Ex Parte Best et al

Patent Trial and Appeal BoardMar 22, 2017

13773395 (P.T.A.B. Mar. 22, 2017)

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. 13/773,395 02/21/2013 Elaine A. Best 009097- 8009.US01 9395 118919 7590 03/24/2017 Prismatic Law Group, PLLC 5335 Wisconsin Ave NW. Suite 440 Washington, DC 20015-2052 EXAMINER ROONEY, NORA MAUREEN ART UNIT PAPER NUMBER 1644 NOTIFICATION DATE DELIVERY MODE 03/24/2017 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): ronkamis@prismaticlaw.com kamisip @ patentwatchonline. com PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE BEFORE THE PATENT TRIAL AND APPEAL BOARD Ex parte ELAINE A. BEST and MARTIN J. McDERMOTT Appeal 2016-003585 Application 13/773,3951 Technology Center 1600 Before DEMETRA J. MILLS, ERIC B. GRIMES, and DAVID COTTA, Administrative Patent Judges. COTTA, Administrative Patent Judge. DECISION ON APPEAL This is an appeal under 35 U.S.C. § 134 involving claims to a method of producing a recombinant protein. The Examiner rejected the claims on appeal as obvious under 35 U.S.C. § 103(a). We affirm. 1 According to Appellants, the real parties in interest is Merck Patent GmbH. App. Br. 3. Appeal 2016-003585 Application 13/773,395 STATEMENT OF THE CASE Claims 1—4, 7, 8, 12—15, 41, and 45—48 are on appeal. Claims 1 and 41 are the only independent claims. Claim 1 is illustrative and reads as follows: 1. A method to produce a recombinant protein comprising a recombinant mite Group 1 protein comprising the steps of: (a) culturing a methyltrophic yeast microorganism transformed with a nucleic acid molecule encoding said recombinant mite Group 1 protein; and (b) recovering said recombinant mite Group 1 protein from said methyltrophic yeast microorganism; wherein said recombinant mite Group 1 protein is selected from the group consisting of: Dermatophagoides farinae, Dermatophagoides pteronyssinus, and Euroglyphus maynei recombinant mite Group 1 proteins (Der f 1, Der p 1 and Eur ml) and has a function selected from the group consisting of: selectively binding IgE and causing proliferation of a T cell that proliferates in response to a native mite Group 1 protein selected from the group consisting of Der f 1, Der p 1 and Eur m 1 and said nucleic acid molecule consists of a nucleic acid sequence selected from the group consisting of: SEQ ID NO:l, SEQ ID NO:4, SEQ ID NO:7, SEQ ID NO: 13, SEQ ID NO: 16, SEQ ID NO: 19, SEQ ID NO:22, SEQ ID NO:25, SEQ ID NO:28, SEQ ID NO:31, SEQ ID NO:34, SEQ ID NO:37, SEQ ID NO:40, SEQ ID NO:43, SEQ ID NO:64, SEQ ID NO:69, SEQ ID NO:76, SEQ ID NO:81, SEQ ID NO:86, and SEQ ID NO:91 wherein said nucleic acid molecule is optionally fused to a signal sequence. App. Br. 9. 2 Appeal 2016-003585 Application 13/773,395 The Examiner rejected the claims under 35 U.S.C. § 103(a) as unpatentable over Garman I,2 Garman II,3 Garman III,4 and Garman IV5 each in view of Sowka.6 ANALYSIS Appellants argue claims 1—4, 7, 8, 12—15, 41, and 45—48 together as a group. We designate claim 1 as representative. The Examiner found that Garman I, II, III and IV (collectively “the Garman References”) each disclosed “production of the Dermatophagoides farinae Der f 1 polypeptide encoded by the nucleic acid of reference SEQ ID NO:5 which comprises instant SEQ ID NO: 1.” Ans. 3.7 The Examiner further found that the Garman References disclosed that the recombinant protein could be expressed in yeast. Id. The Garman References, however, differ from the claimed method in that they do not disclose the expression of Dermatophagoides farinae Der f 1 in “methyltrophic yeast” as recited in claim 1. Id. at 4. 2 Garman et al., US Patent No. 5,820,862, issued Oct. 13, 1998 (“Garman I”). 3 Garman et al., US Patent No. 5,968,526, issued Oct. 19, 1999 (“Garman II”). 4 Garman et al., US Patent No. 6,268,491 Bl, issued July 31, 2001 (“Garman III”). 5 Garman et al., US Patent No. 7,288,256 Bl, issued Oct. 30, 2007 (“Garman IV”). 6 Sowka et al., Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and a Major Allergen of Avocado, and its Expression in the Yeast Pichia Pastoris, 273(43) Journal of Biological Chemistry 28091- 97 (1998) (“Sowka”). 7 Garman I, II, III and IV all claim priority from a common parent and share, in relevant respects, substantially the same disclosure. 3 Appeal 2016-003585 Application 13/773,395 The Examiner found that Sowka disclosed the recombinant production of an avocado allergen in Pichia pastoris, a methyltrophic yeast. Id. at 4—5. The Examiner further found that Sowka taught that the Pichia pastoris was used to “take advantage of the eukaryotic folding machinery, which is important for producing proteins with enzyme activity,” and that “the recombinantly produced Prs a 1 allergen was correctly folded, bound IgE and had enzymatic activity, making it equivalent to natural Prs a 1.” Id. at 4. The Examiner concluded that it would have been obvious to produce the peptide disclosed in the Garman References using Pichia pastoris methyltrophic yeast, because Sowka taught that “allergens with enzymatic activity can be recombinantly produced in Pichia pastoris yeast” with “proper folding with enzymatic and antibody binding characteristics like that of the wild type allergen.” Id. at 4—5. We agree with and adopt the Examiner’s findings and reasoning, and agree that claim 1 would have been obvious based on the Garman References and Sowka. Appellants argue that Sowka is directed to recombinant production of a plant protein and that “the methods disclosed in Sowka for the expression of plant proteins cannot be employed to express arthropod proteins without significant modifications.” App. Br. 7. Appellants, however, do not identify any evidence to support their argument that significant modifications would be required in order to express an arthropod protein recombinantly in Pichia pastoris. See, Johnston v. IVAC Corp., 885 F.2d 1574, 1581 (Fed. Cir. 1989) (“Attorneys’ argument is no substitute for evidence.”); See also, In re Pearson, 494 F.2d 1399, 1405 (CCPA 1974). Appellants contend that “[pjrior to the instant claimed subject matter, the attempts of scientists in the art to achieve th[e] result of the claimed 4 Appeal 2016-003585 Application 13/773,395 subject matter was unsuccessful in several different expression systems.” App. Br. 6. We are not persuaded because Appellants have not identified persuasive evidence that Appellants provided a solution to a recognized problem. See, In re Gershon, 372 F.2d 535, 538 (CCPA 1967) (“Since the alleged problem in this case was first recognized by appellants, and others apparently have not yet become aware of its existence, it goes without saying that there could not possibly be any evidence of either a long-felt need in the . . . art for a solution to a problem of dubious existence or failure of others skilled in the art who unsuccessfully attempted to solve a problem of which they were not aware.”). The Specification teaches only that prior art methods of expressing the claimed proteins were inferior to the claimed method, not that they failed to produce the claimed protein. See, Spec. 2—3 (teaching that prior art methods produced “very low yields,” enjoyed “only limited success in producing an active, easily purified . . . protein,” “exhibited only about 50% of the IgE reactivity of the native protein,” and “required an additional post purification step of either acid or enzymatic treatment to cleave the pro-form to a mature form”). While the claimed process may well represent an improvement on these prior art processes, this is not sufficient to establish the failure of others as an objective indicium of non-obviousness. In this regard, we note that the claims do not require any particular yield, ease of purification, and/or absence of post-purification steps. Further, while claim 1 requires that the recombinant mite Group 1 protein “has a function selected from the group consisting of: selectively binding IgE and causing proliferation of a T cell that proliferates in response to native mite Group 1 5 Appeal 2016-003585 Application 13/773,395 protein . . . the claim does not require a particular level of IgE reactivity relative to the native protein. Appellants argue that “surprisingly, the claimed specific variants of Der f 1, Der p 1 and Eur m 1 nucleic acid sequences overcome these problems [in the prior art]. . . being easily and successfully processed and secreted and resulting in soluble mature fully active Der f 1, Der p 1 and Eur m 1 proteins.” App. Br. 6. However, we agree with the Examiner: Producing an active, fully functional, recombinant protein which binds to IgE in mite-allergic patients in a manner equivalent to native allergen is neither a surprising nor an unexpected result given the teachings of Sowka et al. which resulted in an active, fully functional recombinant protein allergen which binds to IgE equivalently to native allergen. Ans. 6. See also, Sowka 28095, right col. (“[T]he recombinant protein was correctly folded and equivalent to its natural counterpart.”). Moreover, Appellants have not provided persuasive evidence that practicing the claimed process produced unexpected results as compared to the closest prior art. See, Johnston 885 F.2d at 1581; Pearson, 494 F.2d at 1405. Accordingly, we affirm the Examiner’s rejection of claim 1. Because they were not argued separately, claims 2-4, 7, 8, 12—15, 41, and 45—48 fall with claim 1. SUMMARY For these reasons and those set forth in the Examiner's Answer, and the Final Office Action, the Examiner’s decision to reject claims 1—4, 7, 8, 12—15, 41, and 45—48 is affirmed. 6 Appeal 2016-003585 Application 13/773,395 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). AFFIRMED 7