Ex Parte Dassler et al

Patent Trial and Appeal Board

Mar 1, 2016

11859350 (P.T.A.B. Mar. 1, 2016)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
111859,350 09/21/2007
22045 7590 03/03/2016
BROOKS KUSHMAN P,C
1000 TOWN CENTER
TWENTY-SECOND FLOOR
SOUTHFIELD, MI 48075
FIRST NAMED INVENTOR
Tobias Dassler
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.
WAS0905PUS 4494
EXAMINER
VOGEL, NANCY TREPTOW
ART UNIT PAPER NUMBER
1636
NOTIFICATION DATE DELIVERY MODE
03/03/2016 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):
docketing@brookskushman.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte TOBIAS DASSLER,
ANNELIESE REUTTER-MAIER, and GUENTER WICH
Appeal2013-005593
Application 11/859,350
Technology Center 1600
Before DONALD E. ADAMS, MELANIE L. McCOLLUM, and
JACQUELINE T. HARLOW, Administrative Patent Judges.
ADAMS, Administrative Patent Judge.
DECISION ON APPEAL 1
This appeal2 under 35 U.S.C. § 134(a) involves claims 3---6, 8-11, 13-
20, 25, and 26 (Ans. 3; App. Br. 2). 3 Examiner entered rejections under
35 U.S.C. § 103(a). We have jurisdiction under 35 U.S.C. § 6(b).
We AFFIRM.
1 Appellants identify the Real Party in Interest as "Wacker Chemie AG"
(App. Br. 1 ).
2 This Appeal is related to Appeal 2013-004508, Application 11/859,616.
3 Claims 21-23 stand "withdrawn from consideration" (App. Br. 2).
Appeal2013-005593
Application 11/859,350
STATEMENT OF THE CASE
Appellants disclose "a process for the fermentative production of
heterologous proteins by using an Escherichia coli strain having a
lipoprotein mutation" (Spec. 1 :7-9). Claim 25 is representative and
reproduced in the Claims Appendix of Appellants' Brief.
Claims 5, 6, 8, 19, 20, and 25 stand rejected under 35 U.S.C. § 103(a)
as unpatentable over the combination of Inouye4 and Better. 5
Claim 9 stands rejected under 35 U.S.C. § 103(a) as unpatentable over
the combination of Inouye, Better, and Carter. 6
Claims 10 and 11 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Inouye, Better, and either Kowalski7
or Schmid. 8
Claim 4 stands rejected under 35 U.S.C. § 103(a) as unpatentable over
the combination of Inouye, Better, and Giam. 9
Claim 3 stands rejected under 35 U.S.C. § 103(a) as unpatentable over
the combination of Inouye, Better, and Inouye 2. 10
4 Inouye et al., US 4,643,969, issued Feb. 17, 1987.
5 Marc Better et al., Potent anti-CD5 ricin A chain immunoconjugates from
bacterially produced Fab' and F(ab ') 2, 90 PROC. NATL. AcAD. SCI. USA
457--461 (1993).
6 Paul J. Carter, WO 93/06217, published Apr. 1, 1993.
7 Kowalski et al., US 5,521,084, issued May 28, 1996.
8 Schmid et al., US 5,204,254, issued Apr. 20, 1993.
9 Chou-Zen Giam et al., Prolipoprotein modification and processing in
Escherichia coli A unique secondary structure in prolipoprotein signal
sequence for the recognition by glyceryl trans/erase, 141 EUR. J. BIOCHEM.
331-337 (1984).
10 Sumiko Inouye et al., Amino Acid Replacement in a Mutant Lipoprotein of
the Escherichia coli Outer Membrane, 132 J. BACTERIOLOGY 308-313
(1977).
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Appeal2013-005593
Application 11/859,350
Claims 13-15 and 26 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Inouye, Better, and Simmons. 11
Claim 16 stands rejected under 35 U.S.C. § 103(a) as unpatentable
over the combination of Inouye, Better, and Kasche. 12
Claims 17 and 18 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Inouye, Better, Simmons, and
Suzuki. 13
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness?
FACTUAL FINDINGS (FF)
We adopt the Examiner's findings concerning the scope and content
of the prior art (Ans. 4--20) and repeat the following for emphasis.
