Ex Parte Loessner

Board of Patent Appeals and Interferences

May 22, 2008

10406897 (B.P.A.I. May. 22, 2008)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
____________

Ex parte MARTIN LOESSNER
____________

Appeal 2008-2122
Application 10/406,897
Technology Center 1600
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Decided: May 22, 2008
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Before TONI R. SCHEINER, DEMETRA J. MILLS, and DONALD E.
ADAMS, Administrative Patent Judges.

ADAMS, Administrative Patent Judge.

DECISION ON APPEAL

This appeal under 35 U.S.C. § 134 involves claims 1-7, 14, 15, 21, 25-
27, 31, and 124-129, the only claims pending in this application. We have
jurisdiction under 35 U.S.C. § 6(b).

Appeal 2008-2122
Application 10/406,897

INTRODUCTION
The claims are directed to a method for the binding of target cells,
Listeria Serovar 1/2, 3, 4, 5, 6, or 7 or any mixture thereof, to a solid phase.
Claims 1 and 5 are illustrative:
1. A method for the binding of target cells to a solid phase, said target
cells being cells of Listeria Serovar 1/2, 3, 4, 5, 6 or 7 or any mixture
thereof, wherein the method comprises the following steps:
(a) providing polypeptide fragments, derived from Ply 500 protein and
Ply 118 protein, bound to a solid phase, said fragments having the ability to
bind to a cell wall of said target cells, said polypeptide fragments not having
any hydrolytic activity, and
(b) contacting said protein fragments bound to said solid phase with a
sample which comprises the target cells.

5. The method according to claim [1, wherein said bound fragments
are bound by covalent binding, wherein said solid phase consists of beads,
preferably latex beads], wherein the latex beads have an average surface of
between 10 and 1000 µm2/bead, preferably between 10 and 100 µm2/bead,
especially preferred between 20 and 50 µm2/bead and an average diameter of
1 to 40 µm, preferably 1 to 10 µm, especially preferred 2 to 5 µm.

The Examiner relies on the following prior art references to show
unpatentability:
Dorman et al. US 4,210,723 Jul. 1, 1980
Scherer et al. WO 00/11472 Mar. 2, 2000
(Translation PTO 05-1444)
Miller US 2002/0127547 A1 Sep. 12, 2002

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The rejections as presented by the Examiner are as follows:
1. Claims 1-4, 31, and 124 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Miller and Scherer.
2. Claims 5-7, 14, 15, 21, 25-27, and 125-129 stand rejected under 35
U.S.C. § 103(a) as unpatentable over the combination of Miller, Scherer, and
Dorman.
We affirm.

DISCUSSION
Claim Interpretaton:
Claim 1 is drawn to a method for the binding target cells to a solid
phase. Claim 1 defines the target cells as any one of Listeria Serovar 1/2, 3,
4, 5, 6 and 7; or any mixture thereof. The method comprises two steps:
(a) providing polypeptide fragments, derived from Ply 500 protein and
Ply 118 protein, bound to a solid phase; and
(b) contacting the protein fragments bound to the solid phase with a
sample which comprises the target cells.
Claim 1 further requires that the polypeptide fragments (1) have the
ability to bind to a cell wall of the target cells, and (2) do not have any
hydrolytic activity.
Claim 5 ultimately depends from and further limits claim 1 to require:
(a) the fragments are bound by covalent binding,
(b) the solid phase consists of beads, preferably latex beads having an
average surface of between 10 and 1000 µm2/bead and an average
diameter of 1 to 40 µm.

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Claim Grouping:
The claims have not been argued separately and therefore stand or fall
together for each ground of rejection. 37 C.F.R. § 41.37(c)(1)(vii).
Therefore, we limit our discussion to representative claims 1 and 5.

