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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 09/04/2025 has been entered.
Claims 1-3, 7, 8, 11, 12, 14, 15, 21-25, 40, 43-45, 47-49, 57-59, 61-64, 66, 67, 69, 70 are pending in the application. Claims 4-6, 9, 10, 13, 16-20, 26-39, 41, 42, 46, 50-56, 60, 65, 68, were canceled.
Claims 1-3, 7, 8, 11, 12, 14, 15, 21-25, 40, 43-45, 47-49, 57-59, 61-64, 66, 67, 69, 70 are currently under examination on the merits.
Information Disclosure Statement
The information disclosure statement (IDS) was submitted on 10/28/2021, 06/21/2023, 12/21/2023, 06/10/2024, 06/24/2024, 03/03/2025, 03/18/2025, and 09/04/2025. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-3, 7, 8, 11, 12, 14, 15, 21-24, 40, 43-44, 47-49, 57-59, 61-64, 66, 67, 69, 70 are rejected under 35 U.S.C. 103 as being unpatentable over Benjamin et al. in view of Kuo et al. Prior art of record.
See claims 1-3, 7, 8, 11, 12, 14, 15, 21-24, 40, 43-44, 47-49, 57-59, 61-64, 66, 67, 69, 70 as submitted on 09/04/2025.
Regarding claim 1, it is noted that the only amendment to claim 1 filed on 09/04/2025 recites the preamble “An IgG antibody”. Benjamin et al. already teach the antibody of claim 1 (also referred to as antibody MEDI8852 in instant Specification [page 3]) is a human IgG1 monoclonal antibody (¶ [0093]). As previously explained, the antibody of Benjamin et al.’s comprises identical CRDs as the claimed antibody of claim 1. Specifically Benjamin et al. teach the following:
a heavy chain comprising HCDR1, HCDR2, and HCDR3 sequences as set forth in SEQ ID NO: 113, SEQ ID NO: 114, and SEQ ID NO: 115, respectively (¶¶ [0109]; [111], [0141]; page 40); which have 100% identity to heavy chain sequences CDR1-3 set forth in SEQ ID NO: 1, SEQ ID NO: 2, and SEQ ID NO: 3 in instant application. (For SEQ ID NO:1 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-1.align450.rai; for SEQ ID NO:2 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-2.align450.rai; for SEQ ID NO:3 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-3.align450.rai)
a light chain comprising LCDR1, LCDR2, and LCDR3 sequences as set forth in SEQ ID NO: 118, SEQ ID NO: 119, and SEQ ID NO: 119, respectively (¶¶ [0109]; [111], [0141]; page 40); which have 100% identity to light chain sequences CDR1-3 set forth in SEQ ID NO: 4, SEQ ID NO: 5, and SEQ ID NO: 6 in instant application. (For SEQ ID NO:4 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-4.align450.rai; for SEQ ID NO:5 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-5.align450.rai; for SEQ ID NO:6 see Result 1, SCV Sequence Search Results 20240820_105758_us-17-607-383-6.align450.rai)
Benjamin et al. do not teach the antibody defined above wherein the heavy chain constant region comprises an M428L and a N434S mutation.
However, Kuo et al. teach a review the fundamental IgG therapeutic antibodies, including important Fc constant region mutations designed to modulate binding the interaction of IgG antibodies and the FcRn receptor (Abstract, page 1). Kuo et al. further teach common strategies in the art for modulating FcRn-IgG binding affinity and antibody half-life, including an M428L and a N434S mutations in the constant region of the heavy chain termed “LS” (Page 4, 5). Kuo et al. further teach that the introduction of an M428L and a N434S mutations in the constant region of the heavy chain results in improved binding for the neonatal Fc receptor (FcRn) as well as improved serum half-life of the antibody (page 6). Kuo et al.’s teachings demonstrate that improved binding for the neonatal Fc receptor and half-life extension of a therapeutic antibody helps maintain drug therapeutic serum levels and reduce the frequency of administration (page 5).
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Kuo et al. about the M428L and the N434S mutations in the constant region of the heavy chain of antibody 12 as taught by Benjamin et al., for the benefit of improving affinity or the FcRn as well as improving serum half-life of the antibody. One of ordinary skill in the art would have been motivated to introduce an M428L and a N434S mutations in the constant region of the heavy chain of antibody 12 as taught by Benjamin et al. given that improved binding for the neonatal Fc receptor and half-life extension of a therapeutic antibody helps maintain drug therapeutic serum levels and reduce the frequency of administration.
One of ordinary skill in the art would have had a reasonable expectation of success for introducing an M428L and a N434S mutations in the constant region of the heavy chain of antibody 12 as taught by Benjamin et al. given that the methods of antibody cloning and mutagenesis are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 2, as previously explained, Benjamin et al. further teach the antibody defined above binds to a hemagglutinin protein of an influenza A virus (¶¶ [0111], [0295]).
Regarding claim 3, as previously explained, Benjamin et al. further teach the antibody defined above wherein the antibody neutralizes infection with an influenza A virus (¶¶ [0007], [0163], [0298], Table 2).
Regarding claims 7 and 8, as previously explained, Benjamin et al. further teach the antibody defined above wherein the antibody neutralizes infection with an influenza A virus, wherein the virus comprises the polymorphism N146D of H1 HA (¶¶ [0302], [0304], Table 5), which includes influenza A virus subtype H1 A/California/7 /09 (H1 N1) per instant Specification (instant Specification page 12). Neutralization of Antibody 12 of influenza A virus subtype H1 A/California/7 /09 occurs with an IC50 fold change of 0.98 (< 2 as recited in claim 8) relative to the HA of a wild type virus (¶ [0299], Table 5).
Regarding claims 11, 12, 14, 15, as previously explained, Benjamin et al. further teach the antibody defined above wherein the antibody:
is a human antibody (¶¶ [0092], [0126], [0295], Table 2)
is a monoclonal antibody (¶¶ [0091], [0092], [0126], [0295])
is of the IgG type (¶ [0093])
is of the IgG1 type (¶ [0093])
has a kappa light chain for example, VKl-39 (¶ [0116], claim 9)
Regarding claims 21 and 22, as previously explained, Benjamin et al. further teach the antibody defined above wherein the antibody comprises:
a heavy chain variable region comprising an amino acid sequence set forth in SEQ ID NO: 112 which shares 100% sequence identity to SEQ ID NO:7 in instant application. See sequence alignment file: “US-17-607-383-7_pep__vs__US-15-026-276-112_pep__align.pdf” (file of record), (page 40).
a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO: 117 which shares 100% sequence identity to SEQ ID NO:8 in instant application. See sequence alignment file: “US-17-607-383-8_pep__vs__US-15-026-276-117_pep__align.pdf” (file of record) , (page 40).
