Ex Parte SUN et al

Patent Trials and Appeals Board

Jan 17, 2019

13333830 - (D) (P.T.A.B. Jan. 17, 2019)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
13/333,830 12/21/2011
25225 7590 01/22/2019
MORRISON & FOERSTER LLP
12531 HIGH BLUFF DRIVE
SUITE 100
SAN DIEGO, CA 92130-2040
FIRST NAMED INVENTOR
Samuel Sai Ming SUN
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.
549072000900 7011
EXAMINER
WORLEY, CATHY KINGDON
ART UNIT PAPER NUMBER
1662
NOTIFICATION DATE DELIVERY MODE
01/22/2019 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):
PatentDocket@mofo.com
EOfficeSD@mofo.com
pair_mofo@firsttofile.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte SAMUEL SAI MING SUN and LI TIAN 1
Appeal2017-002121
Application 13/333,830
Technology Center 1600
Before TA WEN CHANG, JOHN E. SCHNEIDER, and
TIMOTHY G. MAJORS, 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
method to obtain a desired protein from plants, plant parts, or plant cells,
which have been rejected as obvious. We have jurisdiction under 35 U.S.C.
§ 6(b ).
We AFFIRM.
STATEMENT OF THE CASE
The Specification states that purification of target proteins from plant
samples is estimated to account for 80% of the production costs in large-
1 Appellants identify the Real Party in Interest as The Chinese University of
Hong Kong. (Appeal Br. 1.)
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Application 13/333,830
scale industrial production of recombinant therapeutic proteins by plant-
based bioreactors. (Spec. ,r 3.) The Specification teaches that "[t]raditional
protein purification methods involve expression of target proteins as fusion
to affinity tags," but these methods "suffer from the difficulty and high cost
of scaling-up of the required affinity chromatography." (Id. ,r 4.) The
Specification also describes other purification strategies using fusion tags;
however, the Specification states that proteolytic cleavage is often required
to remove fusion tags, and the "additional cleavage step results in high cost
due to the cost of protease and ... an extra step in its removal, in addition to
the potential occurrence of non-specific protein cleavage." (Id.)
According to the Specification, "development of a simple and cost-
effective downstream recombinant protein purification system is thus highly
desirable." (Id.) The Specification further describes "[t]he elastin-like
polypeptide (ELP)-intein system [as] a simple and efficient method for
purification of protein," wherein ELP proteins have the property of
"temperature-sensitive phase transition" and inteins are "a kind of protein
splicing element [that] catalyzes self-cleavage." (Id. ,r,r 5-6.)
Claims 1, 42, 52, and 53 are on appeal. Claim 1 is illustrative and
reproduced below:
1. A method to obtain a desired protein from plants,
plant parts, or plant cells which method comprises
(a) preparing an extract of proteins from said plants,
plant parts or plant cells that stably produce said desired protein
as a fusion protein from a recombinant expression system that
produces said fusion protein, wherein said fusion protein
comprises at either the N-terminus or C-terminus or both of the
desired protein, an ELP-intein tag which tag comprises an
elastin-like polypeptide (ELP) domain and an intein splicing
element (intein) wherein the intein is between the N- and/or C-
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terminus or both of the desired protein and the ELP domain;
and
wherein any tag at the N-terminus of the desired protein
is cleaved at the C-terminus of the intein and any tag at the C-
terminus of the desired protein is cleaved at the N-terminus of
the intein; and
wherein the codons of the recombinant expression system
are optimized for expression in plants;
(b) optionally removing insoluble materials from said
extract;
( c) aggregating the fusion proteins and separating
them from the remainder of the extract;
( d) resolubilizing the fusion proteins into an aqueous
solution;
optionally repeating steps ( c) and ( d);
( e) effecting cleavage of the fusion protein;
(f) separating the desired protein from the tag(s);
wherein the ELP domain contains at least 20 ELP units; and
wherein the fusion protein further includes one or more
linker sequences between the desired
protein and intein and/ or intein and ELP and/ or
among ELP units.
(Appeal Br. 10 (Claims App.).)
The Examiner rejects claim 1 under pre-AIA 35 U.S.C. § I03(a) as
being unpatentable over Wood2 and Yadav. 3 (Final Act. 10; Ans. 12.)4
2 Wood et al., US 2006/0263855 Al, published Nov. 23, 2006.
3 Yadav et al., US 2004/0172688 Al, published Sep. 2, 2004.
4 Claim 1 was originally rejected as obvious over Wood, Yadav, and
Natarajan et al., Comparison of Protein Solubilization Methods Suitable for
Proteomic Analysis of Soybean Seed Proteins, 342 ANALYTICAL
BIOCHEMISTRY 214 (2005). The Examiner modified the rejection in the
Answer to remove Natarajan in light of the after-final amendments
Appellants submitted on April 13, 2016. (Ans. 12.)
