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 .
Status of the Claims
Claims 1 – 4, 6 – 12, and 21 were pending. Claims 1 and 8 – 12 have been amended; claims 6 – 7 and 10 have been canceled. Claims 1 – 4, 8 – 9 and 11 – 25 are currently pending, with nonelected claims 13 – 20 and 22 – 25 withdrawn from consideration. Claims 1 – 4, 8 – 9, 11 – 12 and 21 are the subject of this Office Action.
Election/Restrictions
The restriction requirement among the species of the second binding domain as set forth in the Office action mailed on 02/08/2024, has been reconsidered in view of the claim amendments of 02/05/2026 and the prior art. The restriction requirement among the species of the second binding domain is hereby withdrawn. However, the restriction among the species of the source of NK cells and the species for the first binding domain are maintained.
Furthermore, claims 13 – 20 and 22 – 25, directed to methods of methods for preparing cryopreserved preloaded human NK cells or a method for reconstituting/preparing viable preloaded human NK cell or methods for treating or ameliorating a disease are withdrawn from consideration because they are in separate groups of inventions that do not relate to a single general inventive concept under PCT Rule 13.1 as discussed in the Requirement for Restriction/Election of 02/08/2024.
In view of the above noted withdrawal of the restriction requirement, applicant is advised that if any claim presented in a divisional application is anticipated by, or includes all the limitations of, a claim that is allowable in the present application, such claim may be subject to provisional statutory and/or nonstatutory double patenting rejections over the claims of the instant application.
Once a restriction requirement is withdrawn, the provisions of 35 U.S.C. 121 are no longer applicable. See In re Ziegler, 443 F.2d 1211, 1215, 170 USPQ 129, 131-32 (CCPA 1971). See also MPEP § 804.01.
OBJECTIONS/REJECTIONS WITHDRAWN
Claim Objections
Claims 8 – 11 are objected to because of the following informalities: each claim recites “selected form the group consisting of”, but should recite “selected from the group consisting of”. Appropriate correction is required.
In view of the claim amendments in the reply of 02/05/2026, this objection is withdrawn.
Claim Rejections - 35 USC § 103
Claims 1, 3, 4, 6, 7, and 21 are rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL in view of OSAKI and BOYDEN (US 2010/0152880 A1, published 06/17/2010, see PTO-892).
In view of the claim amendments in the reply of 02/05/2026, this rejection is withdrawn.
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL in view of OSAKI and BOYDEN as applied to 1, 3, 4, 6, 7, and 21 and in further view CHENG (Cheng, M. et al. “NK Cell-Based Immunotherapy for Malignant Diseases.” Cellular & molecular immunology 10.3 (2013): 230–252).
In view of the claim amendments in the reply of 02/05/2026, this rejection is withdrawn.
Claims 8 and 9 are rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL in view of OSAKI and BOYDEN as applied to 1, 3, 4, 6, 7, and 21, and in further view of TREDER (WO 2016/177846 A1, published 11/10/2016).
In view of the claim amendments in the reply of 02/05/2026, this rejection is withdrawn.
Double Patenting
Claims 1, 3, 4, and 6 – 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, and 9 of U.S. Patent No. 11,510,972 (‘972) in view of LOWDELL, OSAKI, and BOYDEN.
In view of the terminal disclaimer of 02/05/2026, this rejection is withdrawn.
Claims 1, 8, and 9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims listed in the table below of U.S. Patent No. listed below in view of LOWDELL, OSAKI, and BOYDEN.
U.S. Patent No.
Claim No(s).
SEQ ID NO(s):
1
11,167,029
1, 7, 9, 16
1, 4, 5
2
11,001,633
1, 3, 4, 12
2, 61
3
11,180,558
1, 7
9
4
11,535,672
6, 9
N/A
5
9,701,750
1, 12
16
In view of the claim amendments in the reply of 02/05/2026, this rejection is withdrawn.
Claims 1, 8, and 9 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims listed in the table below of copending Application No. listed below in view of LOWDELL, OSAKI, and BOYDEN.
U.S. Application No.
Claim No(s).
SEQ ID NO(s):
1
17/235,854
1, 3, 4, 10, 15, 16, 22
2, 61
2
17/510,738
1, 7
9
3
17/807,211
1, 2, 6
13
4
18/047,917
1, 3, 12, 14
12, 13, 27, 30
In view of the claim amendments in the reply of 02/05/2026 and the abandonment of 17/235,854, this rejection is withdrawn.