Regarding claims 21 and 22, as previously explained, Benjamin et al. further teach the antibody defined above wherein the antibody comprises:
• a heavy chain variable region comprising an amino acid sequence set forth in SEQ ID NO: 112 which shares 100% sequence identity to SEQ ID NO:7 in instant application. See sequence alignment file: “US-17-607-383-7_pep__vs__US-15-026-276-112_pep__align.pdf” (file of record), (page 40).
• a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO: 117 which shares 100% sequence identity to SEQ ID NO:8 in instant application. See sequence alignment file: “US-17-607-383-8_pep__vs__US-15-026-276-117_pep__align.pdf” (file of record), (page 40).
Regarding claim 23, as previously explained, the teachings of Benjamin et al. and Kuo et al. described above teach the antibody defined above with a constant Fc region that does not comprise any further mutations other than M428L and N434S as explained above, therefore the teachings of Benjamin et al. and Kuo et al. in combination meet the limitations of claim 23.
Regarding claim 24, as explained above, Benjamin et al. and Kuo et al. teach the antibody defined above with a constant Fc region that does not comprise any further mutations other than M428L and N434S as explained above, therefore the teachings of Benjamin et al. and Kuo et al. in combination meet the limitations of claim 24.
Regarding claim 40, as previously explained, Benjamin et al. further teach a nucleic acid molecule comprising a polynucleotide encoding the antibody defined above (¶ [0096], claim 17).
Regarding claim 43, as previously explained, Benjamin et al. further teach nucleic acid sequences encoding part or all of the light and heavy chains and CDRs (the first nucleic acid molecule comprises a polynucleotide encoding the heavy chain of the antibody of claim 1; and the second nucleic acid molecule comprises a polynucleotide encoding the corresponding light chain of the same antibody, as recited in claim 43) (¶ [0096], claim 17).
Regarding claim 44, as explained above, Benjamin et al. teach nucleic acid sequences encoding the light and heavy chains as recited in claim 43. Benjamin et al. further teach the following nucleic acid molecules:
a heavy chain variable region SEQ ID NO: 111 encoding an amino acid sequence set forth in SEQ ID NO: 112 comprising the heavy chain CDRs of antibody 12. SEQ ID NO: 112 shares 100% sequence identity to SEQ ID NO:7 in instant application which comprises heavy chain CDR1-3, as explained above (Alignment file cited above) (page 40).
a light chain variable region SEQ ID NO: 116 encoding the amino acid sequence set forth in SEQ ID NO: 117 comprising the heavy chain CDRs of antibody 12. SEQ ID NO: 117 shares 100% sequence identity to SEQ ID NO:8 in instant application which comprises light chain CDR4-6, as explained above (Alignment file cited above) (page 40).
SEQ ID NO: 111 and SEQ ID NO: 116 in Benjamin et al.’s teachings do not share 100% identity to instant SEQ ID NO: 12 and SEQ ID NO: 13 respectively. However, the nucleic acid sequences in Benjamin et al.’s teachings SEQ ID NO: 111 and SEQ ID NO: 116 are equivalent to instant nucleic acids sequences SEQ ID NO: 12 and SEQ ID NO: 13 because they encode the same amino acid sequences. The translation and alignment files provided are as follows:
Regarding instant SEQ ID NO:12:
SEQ ID NO: 111 translation: “US-15026276-111 translate.pdf” (file of record)
Alignment of SEQ ID NO: 111 translation with instant SEQ ID NO:7: “US-17-607-383-7_pep__vs__US-15026276-111 translated_pep__align.pdf” (file of record)
Regarding instant SEQ ID NO:13:
SEQ ID NO: 116 translation: “US-15026276-116 translate.pdf” (file of record)
Alignment of SEQ ID NO: 116 translation with instant SEQ ID NO:8: “US-17-607-383-8_pep__vs__US-15026276-116 translated_pep__align.pdf” (file of record)
Benjamin et al. further teach the codon optimization of nucleic acid sequences to improve the efficiency of translation in expression systems (¶ [0088]). Therefore the sequences recited in claim 44 in instant application, SEQ ID NO: 12 and SEQ ID NO: 13, are obvious variants of the sequences taught by Benjamin et al.’s teachings SEQ ID NO: 111 and SEQ ID NO: 116.
Regarding claim 47, as previously explained, Benjamin et al. teach nucleic acid sequences encoding the light and heavy chains as recited in claim 43. Benjamin et al. further teach a vector comprising isolated nucleic acid sequences encoding the antibody sequences explained above (the combination of nucleic acid molecules of claim 43, as recited in claim 47) (¶ [0097]).
Regarding claim 48, as previously explained, Benjamin et al. further teach a host cell comprising isolated nucleic acid sequences encoding the antibody sequences explained above for expression (a cell expressing, as recited in claim 48) (¶¶ [0098], [0099]).
Regarding claim 49, as previously explained, Benjamin et al. further teach a composition comprising the antibody as explained above and a pharmaceutically acceptable carrier (¶¶ [0100], [0101]).
Regarding claim 57, as previously explained, Benjamin et al. further teach the combination of the antibody as explained above with one or more antiviral medications (¶ [0273]).
Regarding claims 58 and 59, as previously explained, Benjamin et al. further teach the combination of the antibody as explained above with neuraminidase inhibitors such as zanamivir (RELENZA®) (¶ [0273]).
Regarding claim 61, as previously explained, Benjamin et al. further teach a method of treating influenza A virus infection or delaying influenza A virus infection in a subject comprising administering to a subject in need thereof, a therapeutically effective amount of the antibody as explained above (¶¶ [0270], [0271]).
Regarding claim 62, as previously explained, Benjamin et al. further teach a method of claim 61 wherein the antibody is administered prophylactically (¶¶ [0312], [0195]).
