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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 May 13, 2026 has been entered.
Claims 1-15 are pending and being acted upon in this Office Action.
Priority
Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on May 13, 2026 has been considered by the examiner and an initialed copy of the IDS is included with this Office Action.
Rejection Withdrawn
The rejection of claims 8 and 10 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph is withdrawn in view of the claim amendment.
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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
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Claims 1-12 and 14 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 6-12 and 14 of U.S. Patent No. 12,503,487 (reference). Although the conflicting claims are not identical, they are not patentably distinct from each other because the claims 1, 6-8 and 14 and the disclosure of the '487 patent teaches a method of purifying bispecific antibody comprising the step of washing the affinity chromatography column, e.g., protein A chromatography column with a low conductivity aqueous solution value of about 0.5 mS/cm or less (genus) whereas the present claims limited the conductivity value of from 0.03 to 0.35 mS/cm (species). The reference term “or less” encompasses the claimed range from “0.03 to 0.35 mS/cm. The ‘487 patent also teaches that the low conductivity aqueous solution has a conductivity value of from about 0.03 μS/cm to about 0.5 mS/cm. In one embodiment the low conductivity aqueous solution has a conductivity value of from about 0.05 μS/cm to about 0.35 mS/cm, see col. 6, lines 54-58, in particular. The low conductivity aqueous solution comprises about 0.1 mM to about 10 mM Tris.
Issued claim 1. A method of reducing content of a host cell protein in a sample including a human IgG4 or IgG1 isotype antibody and the host cell protein (aka purifying), the method comprising the steps of:
contacting a protein A chromatography material with the sample;
washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of the host cell protein in the sample after the washing step is reduced, wherein said host cell protein is phospholipase B-like 2 (PLBL2), and wherein the low conductivity aqueous solution is deionized water, which corresponds to instant claims 1, 2.
6. The method according to claim 1, wherein the human IgG1 isotype antibody is an antibody against Influenza B or an antibody against VEGF-A or an antibody against CD22 or a bispecific antibody against HER3 and EGFR or an antibody against amyloid beta or an antibody against Her2 or a bispecific antibody against Ang2 and VEGF-A or a bispecific antibody against carcinoembryonic antigen (CEA) and CD3, which correspond to bispecific antibody of instant claims 1, 2, and 14.
7. A method for producing a human IgG4 or IgG1 isotype antibody comprising the steps of:
a) cultivating a cell comprising a nucleic acid encoding a human IgG4 or IgG1 isotype antibody,
b) recovering the human IgG4 or IgG1 isotype antibody from the cell or the cultivation medium,
c) contacting the human IgG4 or IgG1 isotype antibody with a protein A chromatography material,
d) washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of a host cell protein in the sample after the washing step is reduced, wherein said host cell protein is phospholipase B-like 2 (PLBL2),
e) recovering the human IgG4 or IgG1 isotype antibody from the protein A chromatography material and thereby producing the human IgG4 or IgG1 isotype antibody; wherein the low conductivity aqueous solution is deionized water, which corresponds to instant claims 1, 2 and 14.
8. A method for purifying a human IgG4 or IgG1 isotype antibody from a sample comprising the steps of:
a) providing a sample comprising a human IgG4 or IgG1 isotype antibody,
b) purifying the human IgG4 or IgG1 isotype antibody with a protein A chromatography method/step, comprising contacting the sample with a protein A chromatography material and
washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of a host cell protein in the sample after the washing step is reduced and wherein said host cell protein is phospholipase B-like 2 (PLBL2), wherein the low conductivity aqueous solution is deionized water, which corresponds to instant claim 2.
9. The method according to claims 7 or 8, wherein the method additionally comprises washing the affinity chromatography material with a high conductivity aqueous solution and/or with a medium conductivity aqueous solution before or after washing the protein A chromatography material with low conductivity aqueous solution, which corresponds to instant claim 9.
10. The method according to claim 9, wherein the high conductivity aqueous solution has a conductivity value of about 20 mS/cm or higher, which corresponds to high conductivity aqueous solution that has a conductivity value of about 20 mS/cm to about 100 mS/cm of instant claim 10.
11. The method according to claim 9, wherein the medium conductivity aqueous solution has a conductivity value of from more than 0.5 mS/cm to less than 20 mS/cm, which corresponds to instant claim 11.
12. The method according to claim 9, wherein the high or medium conductivity aqueous solution comprises Histidine, which corresponds to the high or medium conductivity aqueous solution comprises histidine of instant claim 12.
14. The method according to claims 7 or 8, wherein the human IgG1 isotype antibody is an antibody against Influenza B or an antibody against VEGF-A or an antibody against CD22 or a bispecific antibody against HER3 and EGFR or an antibody against amyloid beta or an antibody against Her2 or a bispecific antibody against Ang2 and VEGF-A or a bispecific antibody against carcinoembryonic antigen (CEA) and CD3, which corresponds to instant claim 14.