NEW REJECTIONS NECESSITATED BY CLAIM AMENDMENTS
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
Claims 1, 3 – 4, 11 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL (WO 2011004201 A1, published Jan. 13, 2011, an IDS reference submitted 07/23/2021) in view of BOYDEN (US 2010/0152880 A1, published 06/17/2010, see PTO-892: Notice of References Cited of 04/17/2025), DALEY (WO 2018/201051 A1, filed 04/27/2018, published 11/01/2018; see PTO-892 submitted with this Office Action) and KUFER (WO 2013/072415 A1, published 05/23/2013; see PTO-892 submitted with this Office Action).
LOWDELL is directed to a pharmaceutical composition for direct administration to a patient in need thereof comprising previously preserved activated NK cells (see claim 1). LOWDELL discloses that NK cells lose CD 16 expression upon activation and active NK cells expressing low levels of CD 16 may be cryopreserved to maintain activity (see paragraph [0010] and claim 3). Thus, LOWDELL’s NK cells are active prior to freezing.
Although LOWDELL discloses isolated human NK cells that are active and with a modulated CD16a expression that are cryopreserved, LOWDELL does not disclose that the isolated human NK cells in a cryopreserved state are preloaded prior to freezing with a bispecific antibody.
BOYDEN is directed to compositions, methods, devices, systems, and products regarding frozen particles. See abstract. BOYDEN discloses frozen particles containing one or more biological adhesive agents (for example, bispecific antibodies or bispecific proteins) used to bind cells or tissues specifically to therapeutic targets, such as leukocytes. BOYDEN discloses that one or more biological adhesive agent is bound to a leukocyte (or other cell) in vitro prior to incorporation of the cell plus biological adhesive into the one or more frozen particle compositions. See paragraphs 1700 and 1708. BOYDEN further describes leukocytes as macrophages, monocytes, T cells, natural killer cells (NK cells). See paragraph 1698. BOYDEN also describes utilizing the frozen particles in the treatment of cancer. See BOYDEN at Examples 24 – 26, paragraphs 1707 – 1716.
Thus, BOYDEN suggests the bonding of a bispecific antibody (which BOYDEN describes as the “adhesive”) to an NK cell, rendering “wherein the bispecific antibody forms an antibody-antigen bond between the bispecific antibody and the NK cell, wherein the bond maintains the binding of the bispecific antibody on the cell surface of the NK cell during and after the cell is in the cryopreserved state” of claim 1 obvious.
However BOYDEN does not teach that the bispecific antibody that is cryopreserved with the NK cells is one that specifically binds to an NK cell receptor antigen CD 16a on the cell surface of an NK cell and a second binding domain binding to a cell surface antigen on the cell surface of a target cell.
DALEY is directed to a BCMA-targeting agent comprises an anti-BCMA antibody molecule or a BCMA ligand, wherein: the anti-BCMA antibody molecule is a multispecific (e.g., bispecific) antibody molecule that binds to BCMA and a second antigen, wherein the second antigen is CD16 (e.g., CD16A). See DALEY at claim 1.
However, none of the cited references above teach the anti-BCMA CDRs of SEQ ID NOs: 106 – 109, GAS and 111 of present claim 1.
KUFER is directed to a binding molecule comprising a first and a second binding domain, wherein the first binding domain is capable of binding to epitope clusters of BCMA, and the second binding domain is capable of binding to the T cell CD3 receptor complex. See KUFER at the abstract. KUFER teaches that It is also envisaged that the binding molecule has, in addition to its function to bind to the target molecules BCMA and CD3, a further function, which In this format, the binding molecule is a tri-or multifunctional binding molecule by targeting plasma cells through binding to BCMA, mediating cytotoxic T cell activity through CD3 binding and providing a further function such as a fully functional Fc constant domain mediating antibody-dependent cellular cytotoxicity through recruitment of effector cells like NK cells.
KUFER teaches the anti-BCMA CDRs of present SEQ ID NOs: 106 – 108 and SEQ ID NO: 109, GAS and SEQ ID NO: 111. KUFER’s SEQ ID NO: 637 teaches the CDRs of SEQ ID NOs: 106 – 108 with 100% identity, and KUFER’s SEQ ID NO: 658 teaches the CDRs of SEQ ID NO: 109, GAS and SEQ ID NO: 111 with 100% identity. See Appendix.
