Notice of Pre-AIA or AIA Status
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Status of Application, Amendments and/or Claims
2. Applicant’s response dated 8/18/2026 is considered and entered into record. Claims 1-30 are pending.
Election/Restriction
3. Applicant’s election without traverse of “clipped variant” as the species of anti-BAFF-R antibody variant, in the reply filed on 18 August 2026 is acknowledged.
4. Claims 8-17 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 18 August 2026.
5. The requirement is still deemed proper and is therefore made FINAL.
6. Claims 1-7, and 18-30, drawn to a composition comprising anti-B-cell-activating factor receptor (BAFF-R) antibodies, are considered for examination in the instant application.
Specification
7. The disclosure is objected to because of the following informalities:
(A) Brief Description of the drawings:
The description of Figures 5-7 and 21 refers to sequences which are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
MPEP 37 C.F.R. 1.831 - Requirements for patent applications filed on or after July 1, 2022, having nucleotide and/or amino acid sequence disclosures states that: Where the description or claims of a patent application discuss a sequence that is set forth in the "Sequence Listing XML" in accordance with paragraph (a) of this section, reference must be made to the sequence by use of the sequence identifier, preceded by "SEQ ID NO:" or the like in the text of the description or claims, even if the sequence is also embedded in the text of the description or claims of the patent application. Where a sequence is presented in a drawing, reference must be made to the sequence by use of the sequence identifier (§ 1.832(a) ), either in the drawing or in the Brief Description of the Drawings, where the correlation between multiple sequences in the drawing and their sequence identifiers (§ 1.832(a) ) in the Brief Description is clear. It is noted that the sequences in the corresponding drawings (Figures 5-7, 21) also do not have sequence identification numbers (SEQ ID NOs).
(B) Page 77, line 4 has a typographical error “(S58)” instead of “S57”.
(C) Internet address:
The disclosure contains an embedded hyperlink and/or other form of browser-executable code (see, for example, page 58: para 3). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code. See MPEP § 608.01.
8. Appropriate correction is required for each of the informalities.
Claim Rejections - 35 USC § 102
9. 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.
10. Claims 1-7 and 18-30 are rejected under AIA 35 U.S.C. 102(a)(1) as being anticipated by Cosenza et al USP 9,458,240 (application # 13/991,984), 10/4/2016, as evidenced by Patrick et al WO 2021/207657, 10/14/2021 and Boune et al (Antibodies 9: 1-20, 2020).
11. The claims are directed to a composition and a pharmaceutical formulation comprising anti-BAFF-R antibodies, wherein the antibodies comprise a heavy chain (HC) and a light chain (LC) amino acid sequence of SEQ ID NOs: 1 and 2 respectively, at least 90% of the N-glycosylated Fc regions are afucosylated, and 0-10%, 0-7%, 0.5-4% of the N-glycosylated Fc regions comprise a high mannose glycan (claims 1-3, 20); 0-49%, 15-38% of N-glycosylated Fc regions are galactosylated (claims 4, 5); and at least 95% of Fc regions are N-glycosylated (claim 6, 24-26). Claims 21 and 22 recite that the pharmaceutical formulation comprises a unit dose of the BAFF-R antibody in the recited amounts, in a liquid formulation or a lyophilizate. Claim 23 recites a pharmaceutical product comprising a vial or other claimed devices, and the formulation. The claims also recite that the composition comprises a clipped variant (claim 7), comprising a clipping between HC residues 56 and 57 (claim 18), and the clipped variant accounts for up to 10% of the total BAFF-R antibodies and fragments thereof in the composition (claim 19, 27); up to 4% of the BAFF-R antibodies in the composition (claim 29); and a pharmaceutical product comprising the composition, a pharmaceutical carrier and a container containing the composition and carrier (claims 28, 30).
12. Cosenza et al teach anti-BAFFR antibody compositions in a liquid or a lyophilizate formulation having an antibody concentration of at least 50 mg/ml (Abstract). The reference teaches a non-fucosylated (i.e. 100% afucosylated) anti-BAFFR antibody MOR6654B having the amino acid sequences of HC and LC of SEQ ID NOs: 9 and 10 respectively, which are 100% identical to the corresponding instantly claimed HC and LC comprising SEQ ID NOs: 1 and 2 (Appendix a, b – highlighted) (col 1, lines 39-48; col 2, embodiment 4; col 3, embodiment 19), wherein non-fucosylation is an altered type of glycosylation, which increases the ADCC activity (col 18, para 4; claims 1-7, 12, 15-16). The reference also teaches N-linked glycans (glycosylation) attached to the CH2 domain of HC (Fc region), wherein the glycosylation can comprise galactose residues, and wherein the glycans have no effect on "human immunogenic response after administration" (col 18, para 3) (instant claims 1-6, 24). The reference further teaches a pharmaceutical composition comprising the antibody and a carrier (instant claim 20), and a pre-filled syringe (container or pharmaceutical product) including the pharmaceutical composition (formulation) (col 7, lines 1-4, 34-36) (instant claims 23, 28, 30), wherein the anti-BAFFR antibody concentration in the composition is 150 mg/ml or at least about 150 mg/ml or 300 mg/ml (col 8, para 1; claim 16; Table 4) (instant claims 21, 22).