Regarding claim 63, as previously explained, Benjamin et al. further teach a method of claim 61 wherein the antibody is administered prophylactically (¶¶ [0312], [0195]). Benjamin et al. and Kuo et al. in combination teach the antibody of claim 1 comprising the mutations M428L and N434S in the constant region of the heavy chain as explained above. Kuo et al. further teach that the mutations M428L and N434S extended the serum half-life of an antibody in cynomolgus monkey from 9.7 to 31 days, representing a 3.2-fold improvement, which is equivalent to serum half-life of 50 days in humans (page 2). Therefore, the a therapeutically effective (for treatment) dose of an antibody comprising the mutations M428L and N434S is 3.2-fold lower than that of a comparative antibody lacking such mutations.
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Kuo et al. about the improved serum half-life of the antibody comprising the mutations M428L and N434S in the method of prophylactic administration of said antibody as taught by Benjamin et al. One of ordinary skill in the art would have been motivated to reduce the prophylactic dose of the antibody comprising the mutations M428L and N434S by 3.2-fold relative to the dose required for prophylaxis with a comparative antibody which lacks mutations M428L and N434S given that it was known in the art that half-life extension of a therapeutic antibody helps maintain drug therapeutic serum levels and reduce the frequency of administration.
One of ordinary skill in the art would have had a reasonable expectation of success for adjusting the dose of the antibody comprising M428L and N434S mutations. There would have been a reasonable expectation of success given that the methods of prophylactic administration of a composition comprising an antibody are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 64, based on the teachings of Benjamin et al. and Kuo et al. discussed above regarding claim 63, the dose of the antibody comprising the mutations M428L and N434S for treatment is 3.2-fold lower than the dose required for treatment with a comparative antibody which lacks mutations M428L and N434S.
Regarding claim 66, as explained above, Benjamin et al. further teach the method of claim 61 wherein a subject is particularly at risk of or susceptible to influenza A virus infection (¶¶ [0270], [0271]). It is noted that instances wherein a subject is particularly at risk of infection encompasses during an influenza epidemic because an epidemic comprises a rapid and widespread outbreak of a disease. Therefore the teachings of Benjamin et al. and Kuo et al. in combination meet the limitations of claim 66.
Regarding claim 67, as previously explained, Benjamin et al. further teach the method of claim 61 wherein the antibody as explained above is administered in combination with an antiviral such as a neuraminidase inhibitor (¶ [0273]).
Regarding claims 69 and 70, Benjamin et al. teach the method of claim 61 wherein the antibody is administered prophylactically (¶¶ [0312], [0195]). Benjamin et al. and Kuo et al. in combination teach the antibody of claim 1 comprising the mutations M428L and N434S in the constant region of the heavy chain as explained above. Kuo et al. further teach that the mutations M428L and N434S extended the serum half-life of an antibody in cynomolgus monkey from 9.7 to 31 days, representing a 3.2-fold improvement, which is equivalent to serum half-life of 50 days in humans (page 2). Therefore, the a therapeutically effective (prophylactic) dose of an antibody comprising the mutations M428L and N434S is 3.2-fold lower than that of a comparative antibody lacking such mutations which represents a decrease in dose by approximately two-thirds, or a decrease of approximately 66.67% (does not exceed half a dose, as recited in claim 69). As to the recitation of “does not exceed one third” in claim 70, it is noted that this range falls within the dose ranges taught by the cited prior art, approximately 30% of the dose with a comparative antibody. Further, a prophylactic and a treatment dose is considered to be one determined by routine optimization according to one of skill in the art in view of the teachings of Benjamin et al. and Kuo et al.
Accordingly, claims 1-3, 7, 8, 11, 12, 14, 15, 21-24, 40, 43-44, 47-49, 57-59, 61-64, 66, 67, 69, 70 of the claimed invention as submitted on 09/04/2025 were prima facie obvious to one of ordinary skill in the art at the time of filing especially in the absence of evidence to the contrary.
Claims 25 and 45 are rejected under 35 U.S.C. 103 as being unpatentable over Benjamin et al. and Kuo et al., as applied to claims 1-3, 7, 8, 11-15, 21-24, 40, 43-44, 47-49, 57-59, 61-64, 66-70, further in view of Lindner et al. Prior art of record.
See claims 25 and 45 as submitted on 09/04/2025.
Regarding claim 25, as previously explained, the teachings of Benjamin et al. and Kuo et al. in combination disclose the sequence of claim 1.
As per SEQ ID NO: 9 in claim 25 which comprises a heavy chain antibody sequence, it is noted that instant SEQ ID NO:9 is an amino acid sequence 458 residues long comprising the following:
Amino acids 1-128 comprise instant SEQ ID NO:7 which denotes heavy chain CDRs 1-3.
Amino acids 129-458 comprise a heavy chain framework.
As per SEQ ID NO:10 in claim 25 which comprises a light chain antibody sequence, it is noted that instant SEQ ID NO:10 is an amino acid sequence 210 residues long comprising the following:
Amino acids 1-103 comprise instant SEQ ID NO:8 which denotes light chain CDRs 1-3.
Amino acids 104-210 comprise a kappa light chain framework.
The sequences of SEQ ID NO:7 and SEQ ID NO:8 which comprise amino acid residues 1-128 of SEQ ID NO:9 and amino acid residues 1-103 of SEQ ID NO:10 respectively were addressed above in the discussion of claim 22 and shown to be taught by Benjamin et al.
Neither Benjamin et al. nor Kuo et al. teach amino acids 129-458 of SEQ ID NO:9 which comprise a heavy chain framework, nor amino acids 104-210 of SEQ ID NO:10 which comprise a light chain framework.
However, Lindner et al. teach human antibody sequences including a heavy chain framework sequence and a kappa light chain framework sequence which comprise amino acids 129-458 of SEQ ID NO:9 and amino acids 104-210 of SEQ ID NO:10 respectively as follows:
Amino acids 129-458 of SEQ ID NO:9 are taught by Lindner et al. GeneBank accession number MH975460 in combination with the mutations M428L and N434S as taught by Kuo et al. which were explained above. See sequence alignment file: “US-17-607-383-9 aa129-458_pep__vs__GenBank MH975460_pep__align.pdf” (file of record.)
Amino acids 104-210 of SEQ ID NO:10 are taught by Lindner et al. GeneBank accession number MH975601. See sequence alignment file: “US-17-607-383-10 aa104-210_pep__vs__GenBank MH975601_pep__align.pdf” (file of record.)