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The Examiner rejects claims 42 and 52 under pre-AIA 35 U.S.C.
§ I03(a) as being unpatentable over Wood, Yadav, Vierstra, 5 and Sun. 6
(Final Act. 13; Ans. 13.)7
The Examiner rejects claim 53 under pre-AIA 35 U.S.C. § I03(a) as
being unpatentable over Wood, Yadav, Vierstra, Sun, and Ooi. 8 (Final Act.
20; Ans. 13.)9
I.
Issue
The Examiner has rejected claim 1 as obvious over Wood and Yadav.
The Examiner has rejected claims 42 and 52 as obvious over Wood, Yadav,
5 Vierstra et al., US 6,455,759 Bl, issued Sep. 24, 2002.
6 Sun et al., US 2004/0268431 Al, published Dec. 30, 2004.
7 Claims 52 and 53 were added in the April 13, 2016 after-final amendments.
However, the Examiner rejected them "for the same grounds that were
applied to the previously rejected claims 42 and 49, respectively, with the
modification that the rejection of claim 53 no longer requires the reference
of Huang et al., [US 7,417,178 B2, issued Aug. 26, 2008,] which was
required by cancelled claim 49." (Ans. 13.)
8 Linda S.M. Ooi et al., Purification and Characterization of Non-Specific
Lipid Transfer Proteins from the Leaves of Pandanus amaryllifolius
(Pandanaceae), 27 PEPTIDES 626 (2006).
9 The Examiner stated in the Answer that claim 5 3, which was added in the
Apr. 13, 2016 after-final amendment, is "rejected for the same ground[] that
[was] applied to previously rejected claim[] ... 49 ... ; with the
modification that the rejection of claim 53 no longer requires the reference
of Huang et al. which was required by cancelled claim 49." (Ans. 13.)
Claim 49 was rejected as obvious over Wood, Yadav, Huang, and Ooi.
(Final Act. 20.) However, since claim 53 depends from claim 42, which was
rejected over Wood, Yadav, Vierstra, and Sun, we understand the rejection
of claim 53 to be over Wood, Yadav, Vierstra, Sun, and Ooi. Appellants
appear to share this understanding. (Reply Br. 4.)
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Vierstra, and Sun. The same issue is dispositive as to these rejections; we
therefore discuss the rejections together.
The Examiner finds that Wood discloses almost all of the limitations
of claim 1 and specifically suggests plant cells as potential hosts for
expression of its fusion protein, but does not exemplify expression of a
fusion protein in a plant, plant part, or plant cell, as required by claim 1.
(Final Act. 8.) However, the Examiner finds that Yadav teaches transgenic
plants expressing fusion proteins comprising inteins, as well as expression
vectors modified to contain plant optimized codons and operable in plant
cells to express a fusion protein. (Id. at 8-9.) The Examiner concludes that,
[ a ]t the time the invention was made, it would have been
obvious and within the scope of one of ordinary skill in the
art to follow the suggestion of Wood et al to use plant cells
as host cells, and it would have been obvious to use a plant
expression system such as the 35S/NOS system taught by
Yadav et al. Given the success of Wood et al in producing
ELP-intein-protein fusions and utilizing this system to
produce, cleave, and purify the protein of interest, and
give[ n] the success of Yadav et al in producing intein-
protein fusions in a plant system, one would have had a
reasonable expectation of success in moving the system of
Wood et al into a plant system.
(Id. at 9.)
Appellants concede that "Wood discloses the same process steps as
set forth in claim 1" and "exemplifies this [process] in prokaryotes."
(Appeal Br. 5.) Appellants also do not dispute that Wood "speculates" that
"[its] process could also be applied to proteins from plants." (Id.)
Appellants contend, however, that "production [ of recombinant fusion
proteins] in plants is so unpredictable that the artisan would simply dismiss
[Wood's suggestion] as aggressive patent drafting." (Id.)
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Appellants do not advance any additional arguments with respect to
the rejection of claims 42 and 52 over Wood, Yadav, Vierstra, and Sun in
the Appeal Brief. 10 (Appeal Br. 8.) Therefore, the issue with respect to both
rejections is whether a skilled artisan would have had a reasonable
expectation of success in using Wood's method of expressing fusion
proteins in plants, plant parts, or plant cells.