13. Even though Cosenza et al teach that the antibodies are typically glycosylated and N-linked glycans are attached to CH2 of heavy chain, the reference does not teach a clipped variant, a percent of Fc regions that are N-glycosylated, a percent of which are galactosylated, or have a high mannose glycan as recited in instant claims 1-7, 18-19, 24-27, and 29. Cosenza et al, however, teach the same anti-BAFFR antibody (MOR6654B) having identical HC and LC amino acid sequences as stated above, wherein the antibody is produced in the CHO cell line, and wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (col 20, Examples, para 1-3; Table 1). It is noted that the presently claimed anti-BAFFR antibody is also produced using the Chinese hamster ovary (CHO) cells, that have a defined glycosylation profile, and result in non-fucosylation using the same gene expression as taught by Cosenza et al (instant specification: pages 57, 58, Production, para 1, 3). The specification teaches that the abundance of N-glycan glycosylation, high mannose N-glycans and N-glycan galactosylation is defined by the manufacturing cell line (Table 5-1A), which is also evinced by the prior art. For example, Patrick et al provide evidence the presence of reduced amounts of clipped variant, which is in less than 5% of a pharmaceutical composition comprising an antibody that can be produced using CHO cells (page 2, lines 9-11; page 3, lines 28-29; page 34, lines 21-24). Boune et al evidence that high mannose Fc glycans can represent up to 10% of recombinant IgG depending upon cell lines (para spanning pages 11 and 12) in therapeutic antibody compositions, and further state that most therapeutic recombinant antibodies are produced in CHO cells (page 6, para 1). Because Cosenza et al and instant claims teach the same anti-BAFFR antibody having the same sequences, and designation, wherein the antibody is produced using the same cell line and culture method including fucosyltransferase inactivation, the glycosylation and percent of clipped variants, comprising clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary (instant claims 1-7, 18-19, 24-27, and 29). The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977). "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art's functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). [MPEP 2112(I)].
14. Cosenza et al therefore anticipate the invention.
Double Patenting
Non-Statutory
15. 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).
16. 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).
17. 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.
18. 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.
19. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 51-56, and 58-60 of co-pending application number 18/996,905, in view of Cosenza et al (2016), Mimura et al (Front Immunol 13: 1-10, 2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an anti-BAFF-R antibody (ianalumab) that is afucosylated, wherein the antibody of the ‘905 application comprises
a HC and LC of SEQ ID NOs: 1 and 2 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2.
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘905 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘905 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
20. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
21. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 121, 136, 143-145, 147-148, 152-155 and 157 of co-pending application number 18/035472, in view of Cosenza et al (2016), Mimura et al (2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an anti-BAFF-R antibody (ianalumab), wherein the antibody of the ‘472 application comprises
a HC and LC of SEQ ID NOs: 61 and 62 respectively (claim 147) that are a 100% identical to instant corresponding SEQ ID NOs: 1 and 2.
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘472 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract). The presence of glycosylation as part of post-translational modification is also taught by the ‘472 PGPB (para 0148).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘472 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
(iii) ‘472 claims recite a combination comprising a BAFFR binding antibody, while instant claims only recite a composition comprising the BAFFR antibody. It is however, noted that “comprising" is a term of art used in claim language which means that the named elements are essential, but other elements may be added and still form a construct within the scope of the claim. [MPEP 2111.03(I)]. Since instant claims recite the BAFFR antibody as an essential element of the composition, the claims are obvious over the ‘472 claims.
22. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
23. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 10 and 11 of co-pending application number 17/773935, in view of Cosenza et al (2016), Mimura et al (Front Immunol 13: 1-10, 2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an anti-BAFF-R antibody (ianalumab).
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘935 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘935 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
(iii) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while the ‘935 claims do not recite sequences. However, the ‘935 PGPB (para 0016) teaches that the anti-BAFFR antibody (ianalumab) comprises HC and LC of SEQ ID NOs: 9 and 10 respectively, which are 100% identical to instant SEQ ID NOs: 1 and 2.
24. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
25. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-9 and 12-16 of US Patent 9,458,240, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a lyophilized formulation (lyophilizate) or a pharmaceutical formulation comprising an anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody is non-fucosylated or afucosylated, and the antibody of the ‘240 patent comprises a HC and LC of SEQ ID NOs: 9 and 10 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2 (Appendices a, b).