Patent No.:
Rejected over Patent claims:
Low conductivity value
Further chromatography
About 0.1 mM to about 8 mM Tris
About 0.05 to about 2 mM Potassium phosphate
pH of about 7 to about 9.5
12503487
1, 6-11 and 14
about 0.5 mS/cm or less, such as 0.03µS/cm to 0.35 mS/cm, col. 6, lines 54-58
Col. 9, lines 1-2
About 0.1 to about 10 mM Tris, col.
Col. 7, lines 32-36
Col. 7, line 41-42
Col. 7, line 47-50
Applicant's arguments filed May 13, 2026 have been fully considered but they are not persuasive.
Applicant’s position is that as noted in the MPEP @804(II)(B)(1):
When considering whether the invention defined in a claim of an application would have been anticipated by or is an obvious variation of the invention defined in the claim of a patent or copending application, no part of the reference patent or application may be used as if it were prior art. General Foods Corp. v. Studiengesellschaft Kohle mbH, 972 F.2d 1272, 1281, 23 USPQ2d 1839, 1846 (Fed. Cir. 1992) ("Our precedent makes clear that the disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims").
The pending claims relate to methods of producing or purifying a bispecific antibody that includes, in relevant part, the steps of washing the affinity chromatography material with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of from 0.03 pS/cm to 0.35 mS/cm, recovering the bispecific antibody from the affinity chromatography material, and performing a further chromatography step.
The cited claims of the reference patent fail to teach or suggest washing the affinity chromatography material with a low conductivity aqueous solution that has a conductivity value of from 0.03 pS/cm to 0.35 mS/cm and performing a further chromatography step after recovering the bispecific antibody from the affinity chromatography material.
The Office Action states that "the '487 patent teaches a method of purifying bispecific antibody comprising the step of washing the affinity chromatography column, e.g., protein A chromatography column with a low conductivity aqueous solution value of about 0.5 mS/cm or less (genus) whereas the present claims limited the conductivity value of from 0.03 to 0.35 mS/cm (species). The reference term "or less" encompasses the claimed range from "0.03 to 0.35 mS/cm. The '487 patent also teaches that the low conductivity aqueous solution has a conductivity value of from about 0.03 uS/cm to about 0.5 mS/cm. In one embodiment the low conductivity aqueous solution has a conductivity value of from about 0.05 uS/cm to about 0.35 mS/cm, see col. 6, lines 54-58, in particular," (Office Action, page 4).
However, MPEP §804(II)(B)(3) notes that "A nonstatutory double patenting rejection, if not based on an anticipation rationale or an "unjustified timewise extension" rationale, is "analogous to [a failure to meet] the nonobviousness requirement of 35 U.S.C. 103" except that the patent disclosure principally underlying the double patenting rejection is not considered prior art. In re Braithwaite, 379 F.2d 594, 154 USPQ 29 (CCPA 1967). Even though the specification of the applied patent or copending application is not prior art, it may still be used to interpret the applied claims," (emphasis added).
As such, the use of the specification of the reference patent is limited strictly to claim construction (interpreting the meaning of the reference claims), and is not available as prior art to provide motivation or to fill in missing specific range of conductivity values not present in the reference claims. While the claims of the reference patent may disclose the "genus" of low conductivity aqueous solution values of about 0.5 mS/cm or less, there is nothing in the claims of the reference patent that teaches or suggests a conductivity value of from 0.03 uS/cm to 0.35 mS/cm.
Moreover, there is nothing in the claims of the reference patent that teaches or suggests performing a further chromatography step after recovering the bispecific antibody from the affinity chromatography material. Thus, the currently pending claims are patentably distinct over the cited claims of the reference patent.
Accordingly, for at least the reasons set forth above, Applicant respectfully requests the rejections under nonstatutory double patenting be withdrawn.
In response, Issued claim 1 recites a method of reducing content of a host cell protein in a sample including a human IgG4 or IgG1 isotype antibody and the host cell protein, the method comprising the steps of: contacting a protein A chromatography material with the sample; washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of the host cell protein in the sample after the washing step is reduced, wherein said host cell protein is phospholipase B-like 2 (PLBL2), and wherein the low conductivity aqueous solution is deionized water.
Issued claim 7 recites a method for producing a human IgG4 or IgG1 isotype antibody comprising the steps of: a) cultivating a cell comprising a nucleic acid encoding a human IgG4 or IgG1 isotype antibody, b) recovering the human IgG4 or IgG1 isotype antibody from the cell or the cultivation medium, c) contacting the human IgG4 or IgG1 isotype antibody with a protein A chromatography material, d) washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of a host cell protein in the sample after the washing step is reduced, wherein said host cell protein is phospholipase B-like 2 (PLBL2), e) recovering the human IgG4 or IgG1 isotype antibody from the protein A chromatography material and thereby producing the human IgG4 or IgG1 isotype antibody; wherein the low conductivity aqueous solution is deionized water.