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have combined the sequences taught by Lindner et al. and Kuo et al. with the antibody sequences comprising the antibody variable regions as taught by Benjamin et al., for the benefit of formulating a antibody against influenza A with a human framework having improved affinity or the FcRn as well as improved serum half-life. One of ordinary skill in the art would have been motivated to combine the sequences described above given that the human heavy and light chain framework sequences as well as the M428L and N434S mutations were known in the art and Benjamin et al. taught the variable light and heavy chain regions. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
One of ordinary skill in the art would have had a reasonable expectation of success for combining the sequences listed above denoting the heavy and light chain variable regions with the human framework regions wherein the heavy chain framework region comprises the M428L and N434S mutations. There would have been a reasonable expectation of success given that the methods of antibody cloning and mutagenesis are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 45, as previously explained, Benjamin et al. teach nucleic acid sequences encoding the light and heavy chains as recited in claim 43.
As per SEQ ID NO:14 in claim 45 which comprises the nucleic acid sequence of a heavy chain of an antibody, it is noted that instant SEQ ID NO:14 is a nucleotide sequence 1374 base pairs long comprising the following:
Nucleotides 1-384 comprise instant SEQ ID NO:12 which denotes the nucleotide sequence encoding the heavy chain CDRs 1-3.
Nucleotides 384-1374 comprise a nucleotide sequence encoding the heavy chain framework.
As per SEQ ID NO:15 in claim 45 which comprises the nucleic acid sequence of a light chain of an antibody, it is noted that instant SEQ ID NO:15 is a nucleotide sequence 630 base pairs long comprising the following:
Nucleotides 1-309 comprise instant SEQ ID NO:13 which denotes the nucleotide sequence encoding the light chain CDRs 1-3.
Nucleotides 310-630 comprise a nucleotide sequence encoding the light chain framework.
The sequences of SEQ ID NO:12 and SEQ ID NO:13 which comprise nucleotides 1-384 of SEQ ID NO:14 and nucleotides 1-309 of SEQ ID NO:15 respectively, were addressed above in the discussion of claim 44 and shown to be obvious variants of the sequences taught by Benjamin et al.
Neither Benjamin et al. nor Kuo et al. teach nucleotides 384-1374 of SEQ ID NO:14 which comprise a nucleotide sequence encoding the heavy chain framework, nor do they teach nucleotides 310-630 of SEQ ID NO:15 which comprise a nucleotide sequence encoding the light chain framework.
However, Lindner et al. teach human antibody nucleotide sequences including a heavy chain framework sequence and a kappa light chain framework sequence which comprise nucleotides 384-1374 of SEQ ID NO:14 and nucleotides 310-630 of SEQ ID NO:15 respectively as follows:
Nucleotides 384-1374 of SEQ ID NO:14 are taught by Lindner et al. GeneBank accession number MH975460 in combination with the mutations M428L and N434S as taught by Kuo et al. which were explained above. See sequence file: “Lindner JM et al 2019 GenBank MH975460.pdf” (file of record.)
Nucleotides 310-630 of SEQ ID NO:15 are taught by Lindner et al. GeneBank accession number MH975601. See sequence file: “Lindner JM et al 2019 GenBank MH975601.pdf” (file of record.)
The sequences in Lindner et al.’s teachings do not have 100% identity to instant SEQ ID NO: 14 and SEQ ID NO:15 because instant sequences represent codon optimized sequences of the human sequences taught by Lindner et al. Therefore, the nucleic acid sequences in Lindner et al.’s teachings are equivalent to instant nucleic acids sequences SEQ ID NO:14 and SEQ ID NO:15 because they encode the same amino acid sequences as discussed above (see discussion of claim 25 above). Further, Benjamin et al. teach the codon optimization of nucleic acid sequences to improve the efficiency of translation in expression systems (¶ [0088]). Therefore the sequences recited in claim 45 in instant application, SEQ ID NO:14 and SEQ ID NO:15, are obvious variants of the sequences taught by Lindner et al.
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have combined the nucleotide sequences taught by Lindner et al. with the antibody sequences comprising the antibody variable regions as taught by Benjamin et al. and Kuo et al., for the benefit of formulating a nucleotide sequence of an antibody against influenza A with a human framework (constant regions) having improved affinity or the FcRn as well as improved serum half-life. One of ordinary skill in the art would have been motivated to combine the nucleotide sequences described above given that the human heavy and light chain framework sequences as well as the M428L and N434S mutations were known in the art and Benjamin et al. taught the variable regions of the light and heavy chains as well as codon optimization.
One of ordinary skill in the art would have had a reasonable expectation of success for combining the sequences listed above denoting the heavy and light chain variable regions with the human framework regions wherein the heavy chain framework region comprises the M428L and N434S mutations given that the methods of antibody cloning, sequence optimization and mutagenesis are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Accordingly, amended claims 24 and 45 of the claimed invention as submitted on 09/04/2025 were prima facie obvious to one of ordinary skill in the art at the time of filing especially in the absence of evidence to the contrary.
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.
Claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-14 of U.S. patent No.10494419 to Benjamin et al. (09/08/2016) in view of Kuo et al. (previously cited). Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are directed to a human antibody against the hemagglutinin of an influenza A virus, wherein the antibody neutralizes influenza A infection.
See claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 as submitted on 09/04/2025.
As to claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 of instant application, claims 1-3, 5-14 of U.S. patent No.10494419 are directed to: (a) an antibody against the hemagglutinin of an influenza A virus, where in the antibody comprises the same CDR sequences (see alignment files below), (b) wherein the antibody neutralizes influenza A infection subtype H1, (c) said antibody comprises human constant heavy and light chain region, (d) a vector comprising the nucleic acids encoding said antibody, (e) a cell expressing such vector, and (f) a pharmaceutical composition comprising said antibody.
The two sets of claims indicated above are directed to an antibody comprising CDR sequences with 100% sequence identity as shown in the following alignment files of record:
Heavy chain CDRs:
US-17-607-383-1_pep__vs__US-10-10494419-113_pep__align.pdf
US-17-607-383-2_pep__vs__US-10-10494419-114_pep__align.pdf
US-17-607-383-3_pep__vs__US-10-10494419-115_pep__align.pdf
Light chain CDRs:
US-17-607-383-4_pep__vs__US-10-10494419-118_pep__align.pdf
US-17-607-383-5_pep__vs__US-10-10494419-119_pep__align.pdf
US-17-607-383-6_pep__vs__US-10-10494419-120_pep__align.pdf
Claims 1-3, 5-14 of U.S. patent No.10494419 do not teach the antibody wherein the heavy chain constant region comprises an M428L and a N434S mutation.