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘240 patent claims do not have these limitations. However, the ‘240 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (col 20, Examples, para 1-3; Table 1), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’240 patent claims therefore, anticipate instant claims.
26. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 9,458,240.
27. Claims 1-7 and 18-20, 23-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-10 of US Patent 10,899,841, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a lyophilized formulation (lyophilizate) or a pharmaceutical formulation comprising an anti-BAFF-R antibody.
The only differences between the two sets of claims are:
i) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while the ‘841 claims only recite CDR sequences. However, the CDRs recited in the ‘841 patent claims correspond to the HC and LC sequences of SEQ ID NOs: 9, 10 (col 2, embodiments 1, 4), which are 100% identical to instantly claimed SEQ ID NOs: 1 and 2 respectively.
ii) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘841 patent claims do not have these limitations. However, the ‘841 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (col 20, Examples; Table 1), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evidenced from the teachings of Patrick et al and Boune et al as stated in the rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’841 patent claims therefore, anticipate instant claims.
28. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 10,899,841.
29. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-5 of US Patent 12,054,555, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a pharmaceutical formulation comprising an anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody is of the patent comprises a HC and LC of SEQ ID NOs: 9 and 10 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2, and a pre-filled syringe.
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘555 patent claims do not have these limitations. However, the ‘555 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (col 20, Examples; Table 1), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’555 patent claims therefore, anticipate instant claims.
30. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 12,054,555.
31. Claims 1-7 and 18-30 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-8, 10-19 and 21-25 of co-pending application number 18/771283, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a lyophilized formulation (lyophilizate) or a pharmaceutical formulation comprising an anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody is of the patent comprises a HC and LC of SEQ ID NOs: 9 and 10 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2, and a pre-filled syringe.
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, afucosylation, clipped variant, while the ‘283 claims do not have these limitations. However, the ‘283 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (paras 0219, 0220), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’283 claims therefore, anticipate instant claims.
32. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
33. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 3-5 of US Patent 9,216,219, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an aqueous composition comprising a non-fucosylated or afucosylated anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody of the patent comprises a HC and LC of SEQ ID NOs: 9 and 10 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2, and a pre-filled syringe.
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘219 patent claims do not have these limitations. However, the ‘219 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (cols 17-19, Examples of Formulations, paras 1-3), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’219 patent claims therefore, anticipate instant claims.
34. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 9,216,219.
35. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-2, 4-5 of US Patent 9,751,951, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an aqueous composition comprising a non-fucosylated or afucosylated anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody of the patent comprises a HC and LC of SEQ ID NOs: 9 and 10 respectively that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2, and a pre-filled syringe.
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘951 patent claims do not have these limitations. However, the ‘951 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (cols 17-19, Examples of Formulations, paras 1-3), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’951 patent claims therefore, anticipate instant claims.
36. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 9,751,951.
37. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-4 of US Patent 10,689,451, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a pharmaceutical formulation comprising an anti-BAFF-R antibody at a concentration of 150 mg/ml, wherein the antibody is non-fucosylated or afucosylated.
The only differences between the two sets of claims are:
i) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while the ‘451 claims only recite CDR sequences. However, the CDRs recited in the ‘451 patent claims correspond to the HC and LC sequences of SEQ ID NOs: 9, 10 (col 4, lines 36-40, 49-53), which are 100% identical to instantly claimed SEQ ID NOs: 1 and 2 respectively.
ii) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘451 patent claims do not have these limitations. However, the ‘451 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (col 17, Examples of Formulation, para 1-3), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al as stated in the rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’451 patent claims therefore, anticipate instant claims.
38. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 10,689,451.
39. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-5, 7 and 9-13 of US Patent 8,106,163, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a BAFFR antibody and a pharmaceutical composition comprising the antibody that is non-fucosylated or afucosylated, wherein the antibody of the patent comprises a HC and LC of SEQ ID NOs: 75 and 71 respectively (claim 7) that are 100% identical to instant corresponding SEQ ID NOs: 1 and 2.
The only difference between the two sets of claims is:
Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘163 patent claims do not have these limitations. However, the ‘163 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (Example 4; Table 1), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al for reasons explained in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’163 patent claims therefore, anticipate instant claims.
40. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 8,106,163.
41. Claims 1-7 and 18-30 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-3 of US Patent 9,340,620, as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite a BAFFR antibody and a composition comprising the antibody.
