Ex Parte Levinson et alDownload PDFPatent Trial and Appeal BoardFeb 28, 201310518701 (P.T.A.B. Feb. 28, 2013) Copy Citation 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. 10/518,701 09/01/2005 Arnold I Levinson 133172.02201 5645 34136 7590 03/01/2013 Pepper Hamilton LLP 400 Berwyn Park 899 Cassatt Road Berwyn, PA 19312-1183 EXAMINER SZPERKA, MICHAEL EDWARD ART UNIT PAPER NUMBER 1644 MAIL DATE DELIVERY MODE 03/01/2013 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 ARNOLD I. LEVINSON, SANDRA CALAROTA, DAVID B. WEINER, and MIGUEL OTERO __________ Appeal 2011-000475 Application 10/518,701 Technology Center 1600 __________ Before DONALD E. ADAMS, ERIC GRIMES, and ERICA A. FRANKLIN, Administrative Patent Judges. FRANKLIN, Administrative Patent Judge. DECISION ON APPEAL This is an appeal under 35 U.S.C. § 134(a) involving claims to isolated nucleic acid molecules encoding a protein comprising at least one epitope of membrane IgE and at least one nonIgE helper T cell epitope fused by a proteolytic cleavage sequence, and to isolated nucleic acid molecules encoding a protein comprising at least one epitope of membrane IgE and an IgE leader sequence. The Patent Examiner rejected the claims as obvious. We have jurisdiction under 35 U.S.C. § 6(b). We affirm and enter a New Ground of rejection, pursuant to 37 C.F.R. § 41.50(b). Appeal 2011-000475 Application 10/518,701 2 STATEMENT OF THE CASE The Specification states: B cell membrane IgE structure differs from that of IgE in the serum (which finds its way to the surface of mast cells) by containing an additional protein fragment that is found in its cytoplasmic, transmembrane, and membrane-proximal extracellular domains. Accordingly, it should be possible to generate an immune response against components of membrane IgE that will not react with serum IgE. Such an immune response will not be competed by in the serum and will not target IgE sitting on mast cells. Therefore, patients will not be at risk for potentially deleterious mast cell release reactions. Importantly, these membrane IgE components differ significantly from the B cell membrane constituents of IgG and IgM. Therefore, B cells expressing these immunoglobulin isotypes, which represent critical players in normal host defense, will not be targeted. According to the invention, immune responses to IgE bearing B cells are elicited. These immune responses make it possible for the allergic host to scuttle not only IgE bearing B cells in the extant immune repertoire but also those that might develop in the future. This approach has important advantages over a monoclonal anti-IgE antibody, which targets serum IgE. The latter biologic agent requires multiple injections of extremely costly compositions, and its use will likely be limited to a small subset of allergic individuals. By contrast, the immunotherapeutic strategy employed in the present invention requires limited patient encounters and will be very inexpensive to mass-produce. Accordingly, it should enjoy widespread use amongst populations of allergic patients. (Spec. 6, l. 15- 7, l. 2.) Appeal 2011-000475 Application 10/518,701 3 Claims 1-3, 5-8, 22-24, 26-29, 32-37, 50 58-73 are on appeal. Claims 1, 8, and 51 1 are representative and read as follows: 1. An isolated nucleic acid molecule that encodes a protein comprising at least one epitope of membrane IgE and at least one nonIgE helper T cell epitope, and being free of epitopes of serum IgE, wherein said epitope of membrane IgE and said nonIgE helper T cell epitope are fused by a proteolytic cleavage sequence. 8. A vaccine composition comprising a nucleic acid molecule that encodes a protein comprising an IgE leader sequence and at least one epitope of membrane IgE and being free of epitopes of serum IgE, and a pharmaceutically acceptable carrier or diluent. 51. An isolated nucleic acid molecule that encodes a protein comprising an IgE leader sequence and at least one epitope of membrane IgE and being free of epitopes of serum IgE. (App. Br. 38-40, Claims App‟x.)