Ex Parte LoessnerDownload PDFBoard of Patent Appeals and InterferencesMay 22, 200810406897 (B.P.A.I. May. 22, 2008) Copy Citation 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 ____________ Decided: May 22, 2008 ____________ 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 2 Appeal 2008-2122 Application 10/406,897 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. 3 Appeal 2008-2122 Application 10/406,897 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). 4 Appeal 2008-2122 Application 10/406,897 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 5 Appeal 2008-2122 Application 10/406,897 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 6 Appeal 2008-2122 Application 10/406,897 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. 7 Appeal 2008-2122 Application 10/406,897 § 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 8 Copy with citationCopy as parenthetical citation