Analysis
We agree with the Examiner that claim 1 is obvious over Wood and
Yadav. Only those arguments made by Appellants in the briefs have been
considered; arguments not so presented are waived. See 37 C.F.R.
§ 4I.37(c)(l)(iv) (2015); see also Ex parte Borden, 93 USPQ2d 1473, 1474
(BP AI 2010) (informative) ("Any bases for asserting error, whether factual
or legal, that are not raised in the principal brief are waived.").
As discussed above, Appellants concede that "Wood discloses the
same process steps as set forth in claim 1" and "exemplifies this [process] in
prokaryotes." (Appeal Br. 5.) Wood also states that
[ o ]ne advantage of [its] invention is that it can be used with
many different types of host cells. For instance, it is
envisioned that the purification system can be used with a
prokaryotic cell or a eukaryotic cell. Preferably, the host
cell is a bacterial cell, a fungal cell, a mammalian cell, an
10 In the Reply Brief, Appellants do make additional arguments specifically
directed to claims 42 and 52. These arguments are waived, however,
because they were not presented in the opening brief, thereby denying the
Board the benefit of the Examiner's response, and no showing of good cause
was made by Appellants to explain why the late argument should be
considered by the Board. See 3 7 C.F .R. § 41.41 (b )(2 ); Cf Optivus
Technology, Inc. v. Ion Beam Applications S.A., 469 F.3d 978, 989 (Fed. Cir.
2006) ( argument raised for the first time in the Reply Brief that could have
been raised in the opening brief is waived).
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insect cell, a yeast cell, or a plant cell. In one embodiment,
the host cell is a bacterial cell, such as E. coli. More
particularly, it is envisioned that the invention can be used
successfully in mammalian cells.
(Wood ,r 57 ( emphasis added).)
Appellants contend that claim 1 is not obvious over Wood and Y adav
because "it [ would not have been] predictable that fusion proteins
[ comprising] intein and at least 20 ELP units could be produced
recombinantly in plants and extracted in sufficient quantity to subject them
to the macroscopic scale purification process set forth in claim 1." (Appeal
Br. 4.)
We are not persuaded. As an initial matter, as the Examiner points
out, Claim 1 does not require any particular quantity of proteins to be
produced and extracted. (Interview Summary (Apr. 22, 2016).) Appellants
contend that "there is no disagreement that the steps set forth in claim 1 are
done on a macroscopic scale and therefore sufficient fusion proteins must be
produced to permit application of these steps." (Appeal Br. 4; see also id. at
5.) We are not persuaded, however, because claim 1 also does not contain
limitations regarding the scale of the process. "[W]hile it is true that claims
are to be interpreted in light of the specification ... , it does not follow that
limitations from the specification may be read into the claims .... [T]he
claims define the invention." Sjolund v. Musland, 847 F.2d 1573, 1581-82
(Fed. Cir. 1988).
Assuming for the sake of argument that "there is no disagreement that
the steps set forth in claim 1 are done on a macroscopic scale and therefore
sufficient protein must be produced to permit application of these steps"
(Appeal Br. 4), we nevertheless agree with the Examiner that a skilled
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artisan would have had a reason to produce Wood's recombinant protein in a
plant cell, as required by claim 1, with a reasonable expectation of success,
in light of Wood's explicit disclosure that its invention may be used with
many different types of host cells including plant cells and Yadav's
disclosure of transgenic plants expressing fusion proteins comprising inteins
and plant optimized codons. (Wood ,r 57; Yadav Abstract, ,r 19.)
Appellants contend that there is no documentation in support of the
Examiner's position that "it is a routine matter to produce large amounts of
recombinant proteins in plants in view of successes in the art in producing,
for example, pharmaceuticals." (Appeal Br. 4, 7.)
We are not persuaded. The Examiner points to prior art references
that disclose production of significant amounts of recombinant proteins in
plants. (Ans. 13-14; see also e.g., Sun Abstract (describing a "plant
production method ... [having] promising potential to mass-produce some
of the most expensive biopharmaceuticals of restricted availability in a much
cheaper way"); Huang 6:40-43 ( describing "a mature, transgenic monocot
seed that yields, by extracting ground seed with an aqueous medium, a total
soluble protein fraction containing at least 3% by total protein weight of a
human milk protein" and further describing an embodiment wherein "the
total soluble protein fraction contains at least 20% by total protein weight of
the human milk protein").) Moreover, the Specification itself states that
[ u ]sing transgenic plants for large-scale production of pharmaceutical
proteins has been demonstrated as an attractive system with the
advantages of low cost, high yield, easy harvest and reduced health
risks in comparison to traditional microbial and mammalian
bioreactors, and many valuable recombinant therapeutic proteins have
been expressed in transgenic plants as proof-of-concept and feasibility
demonstrations.
