with TCTP;
or
(c) a first fusion protein comprising (a) or (b); and
wherein said second protein is selected from:

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(i) TCTP, or a fragment thereof that interacts with BCL-
XL;
(ii) a second polypeptide having an amino acid sequence
at least 75% identical to that of (i), and that interacts with BCL-
XL; or
(iii) a second fusion protein comprising (i) or (ii).

The prior art
The Examiner relies on the following prior art reference to show
unpatentability:
Yang1 et al. An N-terminal region of translationally controlled tumor
protein is required for its antiapoptotic activity. 24 Oncogene 4778 (2005).
Walensky et al. Novel chemically stabilized helices of the BCL-2
family induce apoptosis of leukemia cells. 102 Blood 5A (2003).
Gachet et al. The growth-related, translationally controlled protein
P23 has properties of a tubulin binding protein and associates transiently
with microtubules during the cell cycle. 112 J. Cell Sci. 1257 (1999).

The Issues
The rejections as presented by the Examiner are as follows:
A. Claims 39-48 stand rejected under 35 U.S.C. § 112, first paragraph, as failing to
comply with the written description requirement.

1 Consonant with to 37 C.F.R. § 41.39(b)(2)(2006), Appellants have
addressed the Yang reference, newly cited in the Examiner’s answer, in the
Reply Brief filed March 19, 2007, thereby maintaining the appeal.

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B. Claims 39-48 stands rejected under 35 U.S.C. § 112, first paragraph, as being
nonenabled for the full scope of the claims.
C. Claims 39-48 stands rejected under 35 U.S.C. § 102(b), as being anticipated by
Gachet.

A. Written Description rejection
The Examiner rejected claims 39-48 under 35 U.S.C. § 112, first
paragraph, on the basis that the “genus of proteins complexes are highly
variant because the genus is not characterized by a functional attribute of the
complex which would serve to identify members of the genus from those
which are not part of the genus” (Ans. 4). The Examiner contends that the
“disclosure of the complex of Bcl-xL and TCTP does not adequately
describe the claimed genus of proteins complexes because the claimed
genuses encompasses protein complexes which differ in both structure and
function from the Bcl-xL-TCTP complex.” (Ans. 4).
Appellant argues that, like the RNA polymerase in Invitrogen, “the
modified Bcl-xL protein in Claim 39 is defined by both structural (sequence
identity to native Bcl-xL protein, or Bcl-xL fragment) and functional
features (interacting with TCTP protein)” (App. Br. 9). Appellant notes that
“both Bcl-xl and TCTP were well known proteins in the art at the time of
filing” (App. Br. 9). Appellant further contends that “the PTO's own
Written Description Guidelines teach that a single species of polypeptide,
disclosed through a combination of structural and functional attributes, is
sufficient to describe a genus of related, variant polypeptides” (App. Br. 10).
Appellant also argues that the “Examiner's allegation that binding is not a
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functional attribute (Final Office Action at paragraph 4, p. 4) has no basis in
law or fact. Invitrogen did not limit what type of functional information,
when combined with structural characteristics, would be sufficient to
describe a genus invention” (App. Br. 11).
In view of these conflicting positions, we frame the description issue before us
as follows:
Does Appellant’s Specification contain a written description sufficient
to show they had possession of their claimed invention at the time the
application was filed, as required by Federal Circuit precedent?
Findings of Fact
1. The Specification teaches that “apoptosis regulator Bcl-XL
(“BCL-XL”) interacts with translationally-controlled tumor protein 1
(“TCTP”, also known as IgE-dependent histamine-releasing factor or HRF)”
(Spec. 6:17-19).
2. The Specification teaches that “homologues, derivatives, and
fragments of BCL-XL and of TCTP may also be used in forming protein
complexes” (Spec. 7:2-4).
3. The Specification refers to the specific Genbank accession
numbers which teach the amino acid sequences of BCL-XL and TCTP (see
Spec. 20, Table 1).
4. The Specification provides no correlation between specific
structural domains of either BCL-XL or TCTP and any functional activities
of the proteins including protein binding (see Spec. 108).
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A. Discussion of Written Description rejection
We agree with the Examiner that the Specification does not
adequately describe the claimed protein complex as broadly claimed.
Describing a claim to a protein complex requires describing the compounds
used in the complex.
It is well settled that

the inventor cannot lay claim to that subject matter unless he
can provide a description of the compound sufficient to
distinguish infringing compounds from non-infringing
compounds, or infringing methods from non-infringing
methods. As the district court observed, “[t]he claimed
method depends upon finding a compound that selectively
inhibits PGHS-2 activity. Without such a compound, it is
impossible to practice the claimed method of treatment.”