FF 1. Inouye discloses the use of "E. coli strains as hosts for cloning and
for subsequent production of [a desired eukaryotic] protein[,]" wherein
"[t]he host cell strains[] have a 'deletion mutant' in the lpp gene, so that the
host cells cannot produce the lipoprotein" (Inouye 15:10-16; Ans. 5).
FF 2. Examiner finds that Inouye's E. coli strain ha[s] a deletion in the lpp
gene, which results in the lpp gene product not being expressed (Ans. 5; id.
11 Laura C. Simmons et al., Expression of full-length immunoglobulins in
Escherichia coli: rapid and efficient production of aglycosylated antibodies,
263 J. IMMUNOL. METHODS 133-147 (2002).
12 Volker Kasche et al., Ca2+ Is a Cofactor Required for Membrane
Transport and Maturation and Is a Yield-Determining Factor in High Cell
Density Penicillin Amidase Production, 21 BIOTECHNOL. PROG. 432--438
(2005).
13 Hideho Suzuki et al., Murein-Lipoprotein of Escherichia coli: A Protein
Involved in the Stabilization of Bacterial Cell Envelope, 167 MOLEC. GEN.
1-9 (1978).
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Appeal2013-005593
Application 11/859,350
at 17 ("the resultant strain would result in cells having no lpp protein product
present in the cells")).
FF 3. Inouye discloses that "[ t ]he use of a deletion mutant strain as the
transformant is thought to stimulate the production of a large amount of the
foreign protein, since the entire capacity of the host cells to produce the
lipoprotein is thereby channeled towards production of the foreign protein"
(Inouye 15:16-26; Ans. 5).
FF 4. Inouye discloses that "secretion of the foreign protein across the
cytoplasmic membrane is facilitated in !pp-defective host cells, since the
secretion sites in the membrane which are intended to be used for lipoprotein
secretion are instead available for secretion of the foreign protein" (Inouye
15:21-26; Ans. 5).
FF 5. Examiner finds that Inouye fails to suggest the fermentation of an E.
coli strain in a fermenter with a volume of more than 5 liters of fermentation
medium or the production of an eukaryotic protein that comprises more than
70 amino acids and relies on Better to make up for the deficiencies in Inouye
by suggesting "a method for producing anti-human CDS antibody fragments,
including F(ab')2 []using an E.coli host cell in a 12 liter fermenter with 10
liters of minimal medium" (Ans. 6).
FF 6. Examiner finds that the combination of Inouye and Better fails to
suggest "an extracellular antibody fragment yield of more than 1 g/L" and
relies on Carter to make up for this deficiency in the combination of Inouye
and Better (Ans. 7).
FF 7. Examiner finds that the combination of Inouye and Better fails to
disclose the "ompA, phoA, or cgtase, signal sequences" and relies on
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Application 11/859,350
Kowalski to suggest "ompA or phoA" signal sequence and Schmid to
suggest the "cgtase" signal sequence (Ans. 7-8).
FF 8. Examiner finds that the combination of Inouye and Better fails to
suggest the use of an lpp deletion mutant wherein the glycine at position 12
of lpp is replaced with aspartic acid and relies on Giam to make up for the
foregoing deficiency in the combination of Inouye and Better (Ans. 8-9).
FF 9. Examiner finds that the combination of Inouye and Better fails to
suggest the use of an lpp deletion mutation wherein the arginine at position
77 of lpp is replaced with cysteine and relies on Inouye 2 to make up for the
foregoing deficiency in the combination of Inouye and Better (Ans. 9-10).
FF 10. Examiner finds that the combination of Inouye and Better fails to
suggest a Ca2+ ion concentration in the range of 10 mg/l to 5000 mg/l and
relies on Simmons to make up for this deficiency in the combination of
Inouye and Better (Ans. 10).
FF 11. Examiner finds that the combination of Inouye and Better fails to
suggest a Ca2+ ion concentration in the range of 40 mg/l to 5000 mg/l and
relies on Kasche to make up for this deficiency in the combination of Inouye
and Better (Ans. 11).
FF 12. Examiner finds that the combination of Inouye, Better, and Simmons
fails to suggest a Mg2+ ion concentration above 48 mg/L and relies on
Suzuki to make up for this deficiency in the combination of Inouye, Better,
and Simmons (Ans. 12-13).
