Ekkehard Neuhaus et al.

Patent Trials and Appeals Board

Sep 4, 2019

13637908 - (D) (P.T.A.B. Sep. 4, 2019)

UNITED STATES PATENT AND TRADEMARK OFFICE
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
13/637,908 12/10/2012 Ekkehard Neuhaus 4297U.001 8768
21917 7590 09/04/2019
MCHALE & SLAVIN, P.A.
2855 PGA BLVD
PALM BEACH GARDENS, FL 33410
EXAMINER
LOGSDON, CHARLES
ART UNIT PAPER NUMBER
1662
NOTIFICATION DATE DELIVERY MODE
09/04/2019 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):
uspatents@mchaleslavin.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
____________

Ex parte EKKEHARD NEUHAUS, OLIVER TRENTMANN,
ALEXANDRA WORMIT, and KARINA WINGENTER1
____________

Appeal 2018-008039
Application 13/637,908
Technology Center 1600
____________

Before ULRIKE W. JENKS, JOHN G. NEW, and MICHAEL A. VALEK,
Administrative Patent Judges.

NEW, Administrative Patent Judge.

DECISION ON APPEAL

1 Appellants identify Technische Universität Kaiserslautern as the real party-
in-interest. App. Br. 3.
Appeal 2018-008039
Application 13/637,908

2
SUMMARY
Appellants file this appeal under 35 U.S.C. § 134(a) from the
Examiner’s Non-Final Rejection of claims 1–3, 5, 6, 11, 12, 15–17, and 19–
21 as unpatentable under U.S.C. § 112, first paragraph, for lack of written
descriptive support.
Claims 1–3, 5, 6, 11, 12, 15–17, and 19–21 also stand rejected as
unpatentable under U.S.C. § 112, first paragraph, for lack of enablement.
Claims 1–3, 5, 6, 11, 12, 15–17, and 19–21 stand further rejected as
unpatentable under U.S.C. § 103(a) as being obvious over the combination
of A. Wormit et al., Molecular Identification and Physiological
Characterization of a Novel Monosaccharide Transporter from Arabidopsis
Involved in Vacuolar Sugar Transport, 18 THE PLANT CELL, 3476–90,
(2006) (“Wormit”) and J. Tjaden et al., A. thaliana mRNA for sugar
transporter, GenBank Accession Z50752 (1996) (“GenBank”).
We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.

NATURE OF THE CLAIMED INVENTION
Appellants’ invention is directed to a method of enhancing the seed
yield and promoting the growth of monocotyledonous or dicotyledonous
plants by overexpression of tonoplast monosaccharide transporter (“TMT”)
protein in isogenic or transgenic plant cells. Abstr.

REPRESENTATIVE CLAIM
Claim 1 is representative of the claims on appeal, and recites:

Appeal 2018-008039
Application 13/637,908

3
Claim 1. A method of enhancing seed yield or promoting
growth of monocotyledonous or dicotyledonous plants
comprising introducing into cells of said monocotyledonous or
dicotyledonous plants an exogenous nucleic acid operatively
linked to at least one promoter which results in overexpression
of TMT (tonoplast monosaccharide transporter) protein, or a
functional variant thereof, the functional variant exhibiting a
sequence homology with an amino acid sequence of Arabidopsis
thaliana TMT (tonoplast monosaccharide transporter) protein
TMT1 according to SEQ ID NO:1 which results in transporting
sugar from cell cytoplasm into a cell vacuole and having
enhanced seed yield or growth promotion of monocotyledonous
or dicotyledonous plants compared to a wild-type plant of the
same species.

App. Br. Claim App’x 1.

ISSUES AND ANALYSES
We are persuaded by, and adopt, the Examiner’s findings, reasoning
and conclusion that Appellants’ claims lack written descriptive support, are
not enabled, and are prima facie obvious over the combined cited prior art.
We address the arguments raised by Appellants below.

A. Rejection of the claims as lacking written descriptive support under 35
U.S.C. § 112, first paragraph

Issue
Appellants argue that the Examiner erred in concluding that
Appellants’ Application has not described a functional variant of the
Arabidopsis tonoplast monosaccharide transporter 1 (“TMT1”) protein with
some amino acid sequence identity to SEQ ID NO: 1, with the ability to
increase seed yield when expressed in plants and transport sugar from the
Appeal 2018-008039
Application 13/637,908

4
cell cytoplasm into a cell vacuole within the full scope of the claims. App.
Br. 5.