University of Rochester v. G.D. Searle & Co., 358 F.3d 916, 926 (Fed. Cir.
2004).
Claim 39 is broadly drawn to not only to a complex of the BCL-XL
and TCTP proteins, for which the sequences are known (FF 1, 3), but also
encompasses the genus of complexes in which fragments of unknown size
and sequence of the BCL-XL and TCTP proteins form the complex (FF 2).
Additionally, the claim encompasses proteins with only 75% identity to
some BCL-XL or some TCTP, without a specific delineation of what
starting sequence is being used for the 75% identity comparison (see claim
39). The Specification therefore must adequately describe that genus of
compounds.
The written description requirement can be met by disclosing
“complete or partial structure, other physical and/or chemical properties,
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functional characteristics when coupled with a known or disclosed
correlation between function and structure, or some combination of such
characteristics.” Enzo Biochem, Inc. v. Gen-Probe Inc., 323 F.3d 956, 964,
(Fed. Cir. 2002).
In this case, the Specification references the complete sequence of the
BCL-XL and TCTP proteins (see FF 3). However, the Specification does
not describe any of the specific structural features of BCL-XL which give
rise to the function of TCTP binding. In fact, the Specification fails to
identify which region, or regions, within the 216 amino acid BCL-XL
protein are involved in TCTP binding.
The present case is therefore analogous to Rochester. In Rochester,
the patent claimed a method of selectively inhibiting the enzyme PGHS-2
(also known as COX-2) by “administering a non-steroidal compound that
selectively inhibits activity of the PGHS-2 gene product to a human.”
Rochester, 358 F.3d at 918. The patent “describes in detail how to make
cells that express either COX-1 or COX-2, but not both . . ., as well as
‘assays for screening compounds, including peptides, polynucleotides, and
small organic molecules to identify those that inhibit the expression or
activity of the PGHS-2 gene product.’” Rochester, 358 F.3d at 927.
The court held that even if a DNA sequence might support a claim to
hybridizing nucleic acids, the “same is not necessarily true in the chemical
arts more generally. Even with the three-dimensional structures of enzymes
such as COX-1 and COX-2 in hand, it may even now not be within the
ordinary skill in the art to predict what compounds might bind to and inhibit
them.” Rochester, 358 F.3d at 925.
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The concern is even more acute in the current case, where unlike in
Rochester, where the claims involved only the use of the natural COX-2
molecule, here the claims encompass any protein that is 75% similar to the
216 amino acid BCL-XL protein or that is 75% similar to the 172 amino
acid TCTP protein.
Appellants have not provided any identification of a single region or
multiple regions within the BCL-XL protein which are involved in TCTP
binding. Appellants have not provided any identification of critical residues
in the BCL-XL which are essential to HCV E2 binding.
As in Rochester, the present application discloses the assay for
screening BCL-XL and TCTP interaction but fails to provide BCL-XL
regions other than the wild type which bind to wild type TCTP (FF 3).
As the district court pointed out: Tellingly, . . . what
plaintiff's experts' [sic] do not say is that one of skill in the
art would, from reading the patent, understand what
compound or compounds-which, as the patent makes clear,
are necessary to practice the claimed method-would be
suitable, nor would one know how to find such a compound
except through trial and error . . . . Plaintiff's experts opine
that a person of ordinary skill in the art would understand
from reading the ′850 patent what method is claimed, but it
is clear from reading the patent that one critical aspect of the
method-a compound that selectively inhibits PGHS-2
activity-was hypothetical, for it is clear that the inventors
had neither possession nor knowledge of such a compound.

