DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
1. Claims 1-46 as filed on August 21, 2023 are pending and under consideration.
Specification
2. The disclosure is objected to because of the following informalities: The current application was filed after July 1, 2022, thus the WIPO Standard ST.26, Sequence Listing in XML format, applies to sequence disclosures. See 37 CFR § 1.831. An ST.26 Sequence Listing in XML must not include any sequences having fewer than 10 specifically defined nucleotides, or fewer than 4 specifically defined amino acids. See 37 CFR § 1.831(j).
Table 5 contains a protein sequence of three amino acids in length associated with SEQ ID NO: 14 (AAS) and a nucleotide sequence of nine nucleotides associated with SEQ ID NO: 13 (gctgcatcc). These sequences are replaced with “000” in the Sequence Listing in XML because the sequences are less than 4 amino acid sequences in length or fewer than 10 specifically defined nucleotides. The SEQ ID NOs in the specification at Table 5 associated with AAS and gctgcatcc, and anywhere else in the specification, should be deleted because the Sequence Listing in XML does not contain the short sequences.
Appropriate correction is required.
Claim Objections
3. Claims 2, 8, 13, 22, 23, 30, 32, 34, and 36 are objected to because of the following informalities:
Claims 2, 8, 13, 22, 23, 30, 32, 34, and 36 recite SEQ ID NO: 13 which represents (gctgcatcc) and SEQ ID NO: 14 which represents (AAS). These sequences are replaced with “000” in the Sequence Listing in XML because the sequences are less than 4 amino acid sequences in length or fewer than 10 specifically defined nucleotide . See 37 CFR § 1.831(j). SEQ ID NO: 13 should be deleted and replaced with gctgcatcc. SEQ ID NO: 14 should be deleted and replaced with AAS. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
4. Claims 21 and 22 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of producing an anti-influenza B HA antibody or antigen-binding fragment thereof, the method comprising growing a host cell under conditions permitting production of the antibody or antigen-binding fragment thereof, wherein the host cell comprises an expression vector comprising: an isolated polynucleotide molecule comprising a polynucleotide sequence that encodes a heavy chain variable region (HCVR) of an antibody that binds specifically to influenza B hemagglutinin (HA), wherein the HCVR comprises a heavy chain complementarity determining region (HCDR1) comprising SEQ ID NO: 4, a heavy chain complementarity determining region 2 (HCDR2) comprising SEQ ID NO: 6, and a heavy chain complementarity determining region 3 (HCDR3) comprising SEQ ID NO: 8 and an expression vector comprising: an isolated polynucleotide molecule comprising a polynucleotide sequence that encodes a light chain variable region (LCVR) of an antibody that binds specifically to influenza B hemagglutinin (HA), wherein the LCVR comprises a light chain complementarity determining region (LCDR1) comprising SEQ ID NO: 12, a light chain complementarity determining region 2 (LCDR2) comprising SEQ ID NO: 14, and a light chain complementarity determining region 3 (LCDR3) comprising SEQ ID NO: 16, does not reasonably provide enablement for the methods of claims 21 and 22. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
The factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). The court in Wands states: "Whether undue experimentation is needed is not a single, simple factual determination, but rather is a conclusion reached by weighing many factual considerations." (Wands, 8 USPQ2d 1404). The factors to be considered in determining whether undue experimentation is required include: (1) the quantity of experimentation necessary, (2) the amount or direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims.
The claims are drawn to:
21. A method of producing an anti-influenza B HA antibody or antigen-binding fragment thereof, the method comprising growing a host cell under conditions permitting production of the antibody or antigen-binding fragment thereof, wherein the host cell comprises an expression vector comprising: an isolated polynucleotide molecule comprising a polynucleotide sequence that encodes a heavy chain variable region (HCVR) of an antibody that binds specifically to influenza B hemagglutinin (HA), wherein the HCVR comprises a heavy chain complementarity determining region (HCDR1) comprising SEQ ID NO: 4, a heavy chain complementarity determining region 2 (HCDR2) comprising SEQ ID NO: 6, and a heavy chain complementarity determining region 3 (HCDR3) comprising SEQ ID NO: 8;
22. A method of producing an anti-influenza B HA antibody or antigen-binding fragment thereof, the method comprising growing a host cell under conditions permitting production of the antibody or antigen-binding fragment thereof, wherein the host cell comprises an expression vector comprising: an isolated polynucleotide molecule comprising a polynucleotide sequence that encodes a light chain variable region (LCVR) of an antibody that binds specifically to influenza B hemagglutinin (HA), wherein the LCVR comprises a light chain complementarity determining region (LCDR1) comprising SEQ ID NO: 12, a light chain complementarity determining region 2 (LCDR2) comprising SEQ ID NO: 14, and a light chain complementarity determining region 3 (LCDR3) comprising SEQ ID NO: 16.