Analysis
The Examiner notes that the claims on appeal have been amended to
require a functional variant of the Arabidopsis TMT1 protein with some
sequence identity to SEQ ID NO:1 and the ability to increase seed yield
when expressed in plants, wherein overexpression of the protein results in
transporting sugar from the cell cytoplasm into a cell vacuole. Non-Final
Act. 3. The Examiner finds that functional variants with some sequence
identity to SEQ ID NO:1 encompass a vast genus of polypeptides; the claims
are not limited to naturally-occurring sequences and therefore encompass all
sequences with some homology to SEQ ID NO:1. Id. The Examiner finds
that such functional variants could have any number of amino acid additions,
deletions, and substitutions relative to SEQ ID NO:1. Id.
The Examiner points to Appellants’ Specification, which discloses
that the TMT1 protein has 12 transmembrane domains, with a large
hydrophilic loop connecting the sixth and seventh domain together. Non-
Final Act. 3 (citing Spec. 5). However, the Examiner finds, Wormit teaches
that these same transmembrane domains are part of several other proteins
that transport sugars in Arabidopsis, indicating that these structures are
common to sugar transporters in plants and are not necessarily the only
transporters that transport sugar from the cell cytoplasm into a cell vacuole.
Id.
Therefore, the Examiner finds, the transmembrane domains are
necessary, but not sufficient, to describe the claimed proteins, and other than
Appeal 2018-008039
Application 13/637,908

5
noting the large size of the hydrophilic loop, no other features or key
domains or residues of the loop required for the claimed vacuolar transport
function are described in the prior art or the specification. Id. at 3–4 (citing
Wormit Fig. 1). The Examiner also finds that a person of ordinary skill in
the art would have found it reasonable to assume, given both the
construction of the claims and the disclosures of Appellants’ Specification,
that transport of sugar from the cell cytoplasm into a cell vacuole is a feature
that is required to produce the claimed increased yield or growth effect. Id.
at 4.
The Examiner finds that the structural features that distinguish a
functional variant of the Arabidopsis TMT1 protein with some amino acid
sequence identity to SEQ ID NO:1, with the ability to increase seed yield
and transport sugar from the cell cytoplasm into a cell vacuole when
expressed in plants, from other proteins with some amino acid sequence
identity to SEQ ID NO:1 are not disclosed by the Specification. Non-Final
Act. 4.
The Examiner notes that the only species provided in the Specification
is SEQ ID NO:1, the sequence encoding the TMT1 protein from
Arabidopsis. Non-Final Act. 4. The Examiner finds that Appellants’
Specification discloses the existence of related TMT2 and TMT3 proteins in
Arabidopsis, but does not provide the sequences for these proteins. Id.
(citing Spec. 3, 5). The Examiner notes that the sequences of TMT2 and
TMT3 are taught by Wormit, and share 64.1% and 55% identity with TMT1,
respectively. Id. (citing Wormit 3488). The Examiner concludes that, given
the size of the claimed genus, and the limited sequence information provided
Appeal 2018-008039
Application 13/637,908

6
by the Specification, in light of the prior art, fails to adequately describe the
claimed genus. Id.
Appellants argue that the claims do not require a functional variant of
the Arabidopsis TMT1, as described by the Examiner. App. Br. 9 (citing
Non-Final Act. 3). Rather, Appellants contend, what is required of the
claims is overexpression of TMT protein, or a functional variant thereof. Id.
Appellants argue that the functional variant is claimed so as to include
various parameters that do in fact provide a description that would allow a
person of ordinary skill in the art to recognize what was claimed. Id.
Appellants assert that the claims require that the functional variant exhibits a
sequence homology with an amino acid sequence of A. thaliana TMT1
protein, as provided by SEQ ID NO:1, which results in transporting sugar
from cell cytoplasm into a cell vacuole, and having enhanced seed yield or
growth promotion of monocotyledonous or dicotyledonous plants compared
to a wild-type plant of the same species. Id. Appellants contend that the
structural feature of having sequence homology with an amino acid
sequence of A. thaliana TMT1 protein according to SEQ ID NO:1 provides
sufficient structural description for one of skill in the art to understand what
was claimed. Id.
Appellants argue that, more importantly, their Specification, and the
knowledge of one of skill in the art, provide the necessary guidance and
knowledge to understand what was claimed. App. Br. 9. Appellants point to
their Specification as disclosing methods of enhancing seed yield or
promoting growth of monocotyledonous or dicotyledonous plants, and a
transgenic plant having the property of an enhanced seed yield or increased
growth, when compared to a wild-type conspecific, through overexpression
Appeal 2018-008039
Application 13/637,908