Because LOWDELL implicates CD16 modulation as a significant factor in the NK-cell activation of a cryopreserved, activated NK cell composition that may be used to treat cancer; BOYDEN discloses frozen particles comprising a bispecific antibody bound to an NK cell for the treatment of cancer; DALEY teaches a bispecific antibody molecule that binds to BCMA and CD16A for the treatment of cancer; and KUFER teaches the anti-BCMA CDRs of present claim 1, it would have been obvious to one having ordinary skill to arrive to the isolated human NK cells in a cryopreserved state of present claim 1.
At the effective filing date of the present claims, it would have been prima facie obvious to the person of ordinary skill in the art to arrive at the claimed invention from the disclosures of LOWDELL, BOYDEN, DALEY and KUFER. The artisan would have been motivated to make and use the isolated human NK cells of claim 1 because LOWDELL teaches cryopreserved NK cells for direct administration to a patient to treat cancer without co-administration (whether simultaneous, separate or sequential) of the activating agent (see LOWDELL at claim 1 and 24 – 25); BOYDEN teaches that NK cells and bispecific antibodies can used to bind cells or tissues specifically to therapeutic targets while frozen; DALEY teaches that a bispecific antibody targeting CD16A and BCMA effective at treating cancer; and KUFER teaches anti-BCMA CDRs that are effective at treating cancer. Thus, the artisan would have a reasonable expectation of success from the combined teachings of LOWDELL, BOYDEN, DALEY and KUFER.
Regarding claims 3 and 21, LOWDELL discloses that “the compositions can be prepared for administration as injectable dosages of a solution or suspension of the substance in a physiologically acceptable diluent with a pharmaceutical carrier that can be a sterile liquid such as sterile pyrogen free water, oils, saline, glycerol, polyethylene glycol or ethanol” (see paragraph [0098]).
Regarding claim 4, DALEY teaches antibody dose titrations for in vitro cell based assays represented here range from 0.1pM to 300nM. See DALEY at p. 193, lines 29 – 30. Thus, the amount of at least 5 nM of bispecific antibody to preload NK cells may be determined in an in vitro cell based assay as taught by DALEY. MPEP § 2144.05 (II) (A) states, “…Optimization Within Prior Art Conditions or Through Routine Experimentation…“[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to dis-cover the optimum or workable ranges by routine experimentation…”.
Regarding claim 11, KUFER teaches the sequences of SEQ ID NO: 112 and 113 with 100% identity. KUFER’s SEQ ID NO: 647 is identical to present SEQ ID NO: 112, and KUFER’s SEQ ID NO: 708 is identical to present SEQ ID NO: 113. See Appendix.
Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made.
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL in view of BOYDEN, DALEY and KUFER as applied to claims 1, 3 – 4, 11 and 21 above, and in further view CHENG (Cheng, M. et al. “NK Cell-Based Immunotherapy for Malignant Diseases.” Cellular & molecular immunology 10.3 (2013): 230–252; see PTO-892 of 04/25/2024).
The teachings of LOWDELL, BOYDEN, DALEY and KUFER With regard to claim 1, from which claim 2 depends, are discussed above and are fully incorporated here. Although LOWDELL, BOYDEN, DALEY and KUFER teach the isolated human NK cells in a cryopreserved state of present claim 1, the cited references do not expressly teach that the NK cells are from Applicant’s elected species of umbilical cord.
CHENG is a review article on NK cell-based cancer immunotherapy aims approaches to overcome NK cell paralysis. See Abstract. CHENG discloses that FcRcIIIa or CD16a enables NK cells to recognize Ab-coated target cells and trigger NK cell-mediated ADCC, resulting in rapid NK-cell activation and degranulation. See p. 235, left column, ADCC.
Regarding claim 2, CHENG discloses that NK cells may be isolated from Applicant’s elected species of umbilical cords (see Cord blood-derived NK cells, p. 236).
At the effective filing date of the present claims, it would have been prima facie obvious to the person of ordinary skill in the art to arrive at the claimed invention from the disclosures of LOWDELL, BOYDEN, DALEY and KUFER. The artisan would have been motivated to make and use the isolated human NK cells of claim 1 because LOWDELL teaches cryopreserved NK cells for direct administration to a patient to treat cancer without co-administration (whether simultaneous, separate or sequential) of the activating agent (see LOWDELL at claim 1 and 24 – 25); BOYDEN teaches that NK cells and bispecific antibodies can used to bind cells or tissues specifically to therapeutic targets while frozen; DALEY teaches that a bispecific antibody targeting CD16A and BCMA effective at treating cancer; KUFER teaches anti-BCMA CDRs that are effective at treating cancer; and CHENG teaches that NK cell-based cancer immunotherapy is derived from umbilical cords. Thus, the artisan would have a reasonable expectation of success from the combined teachings of LOWDELL, BOYDEN, DALEY, KUFER and CHENG.