Rochester, 358 F.3d at 925-926.
Just as in Rochester, it is hypothetical which amino acid modifications
of BCL-XL will share the claimed activity of binding to TCTP. In the
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Specification, there is no possession or knowledge of any such specific
compound which will form the claimed complex.
Appellant argues that Invitrogen supports a finding of that the written
description is satisfied because “the Federal Circuit recognized that (1) the
sequences of the RT gene family were known at the time of filing, and (2)
the specification also discloses methods and data of testing that the enzyme
produced by the listed sequence has the claimed features” (App. Br. 8).
We think that Invitrogen is readily distinguished from the current case
because in Invitrogen, there was “an article by Johnson et al., 83 Proc. Nat'l
Acad. Sci. USA 7648-52, 7651 (1986), established a sufficiently known
correlation between RNase H activity in RT (function) and the RT gene
made by deletion mutation (structure) to satisfy the PTO test for written
description.” Invitrogen Corp. v. Clontech Laboratories, Inc., 429 F.3d
1052, 1072 (Fed. Cir. 2005). Along with the known nucleotide sequences
and the known significant homologies between reverse transcriptases,
Invitrogen also relies upon the correlation between function and structure
that was also known in the prior art. No such correlation has been disclosed
for BCL-XL or for TCTP. The Examiner points out that knowledge of the
structure and separability of the DNA polymerase and RNAse H activities
was disclosed in Invitrogen (Ans. 11).
Appellants cite two papers in Exhibits (App. Br. 10) as evidence that
sequences of TCTP and BCL-XL are known from other species, but neither
Cheng nor Bhisutthibhan discloses any correlation between any function of
either TCTP and BCL-XL and structure, much less the binding function
necessary to form the complex of BCL-XL and TCTP.
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It is the absence of any knowledge of structural elements within BCL-
XL or TCTP which mediate the complex formation that fails the Enzo
description test. Here, as many as ¼ of the amino acids in either or both of
BCL-XL and TCTP may be altered based upon the 75% identity language.
However, the Specification lacks possession of any method, other than trial
and error, to determine whether the alterations will impact the binding to
form the complex (Ans. 4). We find that in the absence of knowledge of
which structural elements of BCL-XL are involved in TCTP binding, there
is no possession of which subset of BCL-XL or TCTP molecules in the
immense genus encompassed by the 75% similarity language will retain the
binding function.
We note that the revised Written Description guidelines have changed
the analysis from that discussed by Appellant (see App. Br. 10). The March
2008 revision discusses the situation where 95% variants of a protein with
function are claimed,
[t]here is no teaching in the specification regarding which
5% of the structure can be varied while retaining the ability
of the protein to catalyze the reaction A->B. Further, there is
no art-recognized correlation between any structure (other
than SEQ ID NO: 3) and the activity of catalyzing A->B,
based on which those of ordinary skill in the art could
predict which amino acids can vary from SEQ ID NO: 3
without losing the catalytic activity. Consequently, there is
no information about which amino acids can vary from SEQ
ID NO: 3 in the claimed genus of proteins and still retain the
catalytic activity.