7
of the TMT1 protein, or functional variant thereof, such as a homolog or
analog of the TMT protein. Id. at 9–10. According to Appellants, their
Specification discloses that a homologue:
[D]enotes a transport protein which exhibits a high sequence
identity with the TMT (tonoplast monosaccharide transporter)
protein TMT1 of Arabidopsis thaliana. Preferably, a homologue
has a sequence identity of 50%, 60%, 70%, 75%, 80%, 85%,
90%, 95%, 96%, 97%, 98%, 99% or 100% with an amino acid
sequence of Arabidopsis thaliana TMT (tonoplast
monosaccharide transporter) protein TMT 1.

Id. at 10 (citing Spec. 6). Appellants also note that their Specification
discloses that an analogue:
[D]enotes a sugar transport protein which is localized in the
vacuole membrane and performs the function of transporting
sugar from the cytoplasm into the vacuole without there
necessarily having to be a sequence homology to the TMT
(tonoplast monosaccharide transporter) protein. An analogue,
therefore, has the same function as the TMT l protein but can’t
[sic] be structurally different. Unlike a homologue, a genetic
relationship is not a prerequisite.

Id.
Appellants next point to the First Declaration of Dr. Ekkehard
Neuhaus, filed February 22, 2016 (the “First Neuhaus Declaration”)2 as
stating that the believed expression of homologous TMT1 proteins found in
Arabidopsis species and other plant species will induce comparable
phenotypes, and thus result in significant seed yield and growth promotion.
App. Br. 10. According to Appellants, Dr. Neuhaus attests that TMT1 and
TMT2 were known to be transporters of sugar within a plant. Id. at 11.

2 Dr. Neuhaus is one of the named inventors on the instant Application.
Appeal 2018-008039
Application 13/637,908

8
Appellants note that they have also identified key transporters
responsible for sucrose accumulation in sugar beet taproot, BvTST2.l. Id.
(citing B. Jung et al., Identification of the Transporter Responsible for
Sucrose Accumulation in Sugar Beet Taproot, 1 NATURE PLANTS 1–6
(January 11, 2015) (“Jung”)). Appellants contend that Jung teaches that
BvTST2.l exhibits a high amino acid sequence similarity to members of the
Arabidopsis TMT family, and is able to increase sugar yields from sugar
beet and other sugar-storing plants. App. Br. 11. Appellants further note
that Jung teaches that BvTST2.1 shares about 68% identical amino acid
sequence with AtTST2. Id. (citing Jung 2). Appellants contend that they
further identified BvTST1, and demonstrated that BvTST1 was able to
transport glucose. Id. (citing First Neuhaus Decl. ¶ 7). Appellants note that
Dr. Neuhaus further attests that the art recognized that each of these sugar
transporters have various degrees of homology with TMT: (1) TMT1 is
64.1% identical to TMT2, and 77.0% similar; (2) TMT1 to is 62.5%
identical to BvTM(S)T1, and 76.0% similar; and (3) TMT1 to
BvTM(S)T2.1 is: 59.4% identical, and 74.3% similar. Id. (citing First
Neuhaus Decl. ¶¶ 8–10). Appellants consequently assert that they have
provided evidence that homologues of TST1 sharing a rather low sequence
identity are able to transport glucose as claimed in the present set of claims.
Id.
We do not find Appellants arguments persuasive. Claim 1 requires:
[O]verexpression of TMT […] protein, or a functional variant
thereof, the functional variant exhibiting a sequence homology
with an amino acid sequence of Arabidopsis thaliana TMT […]
protein TMT1 according to SEQ ID NO: 1 which results in
transporting sugar from cell cytoplasm into a cell vacuole and
having enhanced seed yield or growth promotion of
Appeal 2018-008039
Application 13/637,908