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(Spec. ,r 3.)
In the Reply Brief, Appellants contend that the prior art "shows that
high level heterologous protein production in plants is actually a problem"
and teaches that "in order to achieve high levels of expression, the
conditions must be manipulated in ways that are specific to each protein and
to each type of plant." (Reply Br. 2-3.) Appellants cite Patel1 1 and
Streatfield 12 in support of their argument.
We are not persuaded. Appellants concedes that Patel "suggests using
the ELP unit in multiple copies to enhance expression." (Reply Br. 3.)
However, Appellants argue that Patel does not mention "coupling [ELP
units] to the basic protein to be produced with an intein sequence" and
further argue that, while Patel teaches enhancing expression with an 11.3 kD
ELP tag, it teaches doing so "only in conjunction with an ER retention
signal." (Id.) However, the fact that all of the limitations in a claim are not
described in a single reference does not suffice to render the claim non-
obvious. Likewise, while Patel does state that "it is clear that the 11.3 kDa
ELP tag in conjunction with an ER retention signal[] was instrumental in
increasing the accumulation of three quite different target proteins in
tobacco leaves" (Patel 248, left column), claim 1 does not preclude inclusion
of an ER retention signal.
Appellants also argue that Streatfield "makes it clear that ...
obtaining practical amounts of recombinant proteins in plants is not
11 Patel et al., Elastin-Like Polypeptide Fusions Enhance the Accumulation
of Recombinant Proteins in Tobacco Leaves, 16 TRANSGENIC RESEARCH 239
(2007).
12 Stephen J. Streatfield, Review Article, 5 PLANT BIOTECHNOLOGY J. 2
(2007).
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straightforward, but requires manipulation of conditions that are unique to
individual situations." (Reply Br. 3.) We are not persuaded. Streatfield
teaches that "[ s ]trategies have been developed to increase the levels of
recombinant proteins for plant production systems" and that "[t]he type of
system used for protein production specifies the range of approaches that can
be applied." (Streatfield 4, 1eft column.) Appellants have pointed to no
specific teachings in Streatfield that suggests a skilled artisan would not
have a reasonable expectation of success in adapting known strategies for
increasing recombinant protein levels in plants to produce the recombinant
protein described in \Vood. In this regard, we emphasize that "obviousness
cannot be avoided simply by a showing of some degree of unpredictability
in the art so long as there was a reasonable probability of success":
"[E]xpectation of success need only be reasonable, not absolute." Pfizer,
Inc. v. Apotex, Inc., 480 F.3d 1348, 1364 (Fed. Cir. 2007).
Appellants contend that, while Wood provides "a speculation that it
would be possible to apply [its] process to recombinant plant-produced
fusion proteins," the production of fusion proteins in plants is "so
unpredictable that the artisan would simply dismiss [Wood's suggestion] as
aggressive patent drafting." (Appeal Br. 5.) We are not persuaded. As
discussed, Appellants provide no persuasive evidence to support their
contention that a skilled artisan would not have had a reasonable expectation
of success of applying Wood's process to recombinant plant-produced
fusion proteins to arrive at the claimed invention. "Attorneys' argument is
no substitute for evidence." Johnston v. IVAC Corp., 885 F.2d 1574, 1581
(Fed. Cir. 1989).
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Appellants argue that the Examiner's inclusion of Y adav indicates
that the Examiner agrees that Wood's suggestion of applying its process to
recombinant plant-produced fusion proteins is insufficient to establish a
prima facie case of obviousness as to claim 1. (Appeal Br. 5, 7; Reply Br.
2.) We are not persuaded. Appellants cite no authority, and we are aware of
none, that the Examiner's citation of a combination of art in a§ 103
rejection may or should be treated as a concession that a subset of the
combination is insufficient to invalidate the claim( s) at issue. Indeed, the
predecessor to our reviewing court has suggested the opposite, in holding
that the Board may rely on less than all of the references relied upon by the
Examiner. In re Bush, 296 F.2d 491,496 (CCPA 1961).