ANALYSIS
Based on the combination of Inouye and Better, Examiner concludes
that, at the time Appellants' invention was made, it would have been prima
facie obvious "to have used at least 5 liters of fermentation media, as taught
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Application 11/859,350
by Better [], in the method of Inouye in order to obtain large quantities of
product" (Ans. 6). In addition, Examiner finds that because Inouye
"discloses that the method may be used to produce any eukaryotic protein,
the production of a eukaryotic protein having more than 70 amino acids, as
disclosed by Better [] would have been obvious to one of ordinary skill in
the art" (id.). We find no error in Examiner's conclusion of obviousness.
The method of Appellants' claim 25 comprises the removal of an
eukaryotic protein from the fermentation medium, wherein the eukaryotic
protein comprises more than 70 amino acids (see Appellants' claim 25).
Appellants recognize that Inouye discloses a method wherein an eukaryotic
protein is produced and removed from fermentation medium, wherein the
protein includes "the amino acid sequence of [a] desired eukaryotic protein"
(App. Br. 10 (emphasis removed)). Further, as Examiner explains, the
combination of Inouye and Better suggests "the production of a[ n]
eukaryotic protein having more than 70 amino acids" (Ans. 6). Therefore,
absent persuasive argument or evidence to the contrary, we are not
persuaded by Appellants' contentions regarding the stability of full length
protein products, which fails to establish that the combination of Inouye and
Better fails to suggest the production of protein having more than 70 amino
acids as required by Appellants' claimed invention (App. Br. 10; Reply Br.
1--4; cf Ans. 13-14).
The combination of Inouye and Better suggests the production of an
eukaryotic protein in at least 5 liters of fermentation media (see Ans. 6; FF
1-5). Therefore, we are not persuaded by Appellants' unsupported
contention that a person of ordinary skill in this art would not have found it
prima facie obvious to produce a protein in 5 liters of fermentation media as
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Application 11/859,350
suggested by the combination of Inouye and Better (App. Br. 10-11; cf Ans.
6; FF 1-5). We recognize, but are not persuaded by, Appellants' contentions
regarding protein folding, protein yield, etc., which Appellants' fail to
establish are: (1) requirements of Appellants' claimed invention and (2) not
overcome by the combination of prior art relied upon by Examiner (see
Reply Br. 4--7).
For the reasons set forth by Examiner (Ans. 14--15), we are not
persuaded by Appellants' contention that "Examiner's characterization of
the prior art [] and [conclusion] that one in the field would combine Inouye
[] and Better[] is misguided" (App. Br. 11; Reply Br. 7-8). For the same
reasons, we are not persuaded by Appellants' unsupported contention that
"[ t ]he methods employed by the Appellants, Inouye et al. and Better et al.
are not known for their predictable outcomes" (App. Br. 12).
As Examiner explains, "Inouye teaches a deletion mutant of the lpp
gene [], and therefore, the resultant strain would result in cells having no lpp
protein product present in the cell" (Ans. 17; FF 2). Therefore, we are not
persuaded by Appellants' contentions regarding the claimed "amount of lpp
protein [that may be] detectable in cells" (App. Br. 12; Reply Br. 8-9).
We recognize, but are not persuaded by, Appellants' contentions
regarding the failure of the combination of Inouye and Better to suggest a
"fermentation medium [that] includ[ es] Ca [2+ J ions in a concentration [of]
from 10 mg/l to 5 000 mg/l," which is not required by Appellants' claim 2 5
(see App. Br. 12; cf Ans. 14--15; Appellants' claim 25).
Having found no deficiency in the combination of Inouye and Better,
we are not persuaded by Appellants' contention that: (1) Carter, (2) either
Kowalski or Schmid, (3) Giam, (4) Inouye 2, (5) Simmons, (6) Kasche, or
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Application 11/859,350
(7) the combination of Simmons and Suzuki fail to make up for Appellants'
alleged deficiency in the combination of Inouye and Better (see App. Br.
12-14).
CONCLUSION OF LAW
The preponderance of evidence relied upon by Examiner supports a
conclusion of obviousness. We affirm the rejections of record.
TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).
AFFIRMED
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