Ex Parte Tuinstra et alDownload PDFPatent Trials and Appeals BoardJul 5, 201911951629 - (D) (P.T.A.B. Jul. 5, 2019) Copy Citation UNITED STA TES p A TENT AND TRADEMARK OFFICE APPLICATION NO. FILING DATE 11/951,629 12/06/2007 26691 7590 07/05/2019 POTTER ANDERSON & CORROON LLP ATTN: JANETE. REED, PH.D. P.O. BOX 951 WILMINGTON, DE 19899-0951 FIRST NAMED INVENTOR Mitchell R. Tuinstra 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. KSURF-13454/USl/ORD 8722 EXAMINER KOV ALENKO, MYKOLA V ART UNIT PAPER NUMBER 1662 MAIL DATE DELIVERY MODE 07/05/2019 PAPER 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. PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE BEFORE THE PATENT TRIAL AND APPEAL BOARD Ex parte MITCHELL R. TUINSTRA and KASSIM AL-KHATIB Appeal2018-001278 Application 11/951,629 Technology Center 1600 Before FRANCISCO C. PRATS, JEFFREYN. FREDMAN, and ERICA A. FRANKLIN, Administrative Patent Judges. FREDMAN, Administrative Patent Judge. DECISION ON APPEAL This is an appeal 1,2 under 35 U.S.C. § 134 involving claims to a method of controlling weeds in the vicinity of a cultivated sorghum hybrid. The Examiner rejected the claims as obvious. We have jurisdiction under 35 U.S.C. § 6(b). We reverse. 1 Appellants identify the Real Party in Interest as E. I. du Pont de Nemours and Company (see App. Br. 3). 2 We have considered the Specification of Dec. 6, 2007 ("Spec."); Final Office Action of Mar. 29, 2017 ("Final Act."); Appeal Brief of June 21, 2017 ("App. Br."); Examiner's Answer of Oct. 4, 2017 ("Ans."); and Reply Brief of Nov. 20, 2017 ("Reply Br."). Appeal2018-001278 Application 11/951,629 Statement of the Case Background "Sorghum is the second most important cereal-feed grain grown in the United States. Production is economically critical to farms operating in marginal rainfall areas because of sorghum's ability to tolerate drought and heat" (Spec. 1: 15-17). "[T]he use of herbicides for controlling weeds in crops has become almost a universal practice. However, application of such herbicides can also result in death or reduced growth of the desired crop plant" (Spec. 1 :26-28). One "class of broad-spectrum herbicides are those that inhibit the activity of the acetolactate synthase (ALS) enzyme in a plant" (Spec. 2:2-3). "Acetolactate synthase herbicides control a wide spectrum of grass and broadleaf weeds at very low application rates" (Spec. 2:9-10). However, "[s]orghum is susceptible to many ALS inhibiting herbicides ... making the use of these herbicides to control grassy weeds almost impossible" (Spec. 2:2-7). "[T]he present invention provides for sorghum plants, plant tissues and plant seeds that contain altered acetolactate synthase (ALS) genes and proteins that are resistant to inhibition by herbicides that normally inhibit the activity of the ALS protein" (Spec. 2:22-25). The Claims Claims 11, 12, 19, 35, and 40-43 are on appeal. Independent claim 11 is representative and reads as follows: 11. A method of controlling weeds in the vicinity of a cultivated sorghum hybrid comprising: a) growing said cultivated sorghum hybrid from a seed containing a nucleotide sequence having at least 95% homology to SEQ ID NO: 1, provided that said nucleic 2 Appeal2018-001278 Application 11/951,629 acid sequence encodes a modified sorghum acetolactate synthase protein comprising a valine to isoleucine amino acid substitution at position 531 and a tryptophan to leucine amino acid substitution at position 545, wherein the expression of said nucleotide sequence confers to said cultivated sorghum hybrid increased resistance to inhibition by one or more acetolactate synthase herbicides compared to a cultivated sorghum hybrid not expressing said nucleotide sequence; b) applying one or more acetolactate synthase herbicides to a field comprising the cultivated sorghum hybrid of step (a), and c) controlling weeds in the vicinity of said cultivated sorghum hybrid such that weed growth is adversely affected by the application of said one or more herbicides and growth of said cultivated sorghum hybrid is not adversely affected. Discussion The Examiner rejected claims 11, 12, 19, 35, and 40-43 under 35 U.S.C. § I03(a) as obvious over Bemasconi, 3 Kmiec, 4 Kakefuda, 5 Anderson, 6 Chong,7 Peterson, 8 and Dweikat9 (Final Act. 6-13). 3 Bernasconi et al., US 5,633,437, issued May 27, 1997. 4 Kmiec et al., US 2003/0236208 Al, published Dec. 25, 2003. 5 Kakefuda et al., US 5,853,973, issued Dec. 29, 1998. 6 Anderson et al., US 6,211,438 Bl, issued Apr. 3, 2001. 7 Chong et al., Amino Acid Residues Conferring Herbicide Tolerance in Tobacco Acetolactate Synthase, 279 BIOCHEM. BIOPHYS. RES. COMM. 462- 67 (2000). 8 Peterson et al., Registration of Tx2783 Greenbug Resistant Sorghum Germplasm Line, 24 CROP SCIENCE 390 (1984). 9 Dweikat, A diploid, interspecific, fertile hybrid from cultivated sorghum, Sorghum bicolor, and the common Johnsongrass weed Sorghum halepense, 16 MOLECULAR BREEDING 93-101 (2005). 3 Appeal2018-001278 Application 11/951,629 Appellants contend "while Bernasconi describes five cocklebur ALS amino acid residues, including the homologous Trps4sLeu amino acid substitution ... nowhere does Bernasconi provide even a hint that would prompt the skilled artisan to home in on the Vals31 position" (App. Br. 19). Appellants further contend "none of the other references disclose, teach, suggest, or even hint at the sorghum ALS Vals31Ile amino acid substitution let alone a sorghum ALS containing both the Vals31Ile and Trps4sLeu amino acid substitutions" (App. Br. 20). Appellants further note that "[ w ]hile Appellants do recognize that the present claims are directed to a method of using the sorghum ALS Vals31Ile/Trps4sLeu variant, the claims nonetheless require a plant expressing a nucleotide sequence having at least 95% homology to SEQ ID NO: 1 and encoding these two mutations" (App. Br. 21 ). Appellants contend "the skilled artisan would not find it obvious to modify either the wild type or mutant cocklebur sequences of Bernasconi to arrive at the present claims" (App. Br. 21). The Examiner responds "[t]here is no evidence in the record that Val531Ile contributes to ALS inhibitor resistance either on its own or in combination with Trp545Leu. The teachings of the prior art suggest that Val531Ile, in fact, does not contribute to herbicide resistance of the enzyme" (Ans. 13). The Examiner finds that Bernasconi teaches "a wild-type, herbicide sensitive ALS from cocklebur contains an isoleucine at position corresponding to position 531 of the sorghum ALS" (Ans. 13). The Examiner finds "position Val531 is located outside of the five conserved ALS domains, in which herbicide resistance mutations are located" (Ans. 14). The Examiner finds "a valine to isoleucine substitution would be 4 Appeal2018-001278 Application 11/951,629 considered a conserved substitution" (Ans. 14). The Examiner concludes that "a sorghum plant comprising an ALS with the Trp545Leu substitution alone would be functionally equivalent to a sorghum plant comprising an ALS with both, Trp545Leu and Val531Ile substitutions, relative to a wild- type enzyme" (Ans. 14--15). Claim 11 requires, as part of the method of controlling weeds around sorghum plants, a sorghum hybrid plant with three requirements: (1) 95% homology to SEQ ID NO: 1; (2) a Vals31Ile mutation; and (3) a Trps4sLeu mutation. While we agree with the Examiner that Sala10,11 and Bernasconi reasonably suggest the Trps4sLeu mutation results in herbicide resistance, we agree with Appellants that the rejection does not provide sufficient reason to either select a Vals31Ile mutation or a sequence 95% homologous to SEQ ID NO: 1. We agree with Appellants (see Reply Br. 12) that the citation to In re Seid, 161 F.2d 229 (CCPA 1947) is inapposite because Seid dealt with ornamental arrangements, not a structural element of a nucleic acid that is asserted by the Specification as being found "in herbicide resistance genotypes" (Spec. 26:26-29). Instead, "we must give effect to all claim limitations." In re Angstadt, 537 F.2d 498, 501 (CCPA 1976). We therefore read the recitation requiring a Vals31Ile mutation as a positive limitation of claim 1. While the Examiner provides some generic evidence suggesting that the Vals31Ile mutation may not impact herbicidal resistance, we note that 10 Sala et al., WO 2007/005581 A2, published Jan. 11, 2007. 11 As we are reversing, we need not determine whether Sala was properly cited by the Examiner as rebuttal evidence. 5 Appeal2018-001278 Application 11/951,629 conserved point mutations may certainly impact protein activity. 12 This generic evidence is not sufficient to rebut the presumption of operability of the Vals31Ile. We therefore conclude that the evidence of record does not provide a teaching or reason in the prior art to incorporate a Vals31Ile mutation into the acetolactate synthase gene in sorghum. We also note that while the Examiner cites Kakefuda for an acetolactate synthase sequence 95% homologous to SEQ ID NO: 1, no reason is given to select this sequence for insertion into Sorghum plants. The Examiner states regarding Kakefuda that: Kakefuda et al teach making ALS herbicide resistant sorghum at Table 1, column 19. Kakefuda et al teach using herbicide resistant plants in a method of controlling weeds by applying an ALS herbicide (Kakefuda et al, paragraph spanning columns 20-21). Kakefuda et al teach, at SEQ ID NO: 4, an amino acid sequence from maize that has 95.2% identity to the instant SEQ ID NO: 6 .... One would recognize that the sequence of Kakefuda et al has a tryptophan in the position corresponding to position 574 in Arabidopsis numbering (545 in the instant SEQ ID NO: 6), and thus represents a wild-type version of the instant SEQ ID NO: 6 with respect to the Trp574Leu mutation. (Ans. 8-10). 12 We do not rely upon, but simply cite to show this point, Wu et al., A Conservative Isoleucine to Leucine Mutation Causes Major Rearrangements and Cold Sensitivity in KlenTaql DNA Polymerase, 54 Biochemistry 881-9 (2015). Wu asks "[h]ow can a conservative mutation located over 20 A away from the active site affect activity selectively at lower temperature?" (Wu 886) but then explains "the mutation can affect the structure and function of the enzyme despite the large distance between the mutation and the enzyme active site" (Wu 887-8). 6 Appeal2018-001278 Application 11/951,629 Simply because the maize acetolactate synthase sequence has 95% identity to SEQ ID NO: 1 does not provide any reason to select this sequence. The "examiner bears the initial burden ... of presenting a prima facie case ofunpatentability." In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992). Here, we find the Examiner has not satisfied that burden because the rejection fails to provide a persuasive reason why a person of ordinary skill in the art would have selected a seed containing a nucleotide sequence having 95% identity to SEQ ID N0:1. SUMMARY We reverse the rejection of claims 11, 12, 19, 35, and 40-43 under 35 U.S.C. § 103(a) as obvious over Bernasconi, Kmiec, Kakefuda, Anderson, Chong, Peterson, and Dweikat. REVERSED 7 Copy with citationCopy as parenthetical citation