Appellants argue that Y adav "falls short of establishing predictability
for the fusion proteins of the present claims," because Yadav's fusion
proteins do not contain ELP units. (Appeal Br. 6.) Appellants argue that,
because the "at least 20 ELP units" required by claim 1 would add to the
fusion protein "a 100-amino acid 'tail' ... contain[ing] 20 prolines," and
because proline is "instrumental in determining protein conformation and
stability," a skilled artisan "would not consider it predictable that plants
would be a successful host for producing recombinant proteins to be
subjected to the purification procedure of claim 1." (Id.)
We are not persuaded. As already discussed, arguments from
attorneys cannot take the place of evidence, Johnston, 885 F .2d at 15 81
(Fed. Cir. 1989), and Appellants cite insufficient persuasive evidence that
supports their attorneys' arguments. In addition, Appellants attack Y adav
individually. However, "[ n ]on-obviousness cannot be established by
attacking references individually where the rejection is based upon the
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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).
Finally, citing to paragraphs 8-13, Appellants argue that the
disclosures in the Specification supports their contention regarding the lack
of reasonable expectation of success. (Appeal Br. 6, 7.)
We are not persuaded. Paragraphs 8-11 state that, while the prior art
discloses "application of ELP or intein in the alternative in transgenic
plants," Appellants are "not aware of any report on the use of ELP and intein
in combination in transgenic plants." (Spec. ,r,r 8-11.) However, as already
discussed, the mere fact that all of the limitations of a claim are not found in
a single prior art reference does not suffice to show that the claim is non-
obvious. Neither have Appellants argued or provided evidence of the
existence of any secondary considerations of non-obviousness, such as
failure of others.
Paragraphs 12 and 13 describe difficulties that may be encountered
and/or have been encountered by Appellants in practicing the claimed
invention. (Spec. ,r,r 12-13.) However, the Specification suggests that such
difficulties may be overcome simply by "routine optimization" of extraction
and purification conditions and procedures. (Id. ( stating that "[ r ]outine
optimization of extraction and purification procedures ... may be needed to
purify target proteins from plant samples by the ELP-intein system" after
describing potential issues in practicing the claimed method).) Thus, we are
not persuaded that the Specification supports Appellants' attorney argument
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that a skilled artisan would not have had reasonable expectation of success
in combining Wood and Yadav to arrive at the claimed invention. 13
Accordingly, we affirm the Examiner's rejection of claim 1. Claims
42 and 52, which are not separately argued, fall with claim 1. 37 C.F.R.
§ 4I.37(c)(l)(iv).
II.
Issue
The Examiner has rejected claim 53 as obvious under Wood, Yadav,
Vierstra, Sun, and Ooi. Claim 53 depends from claim 42, which is
reproduced below:
42. The method of claim 1:
(i) wherein the plants, plant parts or plant cells are
tobacco and the expression system comprises in the 5' to 3'
orientation: a 35S promoter, a sequence encoding ubiquitin, a
sequence encoding a phaseolin signal peptide, a sequence
encoding a desired protein, a sequence encoding an intein, a
13 In the Appeal Brief, Appellants mention certain other limitations of claim
1 - in particular that "the fusion protein further includ[ing] one or more
linker sequences between the desired protein and intein and/ or intein and
ELP and/ or among ELP units," and that "codons be optimized for expression
in plants." (Appeal Br. 7.) Appellants do not dispute that those limitations
are disclosed in either Wood or Y adav and argue only that "Wood is directed
to production of ... proteins in bacteria" and that Y adav does not teach
plant-optimized codon "with the view of providing successful production of
the [claimed] fusion protein as opposed to simply the intein/desired protein
fusion." (Id.) We are not persuaded for the reasons already discussed:
Based on the record before us, we agree with the Examiner that a skilled
artisan would have had reason to combine Wood and Y adav to arrive at the
claimed invention, with a reasonable expectation of success, and Appellants'
arguments, which amount to an attempt to establish non-obviousness by
attacking the references individually, accordingly fail. In re Merck & Co.,
800 F.2d at 1097.
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linker sequence, a sequence encoding at least 20 ELP repeats
and a NOS terminator sequence; or
(ii) wherein the plants, plant parts or plant cells are rice
and the expression system comprises in the 5' to 3 ' orientation
a glutelin promoter, a sequence encoding a phaseolin signal
peptide, a sequence encoding at least 20 ELP repeats, a linker
sequence, a sequence encoding an intein, a sequence encoding a
desired protein and a NOS terminator sequence.