However, Kuo et al. teach an anti-vascular endothelial growth factor (VEGF) IgG1 antibody referred to as bevacizumab with an M428L and a N434S mutations in the constant region of the heavy chain (Abstract, page 1). The M428L and the N434S mutations in Kuo et al.’s teachings resulted in 11-fold improved binding for the neonatal Fc receptor (FcRn) as well as improved serum half-life of the antibody (Abstract, page 1, 2). Half-life extension of therapeutic antibody in Kuo et al.’s teachings helps maintain drug therapeutic serum levels and reduce the frequency of administration.
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Kuo et al. about the M428L and the N434S mutations in the constant region of the heavy chain of an antibody as taught by claims 1-3, 5-14 of U.S. patent No.10494419, for the benefit of improving affinity or the FcRn as well as improving serum half-life of the antibody. One of ordinary skill in the art would have been motivated to introduce an M428L and a N434S mutations in the constant region of the heavy chain of antibody 12 as taught by claims 1-3, 5-14 of U.S. patent No.10494419. given that half-life extension of a therapeutic antibody helps maintain drug therapeutic serum levels and reduce the frequency of administration.
One of ordinary skill in the art would have had a reasonable expectation of success for introducing an M428L and a N434S mutations in the constant region of the antibody heavy chain as taught by claims 1-3, 5-14 of U.S. patent No.10494419. There would have been a reasonable expectation of success given that the methods of antibody cloning and mutagenesis are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
The sets of claims indicated above differ in scope; instant claims include narrower limitations than those recited in claims 1-3, 5-14 of U.S. patent No.10494419. Instant claims 1-3, 7, 11-15, 40, 43, 47-49 are directed to (a) a human monoclonal antibody type IGg1 against the hemagglutinin of an influenza A virus, (b) wherein the antibody neutralizes influenza A infection wherein the influenza virus comprises the polymorphism N146D of influenza subtype H1 NA, (c) said antibody comprises human constant heavy and light chain regions wherein heavy chain constant region comprises an M428L and a N434S mutation, (d) a vector comprising the nucleic acids encoding said antibody, (e) a cell expressing such vector, and (f) a pharmaceutical composition comprising said antibody.
A patent to the instant claims would, necessarily, extend the rights of the already patented claims should the instant claims issue as a patent. Thus, claims 1-3, 7, 11-15, 40, 43, 47-49 are rejected.
Claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18, 26, 31-33, 37 of copending application No. 18/255,779 in view of Kuo et al. (previously cited). Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are directed to a human antibody against the hemagglutinin of an influenza A virus, wherein the antibody neutralizes influenza A infection. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
See claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 as submitted on 09/04/2025.
As to claims 1-3, 7, 11, 12, 14, 15, 40, 43, 47-49 of instant application, claims 1-18, 26, 31-33, 37 of copending application No. 18/255,779 are directed to: (a) an antibody against the hemagglutinin of an influenza A virus, where in the antibody comprises the same CDR sequences (see alignment files below), (b) wherein the antibody neutralizes influenza A infection, (c) wherein the heavy chain constant region comprises an M428L and a N434S mutation, (d) said antibody comprises human constant heavy and light chain region, (e) a vector comprising the nucleic acids encoding said antibody, (f) a cell expressing such vector, (g) a pharmaceutical composition comprising said antibody, and (h) a method of lowering the risk of influenza A infection comprising administering said antibody.
The two sets of claims indicated above are directed to an antibody comprising CDR sequences with 100% sequence identity as shown in the following alignment files of record:
Heavy chain CDRs:
US-17-607-383-1_pep__vs__US-18-255-779A-1_pep__align.pdf
US-17-607-383-2_pep__vs__US-18-255-779A-2_pep__align.pdf
US-17-607-383-3_pep__vs__US-18-255-779A-3_pep__align.pdf
Light chain CDRs:
US-17-607-383-4_pep__vs__US-18-255-779A-4_pep__align.pdf
US-17-607-383-5_pep__vs__US-18-255-779A-5_pep__align.pdf
US-17-607-383-6_pep__vs__US-18-255-779A-6_pep__align.pdf
The sets of claims indicated above differ in scope; instant claims are directed to (a) a human monoclonal antibody type IGg1 against the hemagglutinin of an influenza A virus, (b) wherein the antibody neutralizes influenza A infection wherein the influenza virus comprises the polymorphism N146D of influenza subtype H1 NA, (c) said antibody comprises human constant heavy and light chain regions wherein heavy chain constant region comprises an M428L and a N434S mutation. Claims 1-18, 26, 31-33, 37 of copending application No. 18/255,779 include additional limitations: a) a G236A mutation, a A330L mutation, and a I332E mutation in the constant region of the heavy chain. Therefore, claims 1-18, 26, 31-33, 37 of copending application No. 18/255,779 recite a subgenus (antibody comprising a G236A mutation, a A330L mutation, and a I332E mutation in addition to an M428L and a N434S mutation) anticipate the instant genus claims (antibody comprising an M428L and a N434S mutation).
Response to Arguments
Applicant's arguments filed on 09/04/2025 have been fully considered but they are not persuasive.
Applicant contends on page 8 of the Remarks: The experimental evidence provided in the present application provides compelling evidence that the claimed antibody provides unexpected results that were not taught or suggested by Benjamin or Kuo. More specifically, the claimed antibody surprisingly provides: (i) enhanced efficacy against influenza infection that was not tied to longer half-life; and (ii) decreased immunogenicity despite the presence of the MLNS substitutions.
In response: Applicant’s argument that the claimed antibody is associated with unexpected results is unpersuasive. As explained above and previously, Kuo et al. teach that the introduction of an M428L and a N434S mutations in the constant region of the heavy chain results in improved binding for the neonatal Fc receptor (FcRn) as well as improved serum half-life of the antibody (page 6). The cited paragraph from the Specification (page 64, lines 24-29) clearly states that the data suggest an enhanced interaction of the claimed antibody with the hFcRn receptor, which was a known effect of the M428L and N434S mutations as taught by Kuo et al. and others such as Zalevsky et al. (Cited in applicant’s IDS submitted on 10/28/2021). Therefore, on the contrary, the effect observed and illustrated by Figures 5 and 6 in instant Specification is in fact fully expected because it was well known in the art that the M428L and N434S mutations improved receptor binding. Regardless of whether the mutations result in a change in serum half-life of the antibody or not, Kou’s teaching about improved receptor binding alone, renders the results of enhanced efficacy observed expected and obvious.