Claims 8 and 9 are rejected under 35 U.S.C. 103 as being unpatentable over LOWDELL in view of BOYDEN, DALEY and KUFER as applied to claims 1, 3 – 4, 11 and 21 above, and further in view of TREDER (WO 2016/177846 A1, published 11/10/2016; see PTO-892 of 04/25/2024).
The teachings of LOWDELL, BOYDEN, DALEY and KUFER With regard to claim 1, from which claims 8 and 9 depend, either directly or indirectly, are discussed above and are fully incorporated here. Although LOWDELL, BOYDEN, DALEY and KUFER teach the isolated human NK cells in a cryopreserved state of present claim 1, the cited references do not expressly teach the anti-CD16a CDRs of present claim 8 or the anti-CD16a VH and VL of present claim 9.
TREDER is directed to a multifunctional antibody having specificity for CD30 and CD16A (see Abstract). TREDER teaches a bispecific CD30/CD16A tandem diabody (TandAb®) binds NK-cells via CD16A and has a second binding domain for CD30, a cancer-specific target that recruits and redirects the NK- cells to CD30+ tumor cells and binds both targets with high affinity, establishing a bridge whereby the NK-cells are activated and redirected to kill the tumor cells. See TREDER at the Description, third paragraph.
Regarding claims 8 and 9, Applicant elected a first binding domain with (a) CDRs of SEQ ID NOs: 29 – 34 and with a VH and VL of SEQ ID NOs: 35 and 36, and TREDER discloses the sequences of SEQ ID NOs: 29 – 36 with 100% identity. TREDER’s SEQ ID NO: 2 is identical to elected SEQ ID NO: 35 of claim 9 and includes the CDRs of SEQ ID NOs: 29 – 31. TREDER’s SEQ ID NO: 5 is identical to elected SEQ ID NO: 36 of claim 9 and includes the CDRs of SEQ ID NOs: 32 – 34. See Appendix.
At the effective filing date of the present claims, it would have been prima facie obvious to the person of ordinary skill in the art to arrive at the claimed invention from the disclosures of LOWDELL, BOYDEN, DALEY, KUFER and TREDER. The artisan would have been motivated to make and use the isolated human NK cells of claim 1 because LOWDELL teaches cryopreserved NK cells for direct administration to a patient to treat cancer without co-administration (whether simultaneous, separate or sequential) of the activating agent (see LOWDELL at claim 1 and 24 – 25); BOYDEN teaches that NK cells and bispecific antibodies can used to bind cells or tissues specifically to therapeutic targets while frozen; DALEY teaches that a bispecific antibody targeting CD16A and BCMA effective at treating cancer; KUFER teaches anti-BCMA CDRs that are effective at treating cancer; and TREDER teaches a bispecific CD16A tandem diabody that binds NK-cells via CD16A redirects the NK- cells tumor cells and binds both targets with high affinity, establishing a bridge whereby the NK-cells are activated and redirected to kill the tumor cells. The artisan would have a reasonable expectation of success from the combined teachings of LOWDELL, BOYDEN, DALEY, KUFER and TREDER.
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 – 4, 8 – 9, 11 and 21 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 – 14 of U.S. Patent No. 11,001,633 in view of LOWDELL, BOYDEN, DALEY, KUFER, CHENG and TREDER.
Patented claim 1 recites a multi specific antigen-binding protein comprising: a) two B cell maturation antigen (BCMA) antigen-binding moieties . . . and b) two CD16A antigen-binding moieties . . .
Patented claim 4 recites that the protein is a tetramer comprising a first polypeptide chain consisting of the amino acid sequence set forth in SEQ ID NO: 61, and a second polypeptide chain consisting of the amino acid sequence set forth in SEQ ID NO: 62.
Patented 5 recites that the two BCMA antigen-binding moieties each comprise: a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO: 65 and/or a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO: 66.
Patented SEQ ID NOs: 61 and 65 teaches the CDRs of SEQ ID NOs: 106, 107 and 108 with 100 % identity, and patented SEQ ID NOs: 62 and 65 teaches the CDRs of SEQ ID NO: 109, GAS and SEQ ID NO: 111. See Appendix.