Thus, the claims are drawn to producing an anti-influenza B HA antibody or antigen-binding fragment thereof by only expressing the claimed HCVR or LCVR.
The specification teaches producing the anti-HA antibody mAB35490 comprising the HCVR of SEQ ID NO: 2 and the LCVR of SQ ID NO: 10 . See Examples 1-3 and Tables 1-2.
It was well-known in the antibody art that antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. See Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (see Section 3) “Antibody Structure and the Antigen Binding Site” and Figure 1).
Thus, given that binding of an antigen generally requires the pairing of both the heavy and light variable regions that are specific for a particular antigen, e.g. the HA antigen, one of skill in the art could not predictably make and use a host cell expressing only the LCVR or only the HCVR of the anti-HA antibody mAB35490 to produce an anti-influenza B HA antibody. Thus, one of skill in the art could not predictably make and use the methods of claims 21 and 22 as claimed to produce an anti-influenza B HA antibody without undue experimentation.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
5. Claim(s) 2, 7-10, 12, 15, 19, 20, 22, 25, 27, and 30-33 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by US 2016/0176953 A1 (Ngambo et al. June 23, 2016), “Ngambo”.
Ngambo teaches monoclonal antibodies, or antigen-binding fragments thereof, that bind to the influenza hemagglutinin (HA) protein. See abstract and ¶¶ 0012-0014.
Ngambo teaches a LCVR of SEQ ID NO: 66, which is part of antibody that binds HA, (H1H11829N2). See ¶¶ 0046, 0048, and 0049 and Example 2-Table 1.
SEQ ID NO: 66 comprises the claimed protein sequences of SEQ ID NOs: 10, 12, 14, and 16. See Appendix.
Ngambo teaches the nucleic acid sequence SEQ ID NO: 65 encoding the LCVR of SEQ ID NO: 66, which is part of antibody that binds HA, (H1H11829N2). See Example 2-Table 2.
SEQ ID NO: 65 comprises the claimed protein sequences of SEQ ID NOs: 9, 11, 13, and 15. See Appendix.
Although Ngambo does not teach an antibody comprising LCVR of SEQ ID NO: 66, binds to influenza B HA, the claims only require a polynucleotide encoding LCVR. Additionally, the LCVR of SEQ ID NO: 66 has the same structure as claimed and thus would have the same function.
Ngambo teaches expression vectors for expressing the antibodies in host cells for production and recovery of the antibodies. See ¶¶ 0086-0087 and claims 1 and 22-24.
Ngambo teaches expressing the antibodies in isolated mammalian and CHO cells. See ¶¶ 0111 and 0155.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
5. Claims 1-46 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 11,773,156 (Baum et al. Oct. 3, 2023, IDS) in view of US 2016/0176953 (Ngambo et al. June 23, 2016), “Ngambo”.
The ‘156 claims are drawn to:
1. An isolated recombinant antibody or antigen-binding fragment thereof that specifically binds to influenza B hemagglutinin (HA), wherein the antibody comprises (i) three heavy chain complementarity determining regions (CDRs) (HCDR1, HCDR2, and HCDR3) contained within a heavy chain variable region (HCVR) comprising the amino acid sequence set forth in SEQ ID NO: 2; and (ii) three light chain CDRs (LCDR1, LCDR2, and LCDR3) contained within a light chain variable region (LCVR) comprising the amino acid sequence set forth in SEQ ID NO: 10.
2. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising an HCVR having an amino acid sequence of SEQ ID NO: 2.
3. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising an LCVR having an amino acid sequence of SEQ ID NO: 10.
4. An isolated antibody or antigen-binding fragment thereof, comprising: (a) an HCDR1 domain having an amino acid sequence of SEQ ID NO: 4; (b) an HCDR2 domain having an amino acid sequence of SEQ ID NO: 6; (c) an HCDR3 domain having an amino acid sequence of SEQ ID NO: 8; (d) an LCDR1 domain having an amino acid sequence of SEQ ID NO: 12; (e) an LCDR2 domain having an amino acid sequence of SEQ ID NO: 14; and (f) an LCDR3 domain having an amino acid sequence of SEQ ID NO: 16.