Further, with respect to Figure 5 specifically, it is noted that the survival data of the mouse model does not demonstrate unexpected results because the effects of the M428L and N434S mutations as indicated above were known in the art, therefore enhanced efficacy was in fact expected. Applicant’s remark that the differences in survival numbers were not correlated with increased half-life of the claimed antibody is unpersuasive because enhanced efficacy was expected in the light of improved receptor binding upon introduction of an M428L and an N434S mutation.
With respect to Figure 6 specifically, it is acknowledged that the pharmacokinetics of the claimed antibody illustrated in Figs. 1 and 2 show differences in antibody half-life in a 60 day period in a macaque model, and the antibody levels in mice sera shown in Figure 6 are those taken 6 days post infection in a mouse model. It is further noted that the levels of antibody in the macaque model shown in Fig. 1 do show increased half-life of the claimed antibody as compared to the parental antibody, and the difference is observable from about day 10 (Fig. 1). The mouse model data presented in Figure 6 also shows a slight increase in serum levels of the claimed antibody as compared to the parental one (see Fig. 6, day 6 in both conditions with 1 mpk and 0.3 mpk) suggesting an increase in antibody half-life. Accordingly, Applicant’s remark that the differences in survival numbers were not correlated with increased half-life of the claimed antibody is not supported by the data shown because as discussed above, both models show an increase even if it is a slight increase of antibody serum levels suggesting that the M428L and an N434S mutation does in fact confer a longer half-life to the claimed antibody. Further, as indicated above Kou also teaches improved receptor binding, which alone or in combination with the effect of increased half-life, renders the results of enhanced efficacy observed expected and obvious.
Applicant contends on page 10 of the Remarks: The Examiner based their dismissal of Applicant's evidence of improved efficacy independent from half-life on the assertion that Kuo teaches that longer antibody half-life leads to higher drug exposure and consequently improved antibody effector response. See Final Office Action, page 36, 1st full para. Kuo is a review article that focuses on FcRn's role in antibody half-life and Fc mutations for modulating FcRn-IgG interaction. The passage in Kuo that the Examiner cites is a summary of a study by Zalevsky (Nat. Biotech. 28:157-159).
In response: As explained above, Applicant’s claimed evidence of improved efficacy independent from half-life is not supported by the by the data shown. Further, as noted in the Office Action from 05/19/2025, Kuo et al. teach that the introduction of an M428L and a N434S mutations in the constant region of the heavy chain results in improved binding for the neonatal Fc receptor (FcRn) as well as improved serum half-life of the antibody (page 6). Again, Kuo et al. are cited for teaching both results upon the introduction of an M428L and a N434S mutations in the constant region of the heavy chain, not just improved serum half-life of the antibody. Further, it is noted that improved efficacy can result from either of these outcomes, improved binding for the neonatal Fc receptor (FcRn) and improved serum half-life of the antibody, or both (see Kuo, page 6). Therefore, on the contrary, the Examiner did not base “the dismissal of Applicant's evidence of improved efficacy independent from half-life on the assertion that Kuo teaches that longer antibody half-life leads to higher drug exposure and consequently improved antibody effector response”. Instead, the Examiner maintains that there is no such evidence that enhanced efficacy occurs independently from half-life since an increase in antibody levels was indeed observed in both the macaque and the mouse model. Further, even if such evidence were presented, Kuo already teaches improved binding for the neonatal Fc receptor which alone can also lead to enhanced efficacy. With respect to the teachings of Zalevsky, while these results are related to the teachings of Kuo, they are not relevant to this discussion because Zalevsky was not cited as prior art.
Applicant contends on page 11 of the Remarks: The Examiner gives no weight to the mouse serum half-life data presented in FIG. 6 of the present application because they were obtained after a short period of time (6 days) whereas FIGS. 1 and 3 of the present application allegedly demonstrate that FluAB_MLNS has an extended half-life of 60 days and 56 days, respectively.
In response: As indicated above, the mouse model data presented in Fig. 6 has been fully considered alone and in the light of the data of the macaque model in Fig. 1. The mouse model shows only a slight increase of the claimed antibody serum levels compared to the parental one at day 6, whereas the macaque model in Fig. 1 clearly shows an extended half-life for the claimed antibody over a 60 day period (both Figs. are reproduced below). Based on the data from the two models, it is maintained that an antibody bearing the M428L and a N434S mutations would result in enhanced efficacy as taught by Kuo because the mutations do confer an extended half-life (as shown in the macaque model Fig. 1 and to a lesser degree in the mouse model Fig. 6). The results of an enhanced efficacy are entirely consistent with the teachings of Kuo and therefore they are not unexpected. Furthermore, as noted above, regardless of the half-life effect, Kuo et al. already teach improved binding for the neonatal Fc receptor upon introduction of an M428L and a N434S mutations in the constant region of the heavy chain which alone is sufficient to render the claimed findings expected and
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Fig. 1 Macaque Model Fig. 6 Mouse Model
Applicant contends on page 11 of the Remarks: The Examiner's assertion in the Final Office Action that a person of ordinary skill in the art would have been motivated to combine the antibody of Benjamin with the M428L and N434S substitution taught by Kuo to decrease risk of immunogenicity by removal of an N-linked glycosylation site is unfounded and contrary to knowledge in the art. See Final Office Action dated May 19, 2025, pages 18-19, and 37.
In response: The Examiner did not make the assertion in the Final Office Action from 05/19/2025 on pages 18, 19, and 37 that a person of ordinary skill in the art would have been motivated to combine the antibody of Benjamin with the M428L and N434S substitution taught by Kuo to decrease risk of immunogenicity by removal of an N-linked glycosylation site. The motivation to combine the antibody of Benjamin with the teachings of Kuo was not a decrease of immunogenicity, but the benefit of improving affinity or the FcRn as well as improving serum half-life of the antibody (see Final Office Action from 05/19/2025, pages 7 and 8). Further, it is noted that Applicant has not provided any evidence to support the argument that decreased risk of immunogenicity by removal of an N-linked glycosylation site is “unfounded and contrary to knowledge in the art”. The arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965)(See also MPEP § 2143.02, part II (requiring only “at least some degree of predictability,” not complete confidence in a desired outcome). In fact, as previously explained, decreased risk of immunogenicity by removal of an N-linked glycosylation site is well known and consistent with the knowledge in the art. For instance, Benjamin et al. provide evidence that removal of an N-linked glycosylation site results in decreased risk of immunogenicity. Specifically Benjamin et al. teach that removal of an structural liability such as an N-linked glycosylation site is where the glycan attaches to the amine group of asparagine residue (N) results in a reduced risk of immunogenicity (¶¶ [0199], [0200]).