Findings of Fact:
1. Miller teaches a method for binding bacteria (target cells) to a solid phase
(Miller Abstract; Ans. 4).
2. Miller’s method comprises coupling bacteriophage proteins to a support
and contacting/incubating the support coupled to the bacteriophage proteins
with a sample of bacteria (Miller ¶ 0012 and 0024; Ans. 4).
3. Miller teaches that the bacteriophage proteins may be protein portions
(e.g., protein fragments) (Miller ¶ 0015; Ans. 4).
4. Miller teaches that the phage proteins are immobilized on suitable
supporting structures (Miller ¶ 0017).
5. Miller teaches that the phage proteins are immobilized “by adsorption or
by covalent binding, wherein the covalent binding is preferred” (Miller ¶
0017).
6. Miller teaches that “a recombinant or biochemical modification of the
phage proteins may be performed in order to accomplish a switch-off of the
enzymatic activity optionally present, thereby improving the binding or
rendering it irreversible” (Miller ¶ 0016; Ans. 4).
7. Miller teaches that “the method is applicable to all bacteria for which
suitable phages are available or will be isolated in future times, or for
bacteria for which corresponding typing phages or phage proteins may be
generated by selection” (Miller ¶ 0036).
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8. Miller teaches that “at least two distinct bacteriophages and/or
bacteriophage proteins recognizing at least two distinct types and/or genera
of bacteria are used” (Miller 5: 34-37 (claim 5)).
9. Miller does not teach the Ply500 and Ply 118 proteins (Ans. 4).
10. Scherer teaches Ply500 which is coded by Listeria phage A500 (Scherer
7: 12).
11. Scherer describes the use of a GFP-CBD500 construct for the detection
of ScottA, Serovar 4b (Scherer 8: 4-13).
12. Scherer teaches that GFP-CBD500 is a fusion of green-fluorescing
protein (GFP) and the CBD of Ply500 (Scherer 7: 28-29).
13. Scherer defines CBD as cell wall-binding domains (Scherer 6: 35).
14. Scherer teaches in addition to Ply500, the CBD of Ply118 may be used
as well (Scherer 8: 23-24; Ans. 4).
15. Neither Miller nor Scherer teach the use of latex beads having an
average surface of between 10 and 1000 µm2/bead and an average diameter
of 1 to 40 µm (Ans. 5).
16. Dorman teach the coupling of proteins to latex polymer particles of
about 0.15 to 1.5 micrometers in diameter (Dorman Abstract and col. 2, ll.
26-30; Ans. 5).

Analysis:
Claim 1:
Based on the combination of references relied upon the Examiner
concludes that
[i]t would have been obvious for a person of ordinary skill in
the art to use the method for binding target cells to a solid
phase, as described by Miller, with Ply500 protein and Ply118
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protein because Scherer . . . discovered that such proteins bind
to the cell wall of cells of the genus Listeria very rapidly and
efficiently.

(Ans. 4.)
In response, Appellant asserts that “the prior art fails to disclose the
use of Ply 500 and Ply 118 peptides together on a single solid support.
Indeed, the prior art teaches the opposite, namely, that the use of one peptide
will suffice” (App. Br. 7). We are not persuaded. Scherer teaches both
Ply500 and Ply118 (FF 10-14). Miller teaches that at least two distinct
bacteriophage proteins may be used in his method for binding bacteria to a
solid phase (FF 8). Therefore, given the express teachings of Miller, it
would have been prima facie obvious to utilize both of Scherer’s Ply500 and
Ply118 in Miller’s method. Accordingly we are not persuaded by
Appellant’s assertion that the use of Ply500 and Ply118 would be redundant
(App. Br. 8).
Appellant asserts that even if the claimed invention is obvious in view
of Miller and Scherer, “the ability of this particular combination [of
proteins] to bind all seven serotypes of Listeria is a surprising and
unexpected result” (App. Br. 7). We are not persuaded.
In order to establish unexpected results for a claimed invention,
objective evidence of non-obviousness must be commensurate in scope with
the claims which the evidence is offered to support. In re Greenfield, 571
F.2d 1185, 1189 (CCPA 1978); In re Lindner, 457 F.2d 506, 508 (1972); In
re Tiffin, 448 F.2d 791, 792 (1971). On this record, claim 1 does not require
that all seven serotypes of Listeria be bound to a solid phase. To the
contrary claim 1 requires only that any one of Listeria Serovar 1/2, 3, 4, 5, 6
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and 7; or any mixture thereof be bound to a solid phase. Based on the
combination of references relied upon one would reasonably expect that
Listeria Serovar 4b would be bound to a solid phase.
On reflection, we are not persuaded by Appellant’s arguments.
Accordingly we affirm the rejection of claim 1 under 35 U.S.C. § 103(a) as
unpatentable over the combination of Miller and Scherer. Claims 2-4, 31,
and 124 fall together with claim 1.

Claim 5:
Based on the combination of references relied upon the Examiner
concludes that “[i]t would have been obvious for a person of ordinary skill in
the art to modify the method for binding target cells, as described by Miller
and Scherer . . . with the use of latex particles” as taught by Dorman (Ans.
5).
In response, Appellant’s assert that
[T]he cited art fails to disclose the use of Ply 500 and Ply 118
peptides together on a single solid support, and also fails to
provide any motivation to arrive at that combination. Dorman .
. . do not address this point, and thus the further reliance on this
reference does nothing to cure the basic deficiency discussed
above.

(App. Br. 9.)
Having found no deficiency in the combination of Miller and Scherer
we are not persuaded by Appellant’s argument to the contrary. As Appellant
provides no other argument against the Examiner’s prima facie case of
obviousness, we affirm the rejection of claim 5 under 35 U.S.C.
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§ 103(a) as unpatentable over the combination of Miller, Scherer, and
Dorman. Claims 6, 7, 14, 15, 21, 25-27, and 125-129 fall together with
claim 5.
CONCLUSION
In summary, we affirm the rejections of record.
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

Ssc:

STEVEN L. HIGHLANDER
FULBRIGHT & JAWORSKI L.L.P.
600 CONGRESS AVENUE, SUITE 2400
AUSTIN, TX 78701

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