5. The isolated antibody or antigen-binding fragment thereof of claim 4, wherein said isolated antibody or antigen-binding fragment thereof specifically binds to influenza B hemagglutinin (HA).
6. The isolated antibody or antigen-binding fragment thereof of claim 4, which is an antibody comprising an HCVR having an amino acid sequence of SEQ ID NO: 2.
7. The isolated antibody or antigen-binding fragment thereof of claim 4, which is an antibody comprising an LCVR having an amino acid sequence of SEQ ID NO: 10.
8. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising an HCVR/LCVR amino acid sequence pair of SEQ ID NOs: 2/10.
9. The isolated antibody or antigen-binding fragment thereof of claim 1 which is an IgG1 antibody.
10. The isolated antibody or antigen-binding fragment thereof of claim 1 which is an IgG4 antibody.
11. The isolated antibody or antigen-binding fragment thereof of claim 1 which is a bispecific antibody.
12. A pharmaceutical composition comprising the isolated antibody or antigen-binding fragment thereof of claim 1 and a pharmaceutically acceptable carrier or diluent.
13. The pharmaceutical composition of claim 12, wherein said pharmaceutical composition further comprises a second therapeutic agent.
14. The pharmaceutical composition of claim 13, wherein said second therapeutic agent is selected from the group consisting of: an anti-viral drug, an anti-inflammatory drug, a different antibody that binds specifically to influenza HA, a vaccine for influenza, a dietary supplement, and another palliative therapy to treat an influenza infection.
15. The pharmaceutical composition of claim 14, wherein said anti-inflammatory drug is selected from the group consisting of corticosteroids and non-steroidal anti-inflammatory drugs.
16. The pharmaceutical composition of claim 14, wherein said dietary supplement is an anti-oxidant.
17. The pharmaceutical composition of claim 14, wherein said anti-viral drug is oseltamivir.
18. The pharmaceutical composition of claim 14, wherein said anti-viral drug is an anti-influenza A drug.
19. The pharmaceutical composition of claim 18, wherein said anti-influenza A drug is an antibody.
20. The pharmaceutical composition of claim 19, wherein said antibody binds specifically to influenza A HA.
21. The isolated antibody or antigen-binding fragment thereof of claim 1, wherein said antibody or fragment has one or more of the following characteristics: (a) binds to influenza B HA with an EC50 of less than about 10−9 M; and (b) demonstrates an increase in survival in an influenza B-infected animal after administration to said influenza B-infected animal, as compared to a comparable influenza B-infected animal without said administration.
The ‘156 patent is the parent to the instant application; thus all of the antibody SEQ ID NO sequences are the same the claimed sequences.
The ‘156 claims teach as set forth above, but do not teach polynucleotides encoding the anti-HA antibody or methods of antibody production.
Ngambo teaches as set forth above.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘156 claims and Ngambo and isolate nucleic acids encoding the claimed anti-HA antibodies so that the nucleic acids could be inserted into expression vectors for expression, production and use of the anti-HA antibodies as taught by Ngambo. One would have been motivated to isolate nucleic acids encoding the claimed anti-HA antibodies as this was routine in the art for the production and use of antibodies as taught by Ngambo.
Additionally, it is noted that the courts have found that the disclosure of the polypeptide makes the nucleic acid encoding the protein obvious as the methods of obtaining the nucleic acids are routine in the art and can be obtained with a reasonable expectation of success. See MPEP 2143(E)(Example 3), Ex parte Kubin, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007), and In re Kubin 90 USPQ2d 1417 (U. S. Court of Appeals Fed. Cir. 2009).
6. Claims 2, 7-10, 12, 15, 19, 20, 22, 25, 27, and 30-33 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of U.S. Patent No. 10,689,436 B2 (Purcell et al. June 23, 2020) in view of US 2016/0176953 (Ngambo et al. June 23, 2016), “Ngambo”.
The ‘436 claims are drawn to:
1. An isolated antibody or antigen-binding fragment thereof, comprising three heavy chain complementarity determining regions (CDRs) (HCDR1, HCDR2 and HCDR3) contained within a heavy chain variable region (HCVR) comprising the amino acid sequence set forth in SEQ ID NO: 50; and three light chain complementarity determining regions (CDRs) (LCDR1, LCDR2 and LCDR3) contained within a light chain variable region (LCVR) comprising the amino acid sequence set forth in SEQ ID NO: 66.
2. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising a HCVR that comprises an amino acid sequence set forth in SEQ ID NO: 50.
3. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising a LCVR that comprises an amino acid sequence set forth in SEQ ID NO: 66.
4. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising a HCVR that comprises an amino acid sequence set forth in SEQ ID NO: 50; and a LCVR that comprises an amino acid sequence set forth in SEQ ID NO: 66.
14. A polynucleotide molecule comprising a polynucleotide sequence that encodes a HCVR, or an LVCR, or both, of the isolated antibody of claim 5.
15. A vector comprising the polynucleotide molecule of claim 14.
16. An isolated cell comprising the vector of claim 15.
SEQ ID NO: 66 comprises the claimed protein sequences of SEQ ID NOs: 10, 12, 14, and 16. See Appendix, the ‘436 patent is a continuation of Ngambo.
The ‘436 claims teach as set forth above, but do not teach methods of antibody production with polynucleotides encoding the antibody LCVR.
Ngambo teaches as set forth above.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘436 claims and Ngambo and isolate nucleic acids encoding the claimed anti-HA antibodies so that the nucleic acids could be inserted into expression vectors for expression, production and use of the anti-HA antibodies as taught by Ngambo. One would have been motivated to isolate nucleic acids encoding the claimed anti-HA antibodies as this was routine in the art for the production and use of antibodies as taught by Ngambo.
Additionally, it is noted that the courts have found that the disclosure of the polypeptide makes the nucleic acid encoding the protein obvious as the methods of obtaining the nucleic acids are routine in the art and can be obtained with a reasonable expectation of success. See MPEP 2143(E)(Example 3), Ex parte Kubin, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007), and In re Kubin 90 USPQ2d 1417 (U. S. Court of Appeals Fed. Cir. 2009).
7. Claims 2, 7-10, 12, 15, 19, 20, 22, 25, 27, and 30-33 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, 5, 7-12, 19-35 of U.S. Patent No. 11,453,714 B2 (Purcell et al. Sep. 27, 2022) in view of US 2016/0176953 (Ngambo et al. June 23, 2016), “Ngambo”.
The ‘714 claims are drawn in part to:
1. An isolated antibody or antigen-binding fragment thereof that specifically binds to influenza A hemagglutinin (HA), comprising: (a) a heavy chain complementarity determining region 1 (HCDR1) comprising the amino acid sequence of SEQ ID NO: 20 with no more than one amino acid substitution; an HCDR2 comprising the amino acid sequence of SEQ ID NO: 22 with no more than one amino acid substitution; an HCDR3 comprising the amino acid sequence of SEQ ID NO: 24 with no more than one amino acid substitution; a light chain complementarity determining region 1 (LCDR1) comprising the amino acid sequence of SEQ ID NO: 28 with no more than one amino acid substitution; an LCDR2 comprising the amino acid sequence of SEQ ID NO: 30 with no more than one amino acid substitution; and an LCDR3 comprising the amino acid sequence of SEQ ID NO: 32 with no more than one amino acid substitution; or (b) an HCDR1 comprising the amino acid sequence of SEQ ID NO: 52 with no more than one amino acid substitution; an HCDR2 comprising the amino acid sequence of SEQ ID NO: 54 with no more than one amino acid substitution; an HCDR3 comprising the amino acid sequence of SEQ ID NO: 56 with no more than one amino acid substitution; an LCDR1 comprising the amino acid sequence of SEQ ID NO: 68 with no more than one amino acid substitution; an LCDR2 comprising the amino acid sequence of SEQ ID NO: 70 with no more than one amino acid substitution; and an LCDR3 comprising the amino acid sequence of SEQ ID NO: 72 with no more than one amino acid substitution.
5. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising an LCVR having an amino acid sequence of SEQ ID NO: 66.
7. The isolated antibody or antigen-binding fragment thereof of claim 1, comprising an HCVR having an amino acid sequence of SEQ ID NO: 50 with no more than one amino acid substitution and an LCVR having an amino acid sequence of SEQ ID NO: 66 with no more than one amino acid substitution.
8. The isolated antibody of claim 1, wherein the antibody prevents attachment to and/or entry of influenza virus into a host cell.