(Emphasis added). The Examiner rejected the claims as follows: A. Claims 1-3, 5-7, 22-24, and 26-29 under 35 U.S.C. § 103(a) as unpatentable over Chen, 2 Wang, 3 Hollis, 4 and Rutter; 5 B. Claims 1-3, 5-7, 22-24, and 26-29 under 35 U.S.C. § 103(a) as unpatentable over Klysner „038, 6 Wang, and Rutter; 1 In the Answer, the Examiner states that “[c]laims 1-3, 5-8, 22-24, 26-29, 32-37, and 50-73 are rejected in this application.” (Ans. 2.) However, none of the rejections includes independent claim 51 or its dependent claims 52- 57. Claims 51-57 are subject to a new ground of rejection infra. 2 Patent Application Publication No. WO 98/53843 by Alex Chen et al., published Dec. 3, 1998. 3 Patent Application Publication No. WO 99/67293 by Chang Wang et al., published Dec. 29, 1999. 4 US Patent No. 5,629,415 issued to Gregory F. Hollis et al., May 13, 1997. 5 US Patent No. 4,769,326 issued to William J. Rutter, Sep. 6, 1988. Appeal 2011-000475 Application 10/518,701 4 C. Claims 1-3, 5-7, 22-24, and 26-29 under 35 U.S.C. § 103(a) as unpatentable over Klysner „673, 7 Wang, and Rutter; D. Claims 8, 32-37, 50, and 58-73 under 35 U.S.C. § 103(a) as unpatentable over Chen, Wang, Hollis, Rutter, and Walls, 8 as evidenced by Janeway; 9 E. Claims 8, 32-37, 50, and 58-73 under 35 U.S.C. § 103(a) as unpatentable over Klysner „038, Wang, Hollis, Rutter, and Walls, as evidenced by Janeway; F. Claims 8, 32-37, 50, and 58-73 under 35 U.S.C. § 103(a) as unpatentable over Klysner „673, Wang, Rutter, and Walls, as evidenced by Janeway; G. Claims 8, 32-37, and 58-73 under 35 U.S.C. § 103(a) as unpatentable over Klysner „673 and Walls, as evidenced by Janeway; 10 H. Claims 8, 32-37, and 58-73 under 35 U.S.C. § 103(a) as unpatentable over Klysner „038 and Walls, as evidenced by Janeway. 11 6 Patent Application Publication No. WO 02/20038 A2 by Steen Klysner et al., published Mar. 14, 2002. 7 Patent Application Publication No. US 2002/0172673 A1 by Steen Klysner et al., published Nov. 21, 2002. 8 Michael A. Walls et al., Vectors for the expression of PCR-amplified immunoglobulin variable domains with human constant regions, 21 NUCLEIC ACIDS RESEARCH, 2921-2929 (1993). 9 Charles A. Janeway, IMMUNOBIOLOGY: THE IMMUNE SYSTEM IN HEALTH AND DISEASE 3:26-3:31(Garland Publishing Inc., 3rd. ed. 1997). 10 The Examiner withdrew the rejection of claim 50 over Klysner „673 and Walls, as evidenced by Janeway. (Ans. 19.) 11 The Examiner withdrew the rejection of claim 50 over Klysner „038 and Walls, as evidenced by Janeway. (Ans. 19.) Appeal 2011-000475 Application 10/518,701 5 OBVIOUSNESS A. The Rejection over Chen, Wang, Hollis, and Rutter. The Examiner found that Chen disclosed “vaccine constructs comprising the membrane bound domain of IgE coupled to heterologous sequences and excipients.” (Ans. 5.) The Examiner found that the heterologous antigens comprise helper T epitopes and that Chen disclosed that its conjugates suppress IgE mediated responses, such as those that occur in an allergic response. (Id.) The Examiner found that “[t]he disclosure of Chen et al. differs from the instant claimed invention in that the nucleic acids of Chen et al. are not disclosed as being administered to a patient (i.e. the nucleic acids are not disclosed as a vaccine) nor are they disclosed as comprising a proteolytic cleavage sequence.” (Id.) The Examiner found that Wang disclosed vaccine constructs wherein the IgE sequence is coupled to a helper T cell epitope, such as those from tetanus toxoid, wherein the administered construct is a nucleic acid. (Id.) Additionally, the Examiner found that Wang disclosed inserting a linker sequence between IgE and T helper epitopes to advantageously: (a) disrupt artificial secondary structures that result from directly joining the C-terminus of one epitope directly to the N-terminus of the other epitope; and (b) act as a flexible hinge that allows for more effective interactions with immune cells. (Id. at 5-6.) The Examiner found that Hollis taught that recombinant IgE encoding polynucleotides can be inserted into plasmid vectors and used to generate a wide variety of host cells including bacterial and mammalian cells. (Id. at 6.) Additionally, the Examiner found that Hollis taught that such host cells Appeal 2011-000475 Application 10/518,701 6 can be used to express polypeptides, with antibodies specific for the IgE constructs being used for affinity purification of the expressed polypeptide. (Id.) The Examiner found that Rutter disclosed that using linkers comprising proteolytic cleavage sites is desirable in the manufacture of fusion