9
monocotyledonous or dicotyledonous plants compared to a wild-
type plant of the same species.
Claim 1 thus imposes two limitations upon the claimed “functional
variant” of TMT1: (1) a structural requirement that the variant possess a
sequence homology with an (unspecified) amino acid sequence of
Arabidopsis TMT1; and (2) a functional requirement that the variant be
capable of: “transporting sugar from cell cytoplasm into a cell vacuole and
having enhanced seed yield or growth promotion” in plants.
We agree with the Examiner that the structural requirement recited in
claim 1 encompasses a vast genus of possible polypeptides: it merely
requires that a given subject polypeptide share an undefined sequence
homology with an amino acid sequence, similarly undefined, of the
Arabidopsis TMT1 protein (as defined by SEQUENCE ID NO:1).
Appellants’ Specification defines the claim term “homologue” thus:
A “homologue” within the scope of the invention therefore
denotes a transport protein which exhibits a high sequence
identity with the TMT […] protein TMT1 of Arabidopsis
thaliana. Preferably, a homologue has a sequence identity of
50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%,
99% or 100% with an amino acid sequence of Arabidopsis
thaliana TMT […] protein TMT1.

Spec. 6. However, this definition pertains to a protein that is homologous to
the Arabidopsis TMT1 protein overall, and does not refer to a sequence
homology to “an amino acid sequence of Arabidopsis […] TMT1,” as
recited in claim 1. Such a “sequence” could be as small as two or three
amino acids from the primary structure of the TMT1 protein and therefore a
variant need only exhibit homology to a small piece of the overall protein to
meet the “sequence homology” limitation. In other words, the claim
Appeal 2018-008039
Application 13/637,908

10
requires that a sequence have a homology only to any given sequence of
amino acids in the TMT1 protein, and not a homology to the complete
protein (i.e, the full sequence defined by SEQ ID NO:1). When one
considers that that TMT1 protein has 12 transmembrane domains, and a
relatively large, centrally localized hydrophilic loop connecting domains 6
and 7 to one another, and that, in all, TMT1 comprises 734 amino acid
residues (see Wormit 3477), the number of possible polypeptide sequences
that could meet the structural limitation of claim 1 is vast indeed.
Claim 1 also requires that the claimed functional variant of TMT1 be
capable of: “result[ing] in transporting sugar from cell cytoplasm into a cell
vacuole and having enhanced seed yield or growth promotion” in plants
when compared to the wild-type plant. Appellants point to other proteins
that have a degree of homology to TMT1 (i.e., TMT2, BvTST2.l,
BvTM(S)T1) which share a degree of homology with TMT1 and are capable
of transporting sugars across vacuolar membranes in plant cells. See First
Neuhaus Decl. ¶¶ 7–11; see also Jung 2. However, the degree of homology
of these transport proteins (64%, 63% and 60%, respectively) is to the
overall TMT1 protein amino acid sequence, and not to an undefined “amino
acid sequence” of the SEQUENCE ID NO:1 of the TMT1 protein. We
further conclude that, even if the structural requirement did require a
“sequence homology” to SEQ ID NO:1 as a whole, the Specification merely
states that a “homologue” is “preferably” 50% or more identical to the
TMT1 protein, and so could embrace “homologies” of even considerably
less correspondence to SEQ ID NO:1.
Moreover, Appellants provide no structure-function relationship to
identify how a given amino acid sequence affects the structure of a target
Appeal 2018-008039
Application 13/637,908

11
protein so as to predict whether that protein will function in the manner
claimed. Given the enormous scope of the functional variant genus
encompassed by the structural limitation of claim 1, determining the metes
and bounds of the members of that genus that satisfy the functional
requirement of the claim would be extremely burdensome. More
importantly, because there is no way to predict whether a proposed
functional variant polypeptide that meets the structural requirement of claim
1 would also meet the functional requirement, a person of ordinary skill in
the art could have no understanding that Appellants were in actual
possession of the full scope of the claimed invention at the time of filing.
See Ariad Pharms., Inc. v. Eli Lilly and Co., 598 F.3d 1336, 1351 (Fed. Cir.
March 2010) (holding that “the test for sufficiency is whether the disclosure
of the application relied upon reasonably conveys to those skilled in the art
that the inventor had possession of the claimed subject matter as of the filing
date.”)
We consequently affirm the Examiner’s rejection of claims 1–3, 5, 6,
11, 12, 15–17, and 19–21 upon this ground.