(Written Description guidelines at 35, in Example 10 (available at
http://www.uspto.gov/web/menu/written.pdf (last visited May 19, 2008)).
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The revised Written Description guidelines conclude that the claim fails to
comply with the written description requirement because of the absence of
information correlating any structure with function. We think that this
applies directly to the current situation, where the no BCL-XL or TCTP
structure which correlates with the binding activity is disclosed and
consequently, there is no information about which amino acids can vary and
still retain the ability for the protein complex required by claim 39.
We need not address Appellant’s argument that “Applicant has
fulfilled the requirements of § 101 by asserting a specific, substantial,
credible utility that gives the public an immediately useful, powerful new
tool in the search for novel therapeutic compounds that potentially could be
used for the treatment of cancer” (Rep. Br. 7). No utility rejection is present
in the Examiner’s answer.
We affirm the rejection of claim 39 under 35 U.S.C. § 112, first
paragraph, for lack of adequate written description. Pursuant to 37 C.F.R. §
41.37(c)(1)(vii)(2006), we also affirm the rejection of claims 40-48 under 35
U.S.C. § 112, first paragraph as these claims were not argued separately.
B. Enablement rejection
Claims 39-48 stand rejected under 35 U.S.C. § 112, first paragraph, on
the basis that the Specification
while being enabling for complexes comprising Bcl-xL and
TCTP, complexes comprising fragments of Bcl-xL and
TCTP, and complexes comprising Bcl-xL and fragments of
TCTP, does not reasonably provide enablement for
complexes comprising homologues of Bcl- xL having 80%,
90% or 95% amino acid identity to Bcl-xL, or homologues
of TCTP having 80%, 90% or 95% amino acid identity to
TCTP.
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(Answer 5.) The Examiner reasons that the “specification does not teach
which amino acid residues within the disclosed "binding domains" are
necessary for the binding of Bcl-xL to TCTP, and thus it would be necessary
to first determine the tolerance of the Bcl-xL-TCTP interaction to amino
acid substations, and deletions within the binding domains” (Ans. 7). The
Examiner cites the Ibragimova reference to demonstrate that the
unpredictabilty in factors regarding protein structure and stability (see Ans.
7).
Appellants argue that “orthologs of both Bcl-xL and TCTP, i.e.,
naturally occurring Bcl-xL and TCTP proteins from non-human species,
were known in the art at the time of filing. See Exhibits A & B provided
herewith” (App. Br. 14). Appellants further contend that “specific examples
of protein fragments having the claimed features are disclosed in the
Specification” (App. Br. 14). Appellants argue that the “Specification also
provides detailed descriptions of various assays for identifying those
homologues and fragments possessing such functional features” (App. Br.
14).
Appellant “asserts that only routine experiments are required to make
and identify Bcl-xL protein homologues and fragments capable of
interacting with TCTP, and TCTP protein homologues and fragments
capable of interacting with Bcl-xL” (App. Br. 15).
In view of these conflicting positions, we frame the enablement issue before us
as follows:
Would it have required undue experimentation to use the full scope of
the claimed BCL-XL and TCTP proteins of claim 39?
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Findings of Fact
Breadth of the Claims
5. The BCL-XL and TCTP proteins of claim 39 are not limited to
any specific sequences, but encompass any complexes of proteins with
“fragments” of BCL-XL and/or TCTP, and polypeptides “having an amino
acid sequence at least 75 % identical to” either BCL-XL and/or TCTP ( see
Claim 39).
Presence of Working Examples
6. The Specification has a single working example of a BCL-XL
complex with TCTP (see Spec. 20).
Amount of Direction or Guidance Presented
7. The Specification does provide guidance on methods of
identifying interacting proteins, including the use of immunoaffinity
chromatography (Spec. 24:25-31), protein microchips (Spec. 29:14-31), the
yeast two hybrid system (Spec. 42:16-25) and antibody based techniques
(Spec. 37:10-13).
8. The Specification teaches that “it is particularly desirable to
decipher the protein binding sites. Thus, it is important that the mutations
introduced only affect protein-protein interaction and cause minimal
structural disturbances” (Spec. 68:24-26).
9. The Specification teaches that “[o]nce the pharmacophore has
been elucidated, a structural model can be established by a modeling process
that may incorporate data from NMR analysis, X- ray diffraction data,
alanine scanning, spectroscopic techniques and the like” (Spec. 70:3-5).
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State of the Prior Art and Unpredictability of the Art
10. Walensky teaches that “Apoptosis is governed by the BCL-2
family of pro- and anti-apoptotic proteins, which form a complex network of
checks and balances that dictate cell fate” (Walensky, abstract). Walensky
further notes that “BCL-2, for example, is a survival protein whose
overproduction can facilitate pathologic cell survival. Anti-apoptotic
proteins, such as BCL-2 and BCL-XL, and pro-apoptotic proteins, such as
BAK and BAX, share sequence conservation in multiple "BCL-2 homology"
(BH) domains” (Walensky, abstract).
11. Cheng, cited as Exhibit A, teaches that “we demonstrated here
that amino acid substitutions within the BH3 domain of Bcl-xL had no effect
on its death-repressor activity. This suggests that BH3 is not directly
involved in the death repressor activity of Bcl-2 homologs” (Chang 693, col.
2).
12. Cheng, cited as Exhibit A, teaches that “[a]lthough the BH3
domains of Bax and Bak facilitate cell death and mediate heterodimerization