(Appeal Br. 10-11 (Claims App.).) Claim 53 claims "[t]he method of
claim 42 wherein in (ii) the desired protein is Pandanus lectin
protein." (Id. at 11 (Claims App.).)
The Examiner finds that the combination of Wood, Yadav, Viestra,
and Sun suggests all of the limitations of claim 53, except that the
combination does not teach a Pandanus lectin protein. (Final Act. 14--16
(discussing claim 42), 21-22 (discussing cancelled claim 49), Ans. 13 (claim
53 rejected on same ground as cancelled claim 49).) The Examiner finds,
however, that Ooi teaches the purification and characterization of a
Pandanus lectin protein. (Final Act. 22.) The Examiner concludes that it
would have been obvious to a skilled artisan to obtain a Pandanus lectin
protein as taught by Ooi using the method suggested by Wood, Yadav,
Viestra, and Sun, because this would be "an obvious combination of known
elements that produced predictable results." (Id. at 22.)
Appellants contend that claim 53 is patentable for the same reasons as
discussed above with respect to claim 1, and further contend that claim 53 is
patentable for the additional reason that "Ooi does not suggest recombinant
production of Pandanus lectin." (Appeal Br. 9.)
The issue with respect to this rejection is whether it would have been
obvious to a skilled artisan to produce a Pandanus lectin protein using the
method suggested by the combination of Wood, Yadav, Viestra, and Sun.
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Analysis
We agree with the Examiner that claim 53 is obvious over Wood,
Yadav, Vierstra, Sun, and Ooi. Only those arguments made
by Appellants in the briefs have been considered; arguments not so
presented are waived. See 37 C.F.R. § 4I.37(c)(l)(iv) (2015); see also Ex
parte Borden, 93 USPQ2d at 1474.
As to Appellants' contention that claim 53 is patentable for the same
reasons as discussed above with respect to claim 1, we are not persuaded for
the reasons already discussed with respect to claim 1.
Appellants further contend that
[ c ]laim 53 is patentable for the additional reason that there
is no evidence in the art that Pandanus lectin is a candidate
for recombinant production in plants. As is apparent from
the document itself, Pandanus lectin is not produced
recombinantly as a foreign protein in plants, but rather
from its native source, Pandanus amaryllifolius. Ooi does
not provide incentive to produce Pandanus lectin
recombinantly in plants, and claim 53 is patentable for this
additional reason.
(Appeal Br. 8.)
We are not persuaded. Again, "[n]on-obviousness cannot be
established by attacking references individually where the rejection is based
upon the teachings of a combination of references." In re Merck & Co., 800
F .2d at 1097. As the Examiner points out, the other references cited in the
rejection suggest the desirability of plants as a system for producing
recombinant proteins. (Ans. 16; see also e.g., Wood ,r 57 (stating that an
advantage of its inventive purification system is that it can be used with
many different types of host cells, including preferably a plant cell); Y adav
,r 11 (stating that "[p ]lants are increasingly being looked to as platforms for
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the production of materials foreign to plant systems"); Vierstra 1: 18-23
( stating that "it has now become common practice to create ... transgenic
plants"); Sun ,r 5 (stating that "[t]he commercial potential of using
transgenic plants as production systems is very high due to the unique and
outstanding characteristics of the plants").) This suggestion, combined with
Ooi's suggestion of Pandanus lectin14 as a protein of interest (see e.g., Ooi
626-627 (identifying proteins as non-specific lipid transfer proteins and
suggesting possible biological functions and potential application)), provides
a reason for a skilled artisan to combine Ooi with Wood, Yadav, and
Vierstra to arrive at the claimed invention, in the absence of evidence to the
contrary. 15
Accordingly, we affirm the Examiner's rejection of claim 53.
SUMMARY
For the reasons above, we affirm the Examiner's decision rejecting
claims 1, 42, 52, and 53.
14 In their Reply Brief, Appellants argue for the first time that Ooi does not
disclose Pandanus lectin at all. (Reply Br. 5.) While we acknowledge that
Ooi describes the proteins it purifies as "lectin-like" rather than lectins (Ooi
630, right column), no showing of good cause was made by Appellants to
explain why this argument was not presented in the opening brief, thereby
denying the Board the benefit of the Examiner's response. Accordingly, we
decline to consider this argument, which is waived. See 37 C.F.R. §
4I.41(b)(2); Cf Optivus Technology, 469 F.3d at 989.
15 For instance, Appellants have not suggested that using the method
described in Wood to purify a recombinant Pandanus lectin from a plant
host cell produces unexpected results.
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TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).
AFFIRMED
17