With respect to the explanation in pages 18, 19 of the Final Office Action from 05/19/2025, it was indicated that “the step of introducing a N434S mutation into the antibody taught by Benjamin et al. comprises a method of reducing the risk of immunogenicity of an antibody as compared to an antibody with identical sequence lacking an M428L and a N434S mutation” (See Final Office Action from 05/19/2025 pages 18, 19). Further, it was noted that the recitation of “wherein immunogenicity is compared with a comparator antibody that is identical to the antibody except that it does not comprise the M428L and N434S mutations in the constant region of the heavy chain of the antibody” does not impart any additional structural features to the antibody as recited in claim 1, therefore this recitation is considered to flow from the features already present in the antibody as recited in claim 1.
With respect to page 37 of the Final Office Action from 05/19/2025, it was explained then and maintained herein that “Applicant’s argument that the claimed antibody is associated with surprising results of decreased immunogenicity is unpersuasive. As explained above and previously, this result is not surprising because as taught by Benjamin et al. removal of a potential N-glycosylation site, as with the N434S mutation, results in decreased immunogenicity. As previously explained, Benjamin et al. provide evidence that removal of an N-linked glycosylation site results in decreased risk of immunogenicity. Specifically Benjamin et al. teach that removal of an structural liability such as an N-linked glycosylation, where the glycan attaches to the amine group of asparagine residue (N), results in a reduced risk of immunogenicity (¶¶ [0199], [0200]). Accordingly, Applicant’s results of decreased immunogenicity found with the claimed antibody are entirely consistent with the teachings of the prior art and are not considered surprising.
Applicant contends on page 13 of the Remarks: Applicant respectfully submits that the present claims are patentably distinct from the claims of the '419 patent in view of Kuo because, as discussed above, the claimed antibody provides unexpectedly enhanced efficacy against influenza infection independent of increased half-life and decreased immunogenicity despite the presence of the MLNS substitutions. Applicant respectfully requests that this non-statutory obviousness-type double patenting rejection be withdrawn.
In response: As explained in detail above and previously, the enhanced efficacy of claimed antibody against influenza infection is entirely consistent with the teachings of the cited prior art and does not represent unexpectedly results.
Applicant contends on page 13 and 14 of the Remarks: The '779 application is a national phase application of PCT/US2021/062160, effectively filed on December 7, 2021, which is later than the effective filing date of the present application… The Examiner asserts that the claims of the present application are obvious because of the '799 application in view of Kuo. Applicant respectfully submits that issuing an obviousness-type double patenting rejection over a later-filed application containing one or more of the same claim elements is an improper use of the doctrine. If such rejections were proper, it would be impossible to grant claims containing any elements known in the art without invalidating prior patents and applications directed to even one of the elements, if the applications had a common inventor and/or applicant. If this were the case, later-filed applications could receive obviousness-type double patenting rejections if they contain any of the same claim elements, even if time had passed between the filing dates or the later-filed application was nonobvious. This goes against the purpose of the doctrine, "which is to prevent patentees from obtaining a second patent on a patentably indistinct invention to effectively extend the life of a first patent to that subject matter." See Allergan USA, Inc. v. MSNLaboratories Private Ltd., No. 24-1061, slip op. at 16 (Fed. Cir. Aug. 13, 2024). Allowing the present application would not unjustifiably extend the life of the patent. Furthermore, in a recent PTAB decision, Ex Parte Baurin, the Board reversed the examiner on similar facts found in the present application, where the examiner had rejected an earlier-filed application over a later-filed application that did not claim a common priority date (Appeal 2024-002920, Appl. No. 17/135,529 (PTAB Nov. 6, 2024)). Allergan and Ex Parte Baurin support a conclusion that the later-filed '799 application is not a proper obviousness-type double patenting reference against the present application.
In response: Applicant’s analysis of the patent term filing dates is acknowledged. This acknowledgement should not be construed as agreement or disagreement by the Examiner that these dates are correct. The MPEP indicates at MPEP 1701 that Office personnel may not express an opinion regarding the expiration date of any patent.
Applicant cites Ex parte Baurin et al., Appeal 2024-002920 (P.T.A.B Nov. 6, 2024). The Examiner acknowledges Applicant’s arguments with respect to this decision. These arguments are not persuasive as a Request for Rehearing by Examiner under MPEP 12.14.04 was filed on 3 January 2025 in this appeal. The PTAB has not addressed this request at this time.
Improper time-wise extension is not, however, the only reason for requiring a terminal disclaimer. 37 CFR 1.321(c)(3) requires that a terminal disclaimer filed to obviate a nonstatutory double patenting rejection based on commonly owned conflicting claims must also include a provision that any patent granted on that application be enforceable only for and during the period that the patent is commonly owned with the application or patent which formed the basis for the rejection. Whether common ownership “should” or “should not” be a requirement is a policy question upon which the Examiner declines to express an opinion.
A terminal disclaimer to ensure common ownership at present is a requirement, and one which the Federal Circuit in In re Cellect, LLC, 81 F.4th 1216, 2023 U.S.P.Q.2d 1011 (Fed. Cir. 2023) commented upon favorably (“We also agree with the USPTO that the Board did not err in determining that a risk of separate ownership existed and, even in the absence of separate ownership, that a terminal disclaimer would have been required to ensure common ownership.” Id. at 1230).