with BclxL and Bcl-2, the role of BH3 in Bcl-2 and Bcl-xL is not clear”
(Chang 693, col. 2).
13. Bhisutthibhan, cited as Exhibit B, discloses an alignment of
TCTP protein sequences from multiple organisms (Bhisutthibhan 16194, fig.
3).
14. Yang noted that “previous studies did not identify an interaction
between TCTP and BCL-xl (Zhang et al. 2002), presumably due to the
differences in the methods and antibodies used” (Yang 4785, col. 1).
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B. Discussion of 112, first paragraph enablement rejection
We agree with the Examiner that the Specification does not provide
sufficient guidance to enable practice of the full scope of the claimed
invention without undue experimentation. The nature of the invention places
it in the class of invention which the Federal Circuit has characterized as
“the unpredictable arts such as chemistry and biology.” Mycogen Plant Sci.,
Inc. v. Monsanto Co., 243 F.3d 1316, 1330 (Fed. Cir. 2001).
The Specification expressly teaches that the BCL-XL and TCTP
polypeptides encompass fragments and proteins with 75% identity thereto.
However, the Specification does not teach what activity is required of the
complex of BCL-XL and TCTP given the broad claims (FF 5) and the prior
art of Walensky and Chang suggest that BCL-XL may have multiple roles
(FF 10-12).
While there is a single working example in the Specification (FF 6),
the guidance of the Specification focused on methods of screening and
provided no disclosure of function protein regions for either BCL-XL or
TCTP (FF 7-9).
The prior art demonstrates that no functional region was known for
TCTP and that the BH3 region of BCL-XL was unpredictable in its activity,
since mutations in the BCL-XL BH3 region had no effect on death repressor
activity (FF 11-13). The post filing date art of Yang further supports the
unpredictability and difficulties in establishing which regions, if any of
TCTP and BCL-XL interact, since Yang notes that prior studies by Zhang
had failed to identify the TCTP interaction with BCL-XL (FF 14). This
directly supports the “how to use” enablement issue since until the
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disclosure by Yang of the functional regions of TCTP and BCL-XL, it
would have been unpredictable whether any protein with 75% identity to
TCTP or BCL-XL would have formed the claimed complex.
We are not persuaded by Appellant’s reliance on Invitrogen. The
issue in Invitrogen was that enablement for the claims was “not limited by
the method of achieving the mutation.” Invitrogen, 429 F3d at 1071. In the
current situation, the issue is not whether other methods could be used to
obtain the mutation but rather that undue experimentation would have been
required to determine which of the 75% or more identical proteins would
retain the interaction regions necessary to form the TCTP and BCL-XL
complex.
We are also not persuaded by Appellant’s argument that “the
Specification is replete with explanations of methods for making such
homologues and fragments” (App. Br. 14). The enablement concern is not
whether modifications of BCL-XL and TCTP can be made, but whether
such homologues and fragments will form the complex between the proteins.
This undue experimentation is particularly evident given Yang’s disclosure
that a contemporaneous experimenter, Zhang, did not detect an interaction
between TCTP and BCL-XL (FF 14). Additionally, the teaching by Cheng
that mutations in the BH3 domain had little functional effect on BCL-XL
also support a conclusion of undue experimentation since mutations in BCL-
XL were unpredictably related to function, even in conserved domains (FF
11).
We affirm the rejection of claim 39 under 35 U.S.C. § 112, first
paragraph. Pursuant to 37 C.F.R. § 41.37(c)(1)(vii)(2006), we also affirm
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the rejection of claims 40-48 under 35 U.S.C. § 112, first paragraph as these
claims were not argued separately.
C. 35 U.S.C. § 102(b) rejection over Gachet
The Examiner contends that “Gachet et al disclose that TCTP is also
referred to as P23 . . . Gachet et al disclose that ‘P23: is a cytoplasmic
protein that occurs in complexes of 100-150 kDa’ . . . Gachet et al disclose
that said complexes were isolated from HeLa cells” (Ans. 10). The
Examiner concludes that a “complex comprising detectably labeled TCTP
would inherently comprise Bcl-xL” (Ans. 10). The Examiner also notes that
“Yang et al (Oncogene, 2005, Vol. 24, pp. 4778-4768) provides evidence
that in HeLa cells, TCTP and Bcl-xL are co-localized both in the cytosol and
the mitochondria (page 4779, second column, lines 2-18)” (Ans. 15).
Appellant argues that the “Examiner has not shown that Bcl-xL was
necessarily present in the complexes isolated in Gachet” (Rep. Br. 16).
Appellant contends that “TCTP has at least 7 interacting partners beside Bcl-
xL and itself . . . there is strong evidence to show the protein or proteins in
the complex with TCTP of Gachet could have been any of eight different
proteins besides Bcl-xL, and thus was (were) not necessarily Bcl-xL” (Rep.
Br. 16). Appellant argues that the “Examiner's proffered evidence that
TCTP and Bcl-xL co-localize in the cytoplasm and mitochondria of HeLa
cells falls far short of proving that Bcl-xL was necessarily present in
complex with TCTP in Gachet” (Rep. Br. 16).
In view of these conflicting positions, we frame the anticipation issue
before us as follows:
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Would the TCTP containing complexes of Gachet inherently have
comprised BCL-XL?
Findings of Fact
15. Gachet teaches that
P23 is eluted over a fairly wide range of fractions starting
significantly earlier than the elution of the pure recombinant
protein. Calibration of the column showed that the P23
containing fractions correspond to a molecular mass range
from about 40 to 150 kDa, whereas pure recombinant P23
elutes at about 40-60 kDa.