The only differences between the two sets of claims are:
i) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while the ‘620 claims only recite CDR sequences. However, the CDRs recited in the ‘620 patent claim 1b are associated with MOR06654 or the MOR06654B (non-fucosylated IgG1) antibody (Example 4; Table 1), which correspond to the HC and LC sequences of SEQ ID NOs: 75 and 71 (col 14, para 3), and are 100% identical to instantly claimed SEQ ID NOs: 1 and 2 respectively.
ii) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘620 patent claims do not have these limitations. However, the ‘620 BAFFR antibody is also produced in the CHO cell line, wherein the fucosyltransferase gene is inactivated, resulting in a non-fucosylated form designated as MOR6654B (Example 4; Table 1), which is the same as instant antibody (instant specification – pages 57, 58), i.e. both sets of claims recite the same anti-BAFFR antibody that is produced using the same cell line. The amount of glycosylation, galactosylation, high mannose glycans and clipped variant would therefore, inherently be the same as evinced by the teachings of Patrick et al and Boune et al for reasons explained in the 102 rejection. Since both sets of claims recite the same antibody, clipping between HC residues 56 and 57, would inherently be the same, absent any evidence to the contrary. The claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).
The ’620 patent claims therefore, anticipate instant claims.
42. Therefore, the instant claims are not patentably distinct over the issued claims in U.S. patent 9,340,620.
43. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 2 and 4 of co-pending application number 18/558730, in view of Cosenza et al (2016), Mimura et al (2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite an anti-BAFF-R antibody (ianalumab).
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘730 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘730 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
(iii) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while ‘730 claim 2 only recites CDR sequences. However, the ‘730 PGPB (Table 1) teaches that the anti-BAFFR antibody (ianalumab) comprises HC and LC of SEQ ID NOs: 9 and 10 respectively, which are 100% identical to instant SEQ ID NOs: 1 and 2 and which correspond to the claimed CDRs of the ‘730 application.
44. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
45. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 49-51 and 56-57 of co-pending application number 18/019467, in view of Cosenza et al (2016), Mimura et al (2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite ianalumab or an anti-BAFF-R antibody.
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘467 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘467 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al, Patrick et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
(iii) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while ‘467 claims do not recite any sequence. However, the ‘467 PGPB (para 0080; Table 1) teaches that the anti-BAFFR antibody (ianalumab) comprises HC and LC of SEQ ID NOs: 9 and 10 respectively, which are 100% identical to instant SEQ ID NOs: 1 and 2.
46. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
47. Claims 1-7 and 20-26 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 52, 60, 62-69 of co-pending application number 18/019469, in view of Cosenza et al (2016), Mimura et al (2022), as evidenced by Patrick et al (2021) and Boune et al (2020).
Although the conflicting claims are not identical, they are not patentably distinct from each other because in each case the claims recite ianalumab or an anti-BAFF-R antibody.
The only differences between the two sets of claims are:
(i) Instant claims recite high mannose glycan, glycosylation, galactosylation, clipped variant, while the ‘469 claims do not have these limitations. However, these would be obvious over the teachings of Cosenza et al, and as evidenced by Patrick et al and Boune et al. for reasons stated above. The person of ordinary skill in the art would be motivated to consider glycosylation patterns of therapeutic antibodies, as nonfucosylated and galactosylated IgG provide insights to improved therapeutic strategies (Mimura et al, Abstract).
(ii) Instant claims recite percentages of high mannose glycan, glycosylation, galactosylation, and clipped variant, while the ‘469 claims do not have such limitations. However, these would be obvious in view of the teachings of Cosenza et al, Patrick et al and Boune et al, wherein the amount of glycosylation and galactosylation can be defined by manufacturing cell lines (Cosenza et al). The person of ordinary skill would find it obvious and be motivated to optimize therapeutic antibodies by using glycoengineering strategies “to reduce glyco-heterogeneity of mAbs” and “increase their safety profile” for improved therapeutic efficacy (Boune et al, Abstract).
(iii) Instant claims recite the specific HC and LC sequences of the anti-BAFFR antibody corresponding to SEQ ID NOs: 1 and 2, while ‘469 claims do not recite any sequence. However, the ‘469 PGPB (para 0102; Table 1) teaches that the anti-BAFFR antibody (ianalumab) comprises HC and LC of SEQ ID NOs: 9 and 10 respectively, which are 100% identical to instant SEQ ID NOs: 1 and 2.
48. This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
NOTE: It is incumbent on the Applicant to inform the office of all related subject matter and to file all related terminal disclaimers. See 37 CFR 1.56, Duty to disclose information material to patentability
Conclusion
49. No claims are allowed.
50. The prior art considered pertinent to Applicant’s disclosure is as follows:
Shi et al (Biotech Bioeng 111(1907-1919, 2014)
(Reference teaches that traditionally, if the high mannose glycan levels in a biotherapeutic determined by the cell line and cell culture conditions
were less than a threshold (like 10%), “not much was done to modulate their level” (page 1908, col 1, para 2), implying that less than 10% (such as 0-10%) of high mannose glycan levels are acceptable.)
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/A. D./
Examiner, Art Unit 1675
14 September 2026
/KIMBERLY BALLARD/Primary Examiner, Art Unit 1675
Prosecution Insights