The main difference between the present claims and the patented claims is that the present claims recites isolated human NK cells in a cryopreserved state and the anti-CD16a CDRs and VH and VL of present claims 8 and 9. However, LOWDELL, BOYDEN and TREDER teach this difference. The teachings of LOWDELL, BOYDEN, DALEY, KUFER, CHENG and TREDER, and how they relate to the claims, are set forth in the rejection under 35 USC 103 above.
Because the patented claims recite a multispecific antigen-binding protein with binding sites targeting CD16A and BCMA, LOWDELL teaches effective cryopreserved NK cells with anti-tumor activity (see claim 16), and TREDER teaches anti-CD16a CDRs, it would have been obvious to one having ordinary skill in the art to preload LOWDELL’s cells with the antibody of the patented claims.
Allowable Subject Matter
Claim 12 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Applicant’s elected bispecific antibody having the sequences of SEQ ID NOs: 162 and 163 is free of the art.
Conclusion
Claims 1 – 4 , 8 – 11 and 21 are rejected, and claim 12 is objected to.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
/ESTELLA M. GUSTILO/Examiner, Art Unit 1646
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678
APPENDIX
Alignment with SEQ ID NOs: 106, 107 and 108
BAO84664
(NOTE: this sequence has 17 duplicates in the database searched.
See complete list at the end of this report)
ID BAO84664 standard; protein; 121 AA.
XX
AC BAO84664;
XX
DT 18-JUL-2013 (first entry)
XX
DE Anti-BCMA antibody heavy chain variable region (VH), SEQ: 637.
XX
KW APRIL receptor; B-cell maturation antigen; BCMA; CD269; TNFRSF17 protein;
KW amyloidosis; antibody; antibody production; antibody therapy;
KW autoimmune disease; bispecific antibody; cytostatic; endocrine-gen.;
KW heavy chain disease; heavy chain variable region; hematological-gen.;
KW immunomodulator; immunosuppressive; leukemia; macroglobulinemia;
KW metabolic-gen.; multiple myeloma; osteopathic; osteosclerosis;
KW paraproteinemia; plasmacytoma; prophylactic to disease;
KW rheumatoid arthritis; systemic lupus erythematosus; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2013072415-A1.
XX
CC PD 23-MAY-2013.
XX
CC PF 15-NOV-2012; 2012WO-EP072730.
XX
PR 15-NOV-2011; 2011US-0560144P.
PR 15-NOV-2011; 2011US-0560149P.
PR 15-NOV-2011; 2011US-0560162P.
PR 15-NOV-2011; 2011US-0560178P.
PR 15-NOV-2011; 2011US-0560183P.
PR 24-MAY-2012; 2012US-0651474P.
PR 24-MAY-2012; 2012US-0651486P.
XX
CC PA (AMGE-) AMGEN RES MUNICH GMBH.
CC PA (BOEH ) BOEHRINGER INGELHEIM INT GMBH.
XX
CC PI Kufer P, Raum T, Hoffmann P, Kischel R, Lutterbuese R, Rau D;
CC PI Adam P, Borges E, Hebeis B, Hipp S;
XX
DR WPI; 2013-H93864/36.
XX
CC PT New binding molecule for B-cell maturation antigen (BCMA) and CD3, useful
CC PT for preventing, treating or ameliorating plasma cell disorders, B cell
CC PT disorders that correlate with BCMA expression and autoimmune diseases.
XX
CC PS Disclosure; SEQ ID NO 637; 272pp; English.
XX
CC The present invention relates to a novel bispecific binding molecule
CC comprising a first and a second binding domain, wherein the first binding
CC domain is capable of binding to epitope clusters of B-cell maturation
CC antigen (BCMA, TNFRSF17, CD269) and the second binding domain is capable
CC of binding to the T cell CD3 receptor complex. The binding molecule
CC herein comprises single chain Fv (scFv) 2, scFv-single domain monoclonal
CC antibody (mAb), single domain mAb 2, diabodies and oligomers. The
CC bispecific binding molecule is used in the prevention, treatment or
CC amelioration of a disease selected from the group consisting of plasma
CC cell disorders, other B cell disorders that correlate with BCMA
CC expression and autoimmune diseases. The plasma cell disorder is selected
CC from the group consisting of multiple myeloma, plasmacytoma, plasma cell
CC leukemia, macroglobulinemia, amyloidosis, Waldenstrom's macroglobulinemia
CC , solitary bone plasmacytoma, extramedullary plasmacytoma, osteosclerotic
CC myeloma, heavy chain diseases, monoclonal gammopathy of undetermined
CC significance and smoldering multiple myeloma. The autoimmune disease is
CC systemic lupus erythematodes or rheumatoid arthritis. The invention
CC independently claims: (a) a nucleic acid sequence encoding the binding
CC molecule; (b) a vector comprising the nucleic acid sequence; (c) a host
CC cell transformed or transfected with the nucleic acid sequence; (d) a
CC pharmaceutical composition comprising the binding molecule; and (e) a
CC method for generating the antibody which is capable of binding BCMA. The
CC present sequence represents an amino acid sequence of the anti-BCMA
CC antibody heavy chain variable region (VH).