B. Rejection of the claims as lacking enablement under 35 U.S.C. § 112,
first paragraph

Issue
Appellants argue that the Examiner erred because their Application
sufficiently describes the subject matter such that one skilled in the art
would reasonably conclude that the claims are enabled for the full breadth of
the protection desired or would not require undue experimentation to make
and use the claimed invention. App. Br. 13.
Appeal 2018-008039
Application 13/637,908

12
Analysis
Citing several of the factors set forth by our reviewing court in In re
Wands, Appellants note that the level of skill in the art is high. App. Br. 13
(citing 858, F.2d 731, 737 (Fed Cir. 1988)). Appellants argue that their
Specification would teach a person of ordinary skill in the art the necessary
steps to provide the claimed transgenic plant. Id. at 13–14.
Appellants argue that the Examiner incorrectly relies on H.H. Guo et
al., Protein Tolerance to Random Amino Acid Change, 101(25) PROC. NATL.
ACAD. SCI. USA 9205–10 (2004) (“Guo”) as teaching that, although proteins
are fairly tolerant of mutations resulting in single amino acid changes,
increasing the number of substitutions additively increases the probability
that the protein will be inactivated. App. Br. 14 (citing Guo 9209).
Appellants contend that the Examiner therefore concludes that making and
analyzing proteins with numerous amino acid substitutions that also have
seed-yield-increasing activity would require undue trial and error
experimentation. Id. (see Non-Final Act. 7).
In response, Appellants argue that Guo teaches the fact that changes in
amino acids could change the functionality, but the reference does not
address overexpression of a functional variant of the Arabidopsis TMT1
protein with some amino acid sequence identity to SEQ ID NO:1. App. Br.
14. More importantly, Appellants argue, the art at recognizes variants in
sugar transport proteins having the same functionality as required by
Appellants’ claims. Id. (citing arguments presented supra re the BvTST2.l
and BvTST1 sugar beet taproot proteins).
Appellants argue further that the fact that one could change any single
amino acid of SEQ ID NO:1 misses the point of their claims on appeal.
Appeal 2018-008039
Application 13/637,908

13
App. Br. 14. According to Appellants, the functional variant, as claimed,
must result in transporting sugar from cell cytoplasm into a cell vacuole and
having enhanced seed yield or growth promotion of plants when compared
to a wild-type conspecific. Id. In this manner, argue Appellants, a skilled
artisan would not have an undue burden in testing an amino acid sequence
with changes in the sequence to see if the variant is functional. Id. At most,
Appellants contend, one of skill in the art would have to determine
functionality of the particular functional variant. Id.
We are not persuaded by Appellants’ arguments. As we have
explained supra, Appellants’ claims encompass a vast genus of
polypeptides, without providing any structural-functional correlation that
would permit a skilled artisan to reliable predict whether a given member of
that genus, as claimed, would have the functionality required by the claim.
Absent any such disclosure, a person of ordinary skill in the art would not be
able to extrapolate from the sequence provided by SEQUENCE ID NO:1
whether a given polypeptide falling within the structural scope of the claims
would meet the functional requirement as well. Consequently, practicing the
full scope of the claim would require undue experimentation by a person of
ordinary skill in the art.
We therefore affirm the Examiner’s rejection of the claims upon this
ground.

C. Rejection of the claims as being obvious under 35 U.S.C. § 103(a)
Issue
Appellants argue that the Examiner erred because the combined cited
prior art fails to teach or suggest all of the limitations of claim1, and because
Appeal 2018-008039
Application 13/637,908

14
there would have been no motivation, or expectation of success, for a skilled
artisan to combine the references. App. Br. 15.