(Gachet 1260, col. 2.)
16. Yang teaches that “TCTP and Bcl-xL are partially colocalized
in the cytosol” (Yang 4779, col. 2).
17. The Specification teaches that “interactions between BCL-XL
and TCTP will result in the formation of protein complexes both in vitro and
in vivo that contain BCL-XL and TCTP” (Spec. 6:21-22).
18. The Specification teaches that the “protein complexes formed
under physiological conditions can mediate the functions and biological
activities of BCL-XL and TCTP” (Spec. 6:23-24).
C. Discussion of § 102(b) rejection over Gachet
We agree with the Examiner that Gachet as evidenced by Yang
provides sufficient information for a prima facie case of inherent
anticipation. Gachet isolates protein complexes of TCTP (termed P23) from
Hela cells which include TCTP and additional proteins (FF 15). Yang
evidences that Bcl-xl is present in HeLa cells in the same cellular
compartments as TCTP (FF 16). Appellant’s Specification shows that BCL-
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XL and TCTP will form protein complexes under physiological conditions
(FF 17-18).
We are not persuaded by Appellants' argument that the Gachet
composition is necessarily different than that claimed because “TCTP has at
least 7 interacting partners beside Bcl-xl” (Rep. Br. 16). Appellant does not
show that these proteins are located in same cellular compartment, the
cytosol, as TCTP and Bcl-xl. However, even if we accept Appellant’s logic
that seven other proteins are present, then the isolated complexes of TCTP
must represent competition products with all complexes of all the proteins
present in the cellular compartment. See Atlas Powder Co. v. Ireco, Inc.,190
F.3d 1342, 1348 (Fed. Cir. 1999) (“The public remains free to make, use, or
sell prior art compositions or processes, regardless of whether or not they
understand their complete makeup of the underlying scientific principles
which allow them to operate.”).
We are not persuaded by Appellant’s argument that “skilled artisans,
who were most certainly aware of Gachet's findings nevertheless deemed the
Bcl-xL- TCTP interaction novel six years after Gachet!” (Rep. Br. 16). This
argument fails to address the inherent nature of the interaction, since if
Gachet did not look for the interaction with BCL-xl, the mere presence of
the complexes isolated from the superose column would not teach the
presence of BCL-xl, but “[i]t matters not that those of ordinary skill
heretofore may not have recognized these inherent characteristics.” In re
Cruciferous Sprout Litigation, 301 F.3d 1343, 1350 (Fed. Cir. 2002).
In demonstrating that Gachet discloses protein complexes with TCTP
that are derived from the same cell type and same cell compartment as BCL-
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xl (FF 15-16) and where the Specification admits that these proteins interact
under physiological conditions (FF 17-18), we think the Examiner has
reasonably shifted the burden to Appellants to demonstrate that TCTP
complexes isolated from HeLa cells does not contain BCL-xl. As the court
noted in Best, “[w]here, as here, the claimed and prior art products are
identical or substantially identical, or are produced by identical or
substantially identical processes, the PTO can require an applicant to prove
that the prior art products do not necessarily or inherently possess the
characteristics of his claimed product.” In re Best, 562 F.2d 1252, 1255
(CCPA 1977).
We affirm the rejection of claim 39 under 35 U.S.C. § 102(b) over
Gachet. Pursuant to 37 C.F.R. § 41.37(c)(1)(vii)(2006), we also affirm the
rejection of claims 40-48 under 35 U.S.C. § 112, first paragraph as these
claims were not argued separately.
CONCLUSION
In summary, we affirm the rejection of claim 39 under 35 U.S.C. §
112, first paragraph, written description and enablement. We also affirm the
rejection of claim 39 under 35 U.S.C. § 102(b). Pursuant to 37 C.F.R. §
41.37(c)(1)(vii)(2006), we also affirm the rejection of claims 40-48 as these
claims were not argued separately.
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)(iv)(2006).
AFFIRMED

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Appeal 2008-2711
Application 10/122,573

dm

Myriad Genetics Inc.
Intellecutal Property Department
320 Wakara Way
Salt Lake City, UT 84108

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