constructs since said linkers allow for the efficient incorporation and removal of desired functional properties. (Id.) According to the Examiner, it would have been obvious to a person of ordinary skill in the art at the time the invention was made to have modified the nucleic acid constructs of Chen to comprise tetanus toxoid T helper cell epitopes so they could be used in nucleic acid vaccines that would be effective in a majority of individuals in populations comprising diverse MHC haplotypes. (Id.) The Examiner reasoned that using vaccines comprising nucleic acid molecules was well known and routine in the art, as disclosed by Wang, and that such vaccines could be propagated in bacterial host cells, as disclosed by Hollis. (Id.) The Examiner further reasoned that a person of ordinary skill would have been motivated to incorporate proteolytic cleavage sequence linkers into such constructs because (a) Wang taught that separation of epitopes provides the advantages of reduced unwanted secondary structure and provides increases flexibility, and (b) Rutter taught that proteolytic cleavage sequence linkers in particular allow component epitopes to be easily separated without excessive proteolytic degradation. (Id. at 6-7.) Appellants assert that Chen and Wang teach away from using a proteolytic cleavage sequence as a linker. (App. Br. 13.) Specifically, Appellants assert that Chen teaches that “in human use one would expect Appeal 2011-000475 Application 10/518,701 7 that there would be „no inhibition of IgE responses to unrelated, unconjugated antigens.‟” (Id. at 15.) According to Appellants, this disclosure teaches away from using a proteolytic cleavage sequence because, when introduced into physiological conditions, doing so would lead to cleavage by a protease resulting in an unrelated, unconjugated composition, which Chen taught would undesirably result in no inhibition of IgE responses. (Id.) As for Wang, Appellants assert that the reference discloses the use of a spacer between its components and states that the two components are “„adjacent to either the N- or C-terminus of IgE-CH3 domain antigen sequences, in order to evoke efficient antibody responses.‟” (Id.) According to Appellants, Wang teaches away from using a proteolytic cleavage sequence because doing so would separate the epitopes such that they would not be considered adjacent to one another, as required by Wang. Additionally, Appellants assert that upon cleavage, “the epitopes would no longer be physically connected through any linker let alone considered adjacent to one another.” (Id. at 15-16.) In the Response to Argument, the Examiner explains that Rutter contemplated using enzymes that are not proteins expressed in IgE- producing animals, such as Apergillopeptidase B, such that a fusion polypeptide comprising a proteolytic sequence recognized by Aspergillopeptidase B would not be subject to cleavage under physiologic conditions. (Ans. 21.) Therefore, taken in combination, the use of a proteolytic sequence recognized by, for example, Aspergillopeptidase B to link the components suggested by Chen and Wang, satisfies the requirements and functionality suggested by Chen and Wang as well as Appeal 2011-000475 Application 10/518,701 8 Rutter. Accordingly, we agree with the Examiner in that Appellants‟ basis for asserting that Chen and Wang teach away from including a proteolytic cleavage sequence lacks evidentiary support. We recognize, but are not persuaded by, Appellants‟ contention that paragraph 35 of their Specification requires the claims to be interpreted to mean that “[t]he proteolytic cleavage site is provided in the claimed invention as a functional element intended to allow for the separation of the membrane IgE epitope from the non IgE helper T cell epitope in vivo as an alternative to provid[ing] two separate genes or proteins” (Reply Br. 6-7). Notwithstanding Appellants‟ contention to the contrary, paragraph 35 of the Specification discloses that the composition may comprise (a) a non IgE helper T cell epitope and (b) a membrane IgE epitope as (i) separate entities or (ii) a fusion protein. After considering all the evidence and arguments, we conclude that the record supports a conclusion of prima facie obviousness as set forth by the Examiner. In particular, we agree