Analysis
The Examiner finds that Wormit3 teaches that overexpression of the
Arabidopsis thaliana TMT1:GFP fusion protein, which contains a sequence
with 100% identity with SEQ ID NO:1, under the control of the 35S
constitutive promoter, in Nicotiana tabacum plant cells. Non-Final Act. 9
(citing Wormit 3477, 3487). The Examiner finds that Wormit also teaches
that the TMT1 gene is strongly induced by cold conditions and suggests that
expression of the TMT1 protein in plants could be a part of the cold stress
response in plants. Id. (citing Wormit 3479, 3485, 3486 Fig. 5). The
Examiner further finds that Wormit also teaches a method of transforming
plant cells using Agrobacterium-mediated transformation and regenerating
transgenic plants from the cells. Id. (citing Wormit 3487–3488). The
Finally, Examiner finds that Wormit teaches the TMT1 polypeptide
sequence as GenBank Accession Z50752. Id. (see Wormit 3488).
Appellants argue that Wormit simply teaches transiently-expressed
TMT proteins in the form of TMT-Green Fluorescent Protein (GFP) in
isolated tobacco plant protoplasts. App. Br. 16. Appellants contend that this
is simply a TMT1-GFP reporter protein, which is a stable fusion between the
carrier domain (TMT1) and a 30kDa large green-fluorescing protein (GFP).

3 We note that Dr. Neuhaus, Oliver Trentmann, and Alexandra Wormit,
inventors of record in the instant application, are also co-authors of the
Wormit reference.
Appeal 2018-008039
Application 13/637,908

15
Id. Such a construct, Appellants contend, is scientifically different than
Appellants’. Id.
Appellants also point to the Second Declaration of Dr. Neuhaus, filed
April 10, 2017, (the “Second Neuhaus Declaration”). App. Br. 16.
According to Appellants, Dr. Neuhaus avers that it is doubtful that an
extremely hydrophobic membrane transporter (TMT1) exhibits its transport
capacity, having back-packed with such a large hydrophilic GFP domain. Id
(citing Second Neuhaus Decl. ¶ 5). Therefore, Appellants argue, the use of
the construct TMT1-GFP protein to study altered properties in an intact plant
would not be used by a skilled artisan. Id.
Appellants contend that Dr. Neuhaus further attests that, to his
knowledge, no laboratory has shown, or even investigated, that such
transiently TMT1-expressing tobacco protoplasts show any changes in
intracellular sugar compartmentation. App. Br. 16. Appellants contend that
altered intracellular sugar compartmentation is believed to be key for the
observed increase of seed yield. Id. Appellants assert that the data reported
in Wormit was generated on the basis of transiently transformed, single
tobacco protoplast only. Id. Appellants point to Dr. Neuhaus’ statement that
a person skilled in the art would be unable to generate intact adult plants
from the cell preparations taught by Wormit. Id.
Appellants further argue that that the Examiner relies on the
motivation being found in Wormit’s teaching the TMT1 gene is strongly
induced by cold conditions and, therefore, it would be obvious to regenerate
tobacco plants from tobacco cells transformed with the TMT1 gene under
the use of a promoter to determine if the plants show an increased resistance
to cold stress. App. Br. 16–17. Appellants’ position is that the Examiner’s
Appeal 2018-008039
Application 13/637,908

16
position is conclusory and not supported by the teachings and suggestions of
any cited prior art reference. Id. at 17. Appellants argue further that the
Examiner’s position is in contrast to the testimony of Dr. Neuhaus in his
First and Second Declarations. Id.
According to Appellants, Dr. Neuhaus has shown that TMT1 (and
TMT2) gene expression can be induced by cold temperature and that, while
one could speculate that TMT1 is part of the plant cold response program,
the plant cold response program is complex. App. Br. 17. Appellants
contend that, according to Dr. Neuhaus, one would have predicted that
overexpression of TMT1 would lead to even higher leaf sugar contents after
onset of cold temperatures, due to the documented sugar transport activity
into leaf vacuoles. Id. Given that sugars stored in the leaf cannot be
transported into seeds, argue Appellants, a person of skill in the art would
have predicted that a TMT1 overexpressing plant would exhibit less seed
yield when compared to that observed in a corresponding wild type plant.
Id.
We are not persuaded by Appellants’ arguments. Wormit teaches: “a
monosaccharide carrier, named TMT, which has three isoforms [including
TMT1] in Arabidopsis.” Wormit 3484 (citations mitted). Wormit teaches
that: “TMT proteins from Arabidopsis reside in the tonoplast, as suggested
from vacuolar proteome data, and that these transporters play a central role
in vacuolar hexose transport, mainly under stress conditions.” Id. at 3485
(internal citations omitted).
More specifically, Wormit teaches that:
It is well known that in Arabidopsis leaves, osmotic or cold stress
leads to the degradation of starch and consequently to increased
glucose levels. Interestingly, both of these environmental stimuli
Appeal 2018-008039
Application 13/637,908