XX
SQ Sequence 121 AA;
Query Match 84.5%; Score 139.5; Length 121;
Best Local Similarity 35.3%;
Matches 30; Conservative 0; Mismatches 0; Indels 55; Gaps 2;
Qy 1 GFTFSNYD-----------------ISTRGDIT--------------------------- 16
|||||||| ||||||||
Db 26 GFTFSNYDMAWVRQAPGKGLEWVSSISTRGDITSYRDSVKGRFTISRDNSKNTLYLQMNS 85
Qy 17 -----------ARQDYYTDYMGFAY 30
||||||||||||||
Db 86 LRAEDTAVYYCARQDYYTDYMGFAY 110
Alignment with SEQ ID NO: 109, GAS and SEQ ID NO: 111
BAO84685
(NOTE: this sequence has 5 duplicates in the database searched.
See complete list at the end of this report)
ID BAO84685 standard; protein; 107 AA.
XX
AC BAO84685;
XX
DT 18-JUL-2013 (first entry)
XX
DE Anti-BCMA antibody light chain variable region (VL), SEQ: 658.
XX
KW APRIL receptor; B-cell maturation antigen; BCMA; CD269; TNFRSF17 protein;
KW amyloidosis; antibody; antibody production; antibody therapy;
KW autoimmune disease; bispecific antibody; cytostatic; endocrine-gen.;
KW heavy chain disease; hematological-gen.; immunomodulator;
KW immunosuppressive; leukemia; light chain variable region;
KW macroglobulinemia; metabolic-gen.; multiple myeloma; osteopathic;
KW osteosclerosis; paraproteinemia; plasmacytoma; prophylactic to disease;
KW rheumatoid arthritis; systemic lupus erythematosus; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2013072415-A1.
XX
CC PD 23-MAY-2013.
XX
CC PF 15-NOV-2012; 2012WO-EP072730.
XX
PR 15-NOV-2011; 2011US-0560144P.
PR 15-NOV-2011; 2011US-0560149P.
PR 15-NOV-2011; 2011US-0560162P.
PR 15-NOV-2011; 2011US-0560178P.
PR 15-NOV-2011; 2011US-0560183P.
PR 24-MAY-2012; 2012US-0651474P.
PR 24-MAY-2012; 2012US-0651486P.
XX
CC PA (AMGE-) AMGEN RES MUNICH GMBH.
CC PA (BOEH ) BOEHRINGER INGELHEIM INT GMBH.
XX
CC PI Kufer P, Raum T, Hoffmann P, Kischel R, Lutterbuese R, Rau D;
CC PI Adam P, Borges E, Hebeis B, Hipp S;
XX
DR WPI; 2013-H93864/36.
XX
CC PT New binding molecule for B-cell maturation antigen (BCMA) and CD3, useful
CC PT for preventing, treating or ameliorating plasma cell disorders, B cell
CC PT disorders that correlate with BCMA expression and autoimmune diseases.
XX
CC PS Disclosure; SEQ ID NO 658; 272pp; English.
XX
CC The present invention relates to a novel bispecific binding molecule
CC comprising a first and a second binding domain, wherein the first binding
CC domain is capable of binding to epitope clusters of B-cell maturation
CC antigen (BCMA, TNFRSF17, CD269) and the second binding domain is capable
CC of binding to the T cell CD3 receptor complex. The binding molecule
CC herein comprises single chain Fv (scFv) 2, scFv-single domain monoclonal
CC antibody (mAb), single domain mAb 2, diabodies and oligomers. The
CC bispecific binding molecule is used in the prevention, treatment or
CC amelioration of a disease selected from the group consisting of plasma
CC cell disorders, other B cell disorders that correlate with BCMA
CC expression and autoimmune diseases. The plasma cell disorder is selected
CC from the group consisting of multiple myeloma, plasmacytoma, plasma cell
CC leukemia, macroglobulinemia, amyloidosis, Waldenstrom's macroglobulinemia
CC , solitary bone plasmacytoma, extramedullary plasmacytoma, osteosclerotic
CC myeloma, