Ex Parte Sode et al

Patent Trials and Appeals BoardMar 15, 2019

13282243 - (D) (P.T.A.B. Mar. 15, 2019)

UNITED STA TES p A TENT AND TRADEMARK OFFICE APPLICATION NO. FILING DATE 13/282,243 10/26/2011 9629 7590 03/19/2019 Morgan, Lewis & Bockius LLP (WA) 1111 Pennsylvania Avenue, N.W. Washington, DC 20004 FIRST NAMED INVENTOR Koji Sode 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. 068022-5136 5411 EXAMINER STEADMAN, DAVID J ART UNIT PAPER NUMBER 1656 NOTIFICATION DATE DELIVERY MODE 03/19/2019 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): karen.catalano@morganlewis.com patents@morganlewis.com PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE BEFORE THE PATENT TRIAL AND APPEAL BOARD Ex parte KOJI SODE and KA TSUHIRO KOJIMA 1 Appeal2018-001371 Application 13/282,243 Technology Center 1600 Before ULRIKE W. JENKS, JACQUELINE T. HARLOW, and RYAN H. FLAX, Administrative Patent Judges. FLAX, Administrative Patent Judge. DECISION ON APPEAL This is a decision on appeal under 35 U.S.C. Â§ 134(a) involving claims directed to an isolated mutant glucose dehydrogenase (GDH) enzyme with improved specificity to glucose and reduced reactivity to disaccharides as compared to wild-type GDH. Claims 1-3, 8-11, 15, 16, 18, 19, and 25 are on appeal as rejected under 35 U.S.C. Â§ 103(a) and for obviousness-type double patenting. We have jurisdiction under 35 U.S.C. Â§ 6(b ). We affirm. 2 1 The Real Parties in Interest are ARKRAY, INC. and Bioengineering Laboratories, LLC. Br. 1. 2 Herein we refer to the Specification of Oct. 26, 2011 ("Spec."); the Board's Decision in Appeal No. 2014---007206 mailed Aug. 26, 2016 ("Prior Appeal2018-001371 Application 13/282,243 STATEMENT OF THE CASE This is the second appeal to the Board of a final rejection in this application; the first being in Appeal No. 2014---007206, where the Examiner's obviousness and obviousness-type double patenting rejections over substantially identical claims and the same prior art were affirmed. See Prior Decision (the current and previously appealed claims are the same except they now use the acronym "GDH" rather than the term "glucose dehydrogenase," and a new claim 25 is now included, which is identical to current and previously appealed claim 3; also an anticipation rejection, which was reversed in the Previous Decision, is not presented here); cf Appeal Br. 16-18 (Claims Appendix). As also noted in the Prior Decision (at 2), the Specification describes a mutant glucose dehydrogenase (GDH) enzyme having increased substrate specificity, meaning it is more sensitive to glucose relative to maltose than the wild-type enzyme. Spec. ,r 1. GDHs are useful for glucose sensors and the problem addressed by the invention is that such sensors may have difficulty in accurately measuring the blood sugar (glucose) levels where blood maltose level is high because of a high sensitivity thereto. Id. ,r,r 1-2. A mutant enzyme ofCyGDH (a GDH used for blood glucose sensors and comprising a mutant-type a-subunit that constitutes a cytochrome C- containing GDH; see SEQ ID N0:3) having mutations at its 326th and 365th amino acid residues (positions) where glutamine (Q) and tyrosine (Y) are Decision"); the Final Action ofNov. 4, 2016 ("Final Action"); the Appeal Brief of Aug. 4, 2017 ("Appeal Br."); the Examiner's Answer of Sept. 20, 2017 ("Answer"); and the Reply Brief of Nov. 20, 2017 ("Reply Br."). 2 Appeal2018-001371 Application 13/282,243 substitutions, respectively (referred to as CyGDH(QY)) is known to mitigate the influence of maltose in blood glucose testing. Id. ,r,r 1--4, 7, 10. The invention seeks to improve upon this known mutant by introducing an additional mutation at position 4 72 by replacing the respective amino acid with tyrosine (Y). Id. ,r 6. The appealed claims can be found in the Claims Appendix of the Appeal Brief. Claim 1 is the sole independent claim, is representative, and reads as follows: 1. An isolated mutant GDH comprising an amino acid sequence at least 80% identical to the amino acid sequence of SEQ ID NO: 3 and having GDH activity, wherein amino acid residues of the mutant GDH corresponding to positions 326, 365 and 472 of SEQ ID NO: 3 are replaced with glutamine, tyrosine and tyrosine, respectively, wherein said mutant GDH shows an increased substrate specificity to glucose and a reduced reactivity to disaccharides as compared to a wild-type GDH having the amino acid sequence of SEQ ID NO: 3. Appeal Br. 16 (Claims Appendix); cf Prior Decision 2-3 (reproducing claim 1, as previously appealed). The following rejections are on appeal: 3 Claims 1-3, 8-11, 15, 16, 18, 19, and 25 stand rejected under 35 U.S.C. Â§ I03(a) over Sode4 and Yamaoka '833. 5 Final Action 3. 3 Compare with the final rejections previously appealed. Prior Decision 3. 4 US 7,741,090 B2 (issued June 22, 2010) ("Sode"). 5 US 2008/0206833 Al (published Aug. 28, 2008) ("Yamaoka '833"). 3 Appeal2018-001371 Application 13/282,243 Claims 1-3, 8-11, 15, 16, 18, 19, and 25 stand rejected for obviousness-type double patenting over claims 1, 3-8, 11, 13, 15, and 20-25 of Yamaoka '969. 6 Id. at 11. Claims 1-3, 8-11, 15, 16, 18, 19, and 25 stand rejected for obviousness-type double patenting over claims 1 and 4--10 of Yamaoka '5927 in view of Yamaoka '833. Id. at 15. FINDINGS OF FACT We adopt the findings of fact as set forth in the Prior Decision ( at 4-- 9), which, except as directed to the previously appealed anticipation rejection, adopted and incorporated the Examiner's findings of fact and rationale relating to the prior, final obviousness and obviousness-type double patenting rejections. The currently appealed rejections are identical to those addressed in the Prior Decision; we again adopt the Examiner's current findings of fact and rationale on obviousness and obviousness-type double patenting as set forth in the Final Action and Answer. See Final Action 3- 20; Answer 2-25. Any further findings of fact set forth below highlight certain evidence of record. DISCUSSION "[T]he examiner bears the initial burden, on review of the prior art or on any other ground, of presenting aprimafacie case ofunpatentability. If that burden is met, the burden of coming forward with evidence or argument shifts to the applicant." In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992). Arguments made by Appellants in the Appeal Brief and properly presented 6 US 7,604,969 B2 (issued Oct. 20, 2009) ("Yamaoka '969"). 7 US 7,803,592 B2 (issued Sept. 28, 2010) ("Yamaoka '592"). 4 Appeal2018-001371 Application 13/282,243 in the Reply Brief have been considered in this Decision; arguments not so- presented in the Brief are waived. See 37 C.F.R. Â§ 4I.37(c)(l)(iv) (2015); see also Ex parte Borden, 93 USPQ2d 1473, 1474 (BPAI 2010) (informative) ("Any bases for asserting error, whether factual or legal, that are not raised in the principal brief are waived."). Obviousness As applicable to the rejections on appeal and Appellants' arguments there-over, "[t]he combination of familiar elements according to known methods is likely to be obvious when it does no more than yield predictable results." KSR Int'! Co. v. Teleflex Inc., 550 U.S. 398,416 (2007). Put another way, "when a patent claims a structure already known in the prior art that is altered by the mere substitution of one element for another known in the field, the combination must do more than yield a predictable result." Id. ( citation omitted). "[T]he question is whether there is something in the prior art as a whole to suggest the desirability, and thus the obviousness, of making the combination, not whether there is something in the prior art as a whole to suggest that the combination is the most desirable combination available." In re Fulton, 391 F.3d 1195, 1200 (Fed. Cir. 2004) (citation omitted). Picking one of a finite number of known solutions to a known problem is obvious. KSR, 550 U.S. at 421. Furthermore, "[ o ]bviousness does not require absolute predictability of success .... For obviousness underÂ§ 103, all that is required is a reasonable expectation of success." In re O 'Farrell, 853 F.2d 894, 903---04 (Fed. Cir. 1988) (citations omitted). The Federal Circuit has explained that: One way for a patent applicant to rebut a prima facie case of obviousness is to make a showing of 'unexpected results,' i.e., to 5 Appeal2018-001371 Application 13/282,243 show that the claimed invention exhibits some superior property or advantage that a person of ordinary skill in the relevant art would have found surprising or unexpected. In re Soni, 54 F.3d 746, 750 (Fed. Cir. 1995). However, "'differences in degree' of a known and expected property are not as persuasive in rebutting obviousness as differences in 'kind'-i.e., a new property dissimilar to the known property." Bristol-Myers Squibb Co. v. Teva Pharms. USA, Inc., 752 F.3d 967, 977 (Fed. Cir. 2014) (citation omitted). Once again, the Examiner has determined that the claims would have been obvious over the Sode-Yamaoka '833 prior art combination. Final Action 3-11 and Answer 2-6, 14--23 (citing Sode 7:60-8:14, claim 2; citing Yamaoka '833 ,r,r 11, 32-33, 37, 45, 86 (Table 17), 93 (Table 22), 101 (Table 24), 102, Figures 3-5, claims 3-5, 8, 14, 16, 23, 24, 27, 28, 30, 32). Specifically, the Examiner determined that Sode teaches and suggests a method for producing glucose dehydrogenase with SEQ ID N0:3 with 1-10, but preferably 1-3 substituted amino acid residues, having glucose dehydrogenase activity. See Sode 7:60-8:14, claim 2. The Examiner further determined that Yamaoka '83 3 teaches and suggests that 3 such amino acid substitutions should be at positions 326, 365, and 472 of SEQ ID N0:3, including providing glutamine at position 326 (326Q), providing tyrosine at position 365 (365Y), and providing tyrosine at position 472 (472Y). See Yamaoka '833 ,r,r 11, 33--45, 86-87, 91, 101, 106, claims 1, 3, 4, 8, 9, 12, 14, 16 (disclosing various combinations of 326Q, 365Y, and 472Y substitutions with reactivity to glucose and suppressed influence of maltose); see also Spec. ,r 4 (Background: indicating that mutations 326Q+365Y were known in the prior art). Yamaoka '833 disclosed that making such amino 6 Appeal2018-001371 Application 13/282,243 acid substitutions "'improved substrate specificity to glucose' [and] reduced reactivity to other monosaccharides, disaccharides and oligosaccharides such as maltose .... " Yamaoka '833 ,r,r 32--45, 86, 90-91, 93, 101-106. We discern no error in the Examiner's determinations. "Appellants assert that the Examiner is in clear error at least because ... of the unexpected superior property of the claimed combination of mutations recited in the claims, which are not present in the combinations of mutations in the cited references." Appeal Br. 4. The unexpected result alleged by Appellants is The claimed GDH having a substitution at position 472 with tyrosine ( 472Y) in combination with glutamine at position 326 (326Q) and tyrosine at position 365 (365Y) in SEQ ID NO: 3 possesses an unexpected superior glucose specificity and maltose reactivity for glucose measurements compared to 326Q and 365Y mutations alone (QYA) and also compared to other possible mutations at position 472 in combination with 326Q and 365Y in SEQ ID NO: 3. Id. at 5. As evidence of the unexpected superiority in including the 472Y substitution with the 326Q and 365Y substitutions, Appellants point to Table 7 of their Specification, reproduced below: 7 Appeal2018-001371 Application 13/282,243 [Table Tl Spec. ,r 72. Appellants argue "[a]s shown in Table 7 of the specification (reproduced [above]), mutant GDH having 472D, 472G, 472K, 472L, 472P, 472Q, 472R, 472T, 472Vand 472Y in combination with 326Q and 365Y in SEQ ID NO: 3 maintained glucose reactivity while maltose reactivity was reduced." Appeal Br. 5; see also Spec. ,r 73. Then, turning to Table 8 from their Specification (reproduced below), Appellants argue "only 472Y maintained enzyme activities while the enzyme activities of 472D, 472G, 472K, 472L, 472P, 472Q, 472R, 472T, and 4 72V were significantly reduced compared to having no mutation at position 472 (QYA) as shown in Table 8 of the specification below." Appeal Br. 5---6. 8 Appeal2018-001371 Application 13/282,243 IT:i.blc SJ Q\".'\ Km(Gh::):o:..16.! 01M _ Vs:r,.~x. {Gh:..) ..... 14~t3 Uimg ~1~1:.::ta ....... """ SrnM i-OmM 2'5rn~1 I 34 4 {HU.~{~} {:tÂ·~H5~ .. 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