Applicant’s arguments with respect to Allergan USA, Inc. v. MSN Labs. Private LTD., 111 F. 4th 1358, 1369 (Fed. Cir. 2024) are not persuasive. In Allergan the Federal Circuit held that “a first-filed, first-issued, later-expiring claim cannot be invalidated by a later-filed, later-issued, earlier-expiring reference claim having a common priority date.” Allergan is therefore limited only to shielding “a first-filed, first-issued, later-expiring claim.” The Examiner submits that Allergan does not shield the instant application claims from the nonstatutory double patenting rejections as the instant application is not “first-filed” as this term is used in Allergan. Notably, the Allergan court used the term “first-filed” not “earlier-filed” and was focused on the first patent of the patent family, and considered the actual filing dates, not the effective filing dates, in its analysis. In Allergan, the claims of the challenged patent were “first-filed” because the challenged patent was the first-filed patent in its family and had an actual filing date of March 14, 2005,’ while the “later-filed” reference patents had actual filing dates of July 19, 2010, and November 30, 2012.' The reference patents issued from continuing applications claiming benefit to the challenged patent, and all three patents claimed priority to an earlier provisional application filed on March 15, 2004. In view of the facts in Allergan, it is clear that the term “first-filed” refers to the first-filed patent of the patent family and is based on actual filing dates. It would not make sense to read “first-filed” as referring to effective filing dates because the relevant claims in the three patents in Allergan appear to all have the same effective filing date. The instant application cannot be “first-filed” because it has not given rise to the first patent of its patent family.
Secondly, the instant application is not “first-issued” as this term is used in Allergan. The instant application has not yet issued. Because Allergan shields only “first-issued” patent claims from a nonstatutory double patenting challenge, cannot shield the claims of the instant application.
Third, the instant application and the reference application ’779 do not have a “common priority date” as this term is used in Allergan. The Federal Circuit explained in Allergan that it was using the term “priority date” to mean the 35 U.S.C. § 154(a)(2) date, which is the date that starts the clock for the 20-year patent term. The MPEP refers to this date as the “patent term filing date.” See MPEP 804(I)(B)(1)(a). Because a shield under Allergan applies only when a challenged patent and a reference patent have a “common priority date,” Allergan does not shield the claims of the instant application from the claims of the reference application ’779.
MPEP 804 does not instruct examiners to compare filing and expiration dates, as a threshold question, when considering whether or not an issued patent with conflicting claims may be used as a nonstatutory double patenting reference. On filing dates, MPEP 804 specifies only two limited circumstances where an examiner should compare filing dates in the examination of an ordinary (i.e., non-reissue or non-reexamination) application, neither of which is relevant to the issue of whether a patent is available to be used as a reference patent in a nonstatutory double patenting rejection. On expiration dates, MPEP 804 does not instruct examiners to predict the expiration date of a patent that may issue from an ordinary application—including the effect of patent term adjustment and any terminal disclaimers—and compare this predicted expiration date with the expiration date of a potential nonstatutory double patenting reference.
The MPEP does not instruct examiners to predict the expiration dates of patents that may issue from applications they are examining and instructs them to refrain from providing a determination on the expiration of issued patents or patents that may arise from applications. Examiners are not able to predict expiration dates because examiners cannot know how much patent term adjustment will be awarded for the patent that issues from an application under examination; the patent term adjustment calculation includes the interval of time between payment of issue fee and issuance of a patent, as well as applicant or USPTO delays that may occur within the course of prosecution. Furthermore, determining the expiration date of a reference identified on a terminal disclaimer is not always a straightforward matter because that reference itself may be subject to one or more terminal disclaimers, and the language of each terminal disclaimer involved must be considered.
MPEP 804.02(IV) indicates that a terminal disclaimer is required for “[e]ach one of the commonly owned conflicting nonstatutory double patenting references … to avoid the problem of dual ownership of patents to patentably indistinct inventions in the event that the patent issuing from the application being examined ceases to be commonly owned with any one of the double patenting references that have issued or may issue as a patent.” Based on this guidance, an applicant may not overcome multiple nonstatutory double patenting rejections by filing a terminal disclaimer over the earliest-expiring reference and then argue that no further terminal disclaimers are needed for the other reference patents or applications. MPEP 804.02(IV) requires a terminal disclaimer for each reference. It is noted that common ownership between the instant application and the reference patent has not been established.
The “risk of separate ownership” is one of the two public policy concerns underlying nonstatutory double patenting doctrine. In particular, in addition to preventing an unjustified timewise extension of the right to exclude, the nonstatutory double patenting doctrine is also grounded in the policy of avoiding the risk of harassment of an accused infringer by multiple assignees asserting essentially the same patented invention.
The relevant case law and USPTO guidance identify the risk of separate ownership as the basis for making a nonstatutory double patenting rejection and requiring a terminal disclaimer to overcome the rejection. With respect to relevant case law, Cellect at 1230 expressly identified the risk of separate ownership as a reason to uphold the double patenting rejections. This is consistent with a long line of court cases emphasizing this policy concern. Accordingly, this policy concern underlying a double patenting rejection is a separate reason, apart from unjustified timewise extension, that the reference patent could be a proper nonstatutory double patenting reference. With respect to USPTO guidance, MPEP 804.02(VI) explains that the enforcement provision in a terminal disclaimer filed under 37 CFR 1.321(c) is intended to address the risk of separate ownership. Based on this guidance, it is appropriate for an examiner to require a terminal disclaimer that will address the risk of separate ownership even where it is possible that there would be no unjustified timewise extension of the right to exclude. Therefore, even if a pending application is already terminally disclaimed with respect to another patent and thus an improper timewise extension of the patent term is unlikely, the policy rationale for the necessity of the terminal disclaimer based on the risk of separate ownership remains. The way that an Examiner requires a terminal disclaimer to address the risk of separate ownership is by making a double patenting rejection that may be overcome by filing a terminal disclaimer with the enforcement language required by 37 CFR 1.321(c)(3).
Lastly, MPEP Section 804 (I)(B)(1)(b)(i) states that if a provisional nonstatutory double patenting rejection is the only rejection remaining in an application having the earlier patent term filing date, the examiner should withdraw the rejection in the application having the earlier patent term filing date and permit that application to issue as a patent, thereby converting the provisional nonstatutory double patenting rejection in the other application into a nonstatutory double patenting rejection upon issuance of the patent. However, instant claims are also rejected under 35 USC § 103 above. Therefore, MPEP Section 804 (I)(B)(1)(b)(i) does not apply to instant application.
It is maintained that the double patenting rejections are proper.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARLENE V BUCKMASTER whose telephone number is (703)756-5371. The examiner can normally be reached M-F 8-5.
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/MARLENE V BUCKMASTER/Examiner, Art Unit 1671
/THOMAS J. VISONE/ Supervisory Patent Examiner, Art Unit 1671
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