with the Examiner that Appellants have not provided evidentiary support for asserting that Chen and Wang taught away from using a proteolytic cleavage sequence, e.g., one that is not subject to cleavage in physiologic conditions. The Examiner‟s position is based upon sound reasoning which is supported by the evidence of record. Accordingly, we affirm the rejection of claims 1-3, 5-7, 22-24, and 26-29 over Chen, Wang, Hollis, and Rutter. B. The Rejection over Klysner ‘038, Wang, and Rutter. The Examiner found that Klysner „038 disclosed nucleic acid molecules comprising the membrane anchoring region of B-cell bound IgE linked to a foreign T helper epitope, which was disclosed as coming from Appeal 2011-000475 Application 10/518,701 9 tetanus toxoid. (Ans. 7.) The Examiner also found that Klysner „038 disclosed that the nucleic acids are present in plasmids and viral vectors for use in vaccines comprising excipients. (Id.) The Examiner found that Klysner „038 differed from the claimed invention in that it does not disclose the use of linkers comprising a proteolytic cleavage sequence between the epitopes. (Id.) The Examiner relied on Wang and Rutter, as discussed in the rejection over Chen, Wang, Hollis and Rutter. (Ans. 7-8.) According to the Examiner, it would have been obvious to a person of ordinary skill in the art at the time the invention was made to have modified the nucleic acid construct of Klysner „038 to comprise proteolytic cleavage sequence linkers since separation of epitopes provides the advantages of reduced unwanted secondary structure and increased flexibility as disclosed by Wang and provides the advantage of allowing the component epitopes to be easily separated without excessive proteolytic degradation as disclosed by Rutter. (Id. at 8.) Appellants contend that Klysner „038 and Wang teach away from using a proteolytic cleavage sequence. (App. Br. 17.) Specifically, Appellants assert that Klysner „038 teaches that the epitopes of IgE and the helper T cell should be simultaneously presented to the antigen presenting cells. (Id.) According to Appellants, “inclusion of a proteolytic cleavage sequence that allows the epitopes to be separated would function to eliminate the likelihood of simultaneous presentation of the epitopes by the antigen presenting cells.” (Id.) Appellants assert that Wang teaches away from using a proteolytic cleavage sequence as discussed above. (Id.) Appeal 2011-000475 Application 10/518,701 10 We disagree with Appellants that Klysner „038 and Wang taught away from using a proteolytic cleavage sequence as a linker in the Klysner „038 nucleic acid construct for the reasons set forth by the Examiner in the Response to Argument, as discussed above. Accordingly, we affirm the rejection of claims 1-3, 5-7, 22-24, and 26-29 over Klysner „038, Wang, and Rutter. C. The Rejection over Klysner ‘673, Wang, and Rutter. The Examiner found that Klysner „673 disclosed nucleic acid molecules comprising the membrane anchoring region of B-cell bound IgE linked to a foreign T helper epitope, which was disclosed as coming from tetanus toxoid. (Ans. 9.) The Examiner also found that Klysner „673 disclosed that the nucleic acids are present in plasmids and viral vectors for use in vaccines comprising excipients. (Id.) The Examiner found that Klysner „673 differed from the claimed invention in that it does not disclose the use of linkers comprising a proteolytic cleavage sequence between the epitopes. (Id.) The Examiner relied on Wang and Rutter, as discussed in the rejection over Chen, Wang, Hollis and Rutter. (Ans. 9-10.) According to the Examiner, it would have been obvious to a person of ordinary skill in the art at the time the invention was made to have modified the nucleic acid construct of Klysner „673 to “comprise proteolytic cleavage sequence linkers since separation of epitopes provides the advantages of reduced unwanted secondary structure and increased flexibility as disclosed by Wang et al. and provides the advantage of allowing the component epitopes to be easily separated without excessive proteolytic degradation as disclosed by Rutter.” (Id. at 10.) Appeal 2011-000475 Application 10/518,701 11 Appellants contend that Klysner „673 and Wang teach away from using a proteolytic cleavage sequence. (App. Br. 18.) Specifically, Appellants assert that Klysner „673 teaches that the epitopes of IgE and the helper T cell should be simultaneously presented to the antigen presenting cells. (Id.) According to Appellants, “inclusion of a proteolytic cleavage sequence that allows the epitopes to be separated would function to eliminate the likelihood of simultaneous presentation of the epitopes by the antigen presenting cells.” (Id.) Appellants assert that Wang teaches away from using a proteolytic cleavage sequence as discussed above. (Id.) We disagree with Appellants that Klysner „673 and Wang taught away from using a proteolytic cleavage sequence as a linker in the Klysner „673 nucleic acid construct for the reasons set forth by the Examiner in the Response to Argument, as discussed above. Accordingly, we affirm the rejection of claims 1-3, 5-7, 22-24, and 26-29 over Klysner „673, Wang, and Rutter. D.- H. The Rejections over Combinations including Walls, as evidenced by Janeway. The issue relating to each of the rejections D.-H. over combinations including Walls, as evidenced by Janeway is the same. Therefore, we consider these rejections together. The vaccine composition of Appellants‟ claim 8 comprises a nucleic acid molecule that encodes a protein. (App. Br. 38, Claims App‟x.) The encoded protein comprises (a) an IgE leader sequence and (b) at least one epitope of membrane IgE (id.). Claim 8 also requires a pharmaceutically acceptable carrier or diluent and that the composition is free of epitopes of serum IgE (id.). Appeal 2011-000475 Application 10/518,701 12 The Examiner found that none of Chen, Wang, Hollis, Rutter, Klysner „038, and Klysner „673 specified that the leader sequence used in such constructs is “an IgE leader sequence.” (Ans. 11-18.) However, the Examiner found that Walls disclosed vectors comprising an Ig leader sequence comprising an intron which was known to be essential for the efficient expression of Ig genes. (Id. at 11.) According to the Examiner, it would have been obvious to a person of ordinary skill in the art at the time the invention was made to make recombinant constructs, vectors and host cells comprising an Ig leader sequence disclosed by Walls because it encodes an intron which is essential for efficient expression of Ig constructs. (Id.) Further, the Examiner found that Janeway provided evidence that the variable domains of Ig genes are assembled via the process of V(D)J recombination, and that different isotypes, i.e., IgG, IgE, IgA, are obtained by isotype switching. (Id. at 12.) The Examiner found that the Ig heavy chain leader sequence is upstream of the rearranged variable domain, thus an “IgE leader sequence” is the same as an IgM, IgD, IgG and IgA leader sequence because the constant domain exons are not expressed without being joined to an already rearranged variable domain. (Id.) Therefore, the Examiner reasoned that the Ig leader of Walls satisfies the claim recitation of an IgE leader sequence. (Id.) Appellants do not contend that a skilled artisan would not have been motivated to combine the teachings of the prior art, as set forth by the Examiner. Rather, Appellants assert that the Examiner “has failed to show that the combination yields a nucleic acid sequence with an IgE leader sequence or a nucleic acid sequence that encodes a protein comprising an Appeal 2011-000475 Application 10/518,701 13 IgE leader sequence.” (App. Br. 20.) According to Appellants, “not all leader sequences are the same.” (Id.) In support of this contention, Appellants submit the declaration of Dr. David B. Weiner, 12 a co-inventor. (Id.) While we recognize Dr. Weiner‟s expertise in the field of pathology and laboratory medicine (see Dec. ¶ 2) we do not assign his declaration persuasive weight. In the declaration, Dr. Weiner provides a list of Ig leader sequences from IgE variable, IgA constant, IgA variable 1, IgA variable 2, IgA variable 3, IgG constant, IgM variable and IgM VH1, wherein the differences in the sequences are highlighted. (Id. at ¶ 3.) According to Dr. Weiner, “[t]he alignments show that IgE leader sequence is not the same as the leader sequences from the different isotypes.” (Id.) However, for the reasons set forth by the Examiner (Ans. 25-27), to which Appellants do not respond (see Reply Br. 6-8), we do not find that Dr. Weiner‟s declaration provides evidence that the “IgE leader sequence” of the claimed invention differed from the Ig leader sequence disclosed by Walls. Accordingly, we affirm the rejections of claim 8 over combinations including Walls, as evidenced by Janeway. Claims 32-37, 50, and 58-73 have not been argued separately and therefore fall with claim 8. 