9. A pharmaceutical composition comprising an isolated antibody or antigen-binding fragment thereof that binds to influenza HA according to claim 1 and a pharmaceutically acceptable carrier or diluent.
10. An isolated polynucleotide molecule comprising a polynucleotide sequence that encodes an HCVR or an LVCR of an antibody as set forth in claim 1.
11. A vector comprising the polynucleotide of claim 10.
12. An isolated cell expressing the vector of claim 11.
SEQ ID NO: 66 comprises the claimed protein sequences of SEQ ID NOs: 10, 12, 14, and 16. See Appendix, the ‘714 patent is a continuation of Ngambo.
The ‘714 claims teach as set forth above, but do not teach methods of antibody production with polynucleotides encoding the antibody LCVR.
Ngambo teaches as set forth above.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘714 claims and Ngambo and isolate nucleic acids encoding the claimed anti-HA antibodies so that the nucleic acids could be inserted into expression vectors for expression, production and use of the anti-HA antibodies as taught by Ngambo. One would have been motivated to isolate nucleic acids encoding the claimed anti-HA antibodies as this was routine in the art for the production and use of antibodies as taught by Ngambo.
Additionally, it is noted that the courts have found that the disclosure of the polypeptide makes the nucleic acid encoding the protein obvious as the methods of obtaining the nucleic acids are routine in the art and can be obtained with a reasonable expectation of success. See MPEP 2143(E)(Example 3), Ex parte Kubin, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007), and In re Kubin 90 USPQ2d 1417 (U. S. Court of Appeals Fed. Cir. 2009).
Conclusion
8. No claims allowed.
9. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Janet L Epps-Smith can be reached at 571-272-0757. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PETER J REDDIG/ Primary Examiner, Art Unit 1646
APPENDIX
Alignment of SEQ ID NOs: 12, 14 and 16 with SEQ ID NO: 66 of Ngambo
ALIGNMENT:
Query Match 72.8%; Score 67.7; Length 108;
Best Local Similarity 26.4%;
Matches 19; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 QSISS-----------------YAAS---------------------------------- 9
||||| ||||
Db 27 QSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATY 86
Qy 10 --QQSYSTPPIT 19
||||||||||
Db 87 YCQQSYSTPPIT 98
Alignment of SEQ ID NO: 10 with SEQ ID NO: 66 of Ngambo
ALIGNMENT:
Query Match 100.0%; Score 553; Length 108;
Best Local Similarity 100.0%;
Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPS 60
Qy 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPITFGQGTRLEIK 108
||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPITFGQGTRLEIK 108
Alignment of SEQ ID NO: 9 with SEQ ID NO: 65 of Ngambo
ALIGNMENT:
Query Match 100.0%; Score 324; Length 324;
Best Local Similarity 100.0%;
Matches 324; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GACATCCAGATGACCCAGTCTCCATCCTCCCTGTCTGCATCTGTAGGAGACAGAGTCACC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 GACATCCAGATGACCCAGTCTCCATCCTCCCTGTCTGCATCTGTAGGAGACAGAGTCACC 60
Qy 61 ATCACTTGCCGGGCAAGTCAGAGCATTAGCAGCTATTTAAATTGGTATCAGCAGAAACCA 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ATCACTTGCCGGGCAAGTCAGAGCATTAGCAGCTATTTAAATTGGTATCAGCAGAAACCA 120
Qy 121 GGGAAAGCCCCTAAGCTCCTGATCTATGCTGCATCCAGTTTGCAAAGTGGGGTCCCGTCA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGGAAAGCCCCTAAGCTCCTGATCTATGCTGCATCCAGTTTGCAAAGTGGGGTCCCGTCA 180
Qy 181 AGGTTCAGTGGCAGTGGATCTGGGACAGATTTCACTCTCACCATCAGCAGTCTGCAACCT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AGGTTCAGTGGCAGTGGATCTGGGACAGATTTCACTCTCACCATCAGCAGTCTGCAACCT 240
Qy 241 GAAGATTTTGCAACTTACTACTGTCAACAGAGTTACAGTACCCCTCCGATCACCTTCGGC 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 GAAGATTTTGCAACTTACTACTGTCAACAGAGTTACAGTACCCCTCCGATCACCTTCGGC 300
Qy 301 CAAGGGACACGACTGGAGATTAAA 324
||||||||||||||||||||||||
Db 301 CAAGGGACACGACTGGAGATTAAA 324