17
induced the accumulation of tmt1 mRNA, and concomitantly, a
strong stimulation of glucose uptake into isolated mesophyll
vacuoles was observed in wild-type plants. This correlation leads
to the conclusion that TMT1 transport is regulated at the
transcriptional level. However, we cannot exclude the possibility
that posttranslational modification of TMT1 or the two
additional isoforms occurs and contributes to an upregulation of
vacuolar glucose import upon cold induction.

Wormit 3485–3486 (internal citations omitted). Wormit also teaches that:
“The tmt1 knockout mutants exhibit ~60% reduced glucose transport activity
compared with wild-type plants. This reduction is not increased further in
the triple deletion mutant.” Id. at 3486 (internal citation omitted).
In summary, Wormit thus teaches that TMT1 is a tonoplast
monosaccharide transporter (see also Wormit Abstr.) responsible for
transporting monosaccharides into cellular vacuoles, and that knockout tmt1
mutants result in greatly decreased storage of monosaccharides, whereas
cold results in an upregulation of TMT1 expression and increased storage of
monosaccharides in Arabidopsis tonoplasts. Finally, Wormit teaches that:
To perform a careful biochemical analysis of TMT1, TMT2, and
TMT3, either a non-yeast-based expression system has to be
established that allows the synthesis of these intracellular
monosaccharide transporters or, alternatively, overexpression
and purification of the TMT proteins in planta and subsequent
incorporation in liposomes have to be envisaged.

Wormit 3486. Although the context of the overexpression of TMT1
experiments proposed in the quoted passage differs from that of the instant
application, it strongly suggests that inducing overexpression of TMT1
would require only routine experimentation by a person of ordinary skill in
the art. We agree with the Examiner that a skilled artisan, comprehending
Appeal 2018-008039
Application 13/637,908

18
the teachings of Wormit, would have reasonably expected that
overexpression of TMT1 could be successfully performed, and that it could
reasonably be expected to succeed in “transporting sugar from cell
cytoplasm into a cell vacuole” as recited in claim 1. We also note that
GenBank teaches SEQUENCE ID NO.1, and that Wormit teaches the
GenBank/EMBL accession numbers and Arabidopsis Genome Initiative
locus identifiers for the genes. Id.
The Second Neuhaus Declaration states that a person of ordinary skill
would have had no reasonable expectation that overexpression of TMT1 in a
plant would result in increased seed yield or enhanced growth. See Second
Neuhaus Decl. ¶¶ 5–7. However, and as we have explained, we conclude
that a person of ordinary skill in the art would have found in obvious to
conduct the claimed overexpression study and would have had a reasonable
expectation of success in finding that overexpression of TMT1 would have
resulted in increased transport of monosaccharides from the cell cytoplasm
to cell vacuoles. The fact that this process also necessarily results in
increased seed yield and enhanced cell growth is an inherent property of the
overexpression of the TMT1 protein. As our reviewing court has held, the
discovery of such an unknown property of an obvious invention is not
sufficient to overcome the Examiner’s prima facie conclusion of
obviousness. See In re Baxter Travenol Labs., 952 F.2d 388, 392 (Fed. Cir.
1991) (holding that “[m]ere recognition of latent properties in the prior art
does not render nonobvious an otherwise known invention”).
We consequently affirm the Examiner’s rejection of the claims upon
this ground.

Appeal 2018-008039
Application 13/637,908

19
DECISION
The Examiner’s rejection of claims 1–3, 5, 6, 11, 12, 15–17, and 19–
21 under U.S.C. § 112, first paragraph, for lack of written descriptive
support is affirmed.
The Examiner’s rejection of claims 1–3, 5, 6, 11, 12, 15–17, and 19–
21 under U.S.C. § 112, first paragraph, for lack of enablement is affirmed.
The Examiner’s rejection of claims 1–3, 5, 6, 11, 12, 15–17, and 19–
21 under U.S.C. § 103(a) is affirmed.
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). See 37
C.F.R. § 41.50(f).
AFFIRMED