37 C.F.R. § 41.37(c)(1)(vii). I. New Ground of Rejection In the Answer, the Examiner states that “[c]laims 1-3, 5-8, 22-24, 26- 29, 32-37, and 50-73 are rejected in this application.” (Ans. 2.) However, none of the rejections includes independent claim 51 or its dependent claims 12 Declaration of Dr. David B. Weiner, submitted Mar. 20, 2009. Appeal 2011-000475 Application 10/518,701 14 52-57. These claims are directed to isolated nucleic acid molecules that encode proteins comprising the same elements as the nucleic acid molecules comprised in the vaccine compositions of independent claim 8 and its dependent claims. Therefore, we conclude that claims 51-57 are would have been obvious to a person of ordinary skill in the art at the time the invention was made over the combined prior art for the same reasons discussed by the Examiner in the rejections of claim 8 and its dependent claims. (See Rejections D. – H.) Accordingly, we enter the following new ground of rejection: Claim 51-57 are rejected under 35 U.S.C. § 103(a) as being unpatentable over Chen, Wang, Hollis, Rutter, and Walls, as evidenced by Janeway; over Klysner „038. Wang, Rutter, and Walls, as evidenced by Janeway; and over Klysner „673,Wang, Rutter, and Walls, as evidenced by Janeway. SUMMARY We affirm each of the Examiner‟s obviousness rejections. A new ground of rejection under 35 U.S.C. § 103(a) as unpatentable over Chen, Wang, Hollis, Rutter, and Walls, as evidenced by Janeway is ENTERED for claims 51-57. A new ground of rejection under 35 U.S.C. § 103(a) as unpatentable over Klysner „038, Wang, Hollis, Rutter, and Walls, as evidenced by Janeway is ENTERED for claims 51-57. A new ground of rejection under 35 U.S.C. § 103(a) as unpatentable over Klysner „673, Wang, Rutter, and Walls, as evidenced by Janeway is ENTERED for claims 51-57. 37 C.F.R. § 41.50(b) Appeal 2011-000475 Application 10/518,701 15 Regarding the affirmed rejections, 37 C.F.R. § 41.52(a)(1) provides “[a]ppellant may file a single request for rehearing within two months from the date of the original decision of the Board.” In addition to affirming the examiner's rejection(s) of one or more claims, this opinion contains a new ground of rejection pursuant to 37 C.F.R. § 41.50(b) (effective September 13, 2004, 69 Fed. Reg. 49960 (August 12, 2004), 1286 Off. Gaz. Pat. Office 21 (September 7, 2004)). 37 CFR § 41.50(b) provides “[a] new ground of rejection pursuant to this paragraph shall not be considered final for judicial review.” 37 C.F.R. § 41.50(b) also provides that the appellant, WITHIN TWO MONTHS FROM THE DATE OF THE DECISION, must exercise one of the following two options with respect to the new ground of rejection to avoid termination of the appeal as to the rejected claims: (1) Reopen prosecution. Submit an appropriate amendment of the claims so rejected or new evidence relating to the claims so rejected, or both, and have the matter reconsidered by the examiner, in which event the proceeding will be remanded to the examiner.… (2) Request rehearing. Request that the proceeding be reheard under § 41.52 by the Board upon the same record.… Should the appellant elect to prosecute further before the examiner pursuant to 37 C.F.R. § 41.50(b)(1), in order to preserve the right to seek review under 35 U.S.C. §§ 141 or 145 with respect to the affirmed rejection, the effective date of the affirmance is deferred until conclusion of the prosecution before the examiner unless, as a mere incident to the limited prosecution, the affirmed rejection is overcome. Appeal 2011-000475 Application 10/518,701 16 If the appellant elects prosecution before the examiner and this does not result in allowance of the application, abandonment or a second appeal, this case should be returned to the Patent Trial and Appeal Board for final action on the affirmed rejection, including any timely request for rehearing thereof. AFFIRMED; 37 C.F.R. § 41.50(b) cdc Copy with citationCopy as parenthetical citation