Issued claim 8 recites a method for purifying a human IgG4 or IgG1 isotype antibody from a sample comprising the steps of: a) providing a sample comprising a human IgG4 or IgG1 isotype antibody, b) purifying the human IgG4 or IgG1 isotype antibody with a protein A chromatography method/step, comprising contacting the sample with a protein A chromatography material and washing the protein A chromatography material, after the contacting step, with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, wherein the amount of a host cell protein in the sample after the washing step is reduced and wherein said host cell protein is phospholipase B-like 2 (PLBL2), wherein the low conductivity aqueous solution is deionized water.
The specification can be used as dictionary for claim terminology, see MPEP 804 II(b)(1). “The specification may be used to learn the meaning of terms and in interpreting the coverage of a claim.” In re Basell Polliolefine Italia S.P.A. 89 USPQ2d 1030 (Fed. Cir. 2008).
In this case, the specification is used to determine “or less” encompasses by the issued claims. The ‘487 patent discloses washing the protein A chromatography material after the contacting step with a low conductivity aqueous solution that has a conductivity value of from about 0.03 μS/cm to about 0.5 mS/cm. In one embodiment the low conductivity aqueous solution has a conductivity value of from about 0.05 μS/cm to about 0.35 mS/cm, which is the same washing step d) after the contacting step with a low conductivity aqueous solution that has a conductivity value of from about 0.03 μS/cm to about 0.5 mS/cm of instant claims 1, 2, see col. 6, lines 54-58, in particular.
Regarding performing a further chromatography step after recovering the bispecific antibody from the affinity chromatography material, the issued patent also discloses the methods may include one or more further chromatography steps, see col. 9, lines 1-2. Thus the recitation of performing a further chromatography step in instant claim 1 is anticipated by the issued patent. As such, the subject matter claimed in the instant application is fully disclosed in the referenced issued patent and would be covered by the patent.
Further, the submission of a terminal disclaimer in compliance with 37 CFR 1.321(b) is required to overcome a double patenting rejection because it seeks to prevent the possibility of multiple suits against an accused infringer by different assignees of patents claiming patentably indistinct variations of the same invention. In re Van Ornum, 686 F.2d 937, 944-48, 214 USPQ 761, 767-70 (CCPA 1982) and to prevent unjustified timewise extension of patent term based on a judicially created doctrine grounded in public policy. “Fundamental to this doctrine is the policy that: ‘[t]he public should … be able to act on the assumption upon the expiration of the patent it will be free to use not only the invention claimed in the patent but also modifications or variants which would have been obvious to those of ordinary skill in the art at the time the invention was made.’” In re Longi, 892-3, citing In re Zickendraht, 319 F.2d 225, 232 (CCPA 1963) (Rich, J., concurring), emphasis in original. See also Singer Mfg. Co. v. June Mfg. Co., 163 U.S. 169, 185 (1896). Without the protection of the safe harbor provision, these public policy concerns apply to all continuation applications and patents filed from a parent patent. See MPEP 1504.06.
For these reasons, the rejection is maintained.
Claims 1, 2, 13 and 15 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 6-12 and 14 of U.S. Patent No. 12,503,487 (reference) in view of the US Patent No. 8,945,552 (of record, issued February 3, 2015; PTO 892).
The teachings of the ‘487 patent have been discussed supra.
The reference above does not teach the method of producing bispecific antibody wherein the bispecific antibody comprising a) the heavy chain and the light chain of a first full length antibody that specifically binds to a first antigen; and b) the modified heavy chain and the modified light chain of a second full length antibody that specifically binds to a second antigen, wherein the constant domains CL and CH1 are replaced by each other as per claim 13, wherein the first antigen is human VEGF and the second antigen is human ANG-2 or the first antigen is human ANG-2 and the second antigen is human VEGF as per claim 14 and wherein said first antigen-binding site comprises as heavy chain variable domain (VH) the SEQ ID NO: 1, and as light chain variable domain (VL) the SEQ ID NO: 2; and said second antigen-binding site comprises as heavy chain variable domain (VH) the SEQ ID NO: 3, and as light chain variable domain (VL) the SEQ ID NO: 4 as per claim 15.
Regarding claim 13, the ‘552 patent teaches that the bispecific antibody is a full-length antibody wherein the constant domains CL and CH1 are replaced by each other, see Fig. 1 right side, in particular.
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421
548
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Greyscale
Regarding claim 15, the ‘552 patent teaches bispecific anti-VEGF/anti-ANG-2 antibody wherein the first antigen-binding site that binds to VEGF comprise as heavy chain variable domain (VH) the SEQ ID NO: 1, which is 100% identical to the claimed SEQ ID NO: 1, see Summary of the invention, reference SEQ ID NO: 1, sequence alignment below:
Query Match 100.0%; Score 676; Length 230;
Best Local Similarity 100.0%;
Matches 123; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAASGYTFTNYGMNWVRQAPGKGLEWVGWINTYTGEPTY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLVESGGGLVQPGGSLRLSCAASGYTFTNYGMNWVRQAPGKGLEWVGWINTYTGEPTY 60
Qy 61 AADFKRRFTFSLDTSKSTAYLQMNSLRAEDTAVYYCAKYPHYYGSSHWYFDVWGQGTLVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AADFKRRFTFSLDTSKSTAYLQMNSLRAEDTAVYYCAKYPHYYGSSHWYFDVWGQGTLVT 120
Qy 121 VSS 123
|||
Db 121 VSS 123
and a light chain variable domain (VL) comprising SEQ ID NO: 2, which is 100% identical to the claimed SEQ ID NO: 2, see reference SEQ ID NO: 2, sequence alignment below:
Qy 1 DIQMTQSPSSLSASVGDRVTITCSASQDISNYLNWYQQKPGKAPKVLIYFTSSLHSGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQMTQSPSSLSASVGDRVTITCSASQDISNYLNWYQQKPGKAPKVLIYFTSSLHSGVPS 60
Qy 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQYSTVPWTFGQGTKVEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQQYSTVPWTFGQGTKVEIK 107
And the second antigen binding site that binds to angiopoietin 2 (Ang2) comprises SEQ ID NO: 3, which is identical to the claimed SEQ ID NO: 3, see reference SEQ ID NO: 3, sequence alignment below:
Query Match 100.0%; Score 700; Length 128;
Best Local Similarity 100.0%;
Matches 128; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNSGGTNY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNSGGTNY 60
Qy 61 AQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARSPNPYYYDSSGYYYPGAFDIWG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARSPNPYYYDSSGYYYPGAFDIWG 120
Qy 121 QGTMVTVS 128
||||||||
Db 121 QGTMVTVS 128
And a light chain variable domain (VL) comprises the amino acid sequence of SEQ ID NO: 4, which is 100% identical to the claimed SEQ ID NO: 4, see reference SEQ ID NO: 4, sequence alignment below:
Query Match 100.0%; Score 579; Length 110;
Best Local Similarity 100.0%;
Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QPGLTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QPGLTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIPER 60
Qy 61 FSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSDHYVFGTGTKVTVL 108
||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSDHYVFGTGTKVTVL 108
The ‘522 patent teaches the bispecific antibody is useful for treating cancer or suffering from vascular diseases, see col. 29-30.
In view of the combined teachings of the references, it would have been prima facie obvious to a person of ordinary skill in the art before the effective filling date of the claimed invention to have produced and purified the bispecific antibody of the ‘552 patent using the method of the ‘487 patent by substituting ‘487 patent’s bispecific antibody for the ‘552 patent’s antibody that binds to VEGF and angiopoietin 2 (Ang-2) wherein the first antigen-binding site comprises as heavy chain variable domain (VH) the SEQ ID NO: 1, and as light chain variable domain (VL) the SEQ ID NO: 2; and said second antigen-binding site comprises as heavy chain variable domain (VH) the SEQ ID NO: 3, and as light chain variable domain (VL) the SEQ ID NO: 4 with a reasonable expectation of success, e.g., removing host cell proteins contaminants.
One of ordinary skill in the art would have had a reasonable expectation of success in producing the full-length IgG bispecific antibody that binds to human VEGF and human angiopoietin 2 (Ang-2) because the ‘522 patent teaches the heavy and light chain variable regions of the bispecific antibody that binds to human VEGF and human Ang-2 and the wherein the constant domains CL and CH1 are replaced by each other to facilitate heavy and light chain pairing and Nadarajah teaches that low conductivity buffer can used to wash the affinity chromatography materials for better removal of host cells contaminants.
One of ordinary skill in the art would have been motivated to do so because the ‘522 patent teaches the bispecific antibody is useful for treating cancer or suffering from vascular diseases, see col. 29-30.
Given the lack of any additional rebuttal, the rejection is maintained for reasons of record.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PHUONG HUYNH whose telephone number is (571)272-0846. The examiner can normally be reached on 9:00 a.m. to 6:30 p.m. The examiner can also be reached on alternate alternative Friday from 9:00 a.m. to 5:30 p.m.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Misook Yu, can be reached at 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PHUONG HUYNH/ Primary Examiner, Art Unit 1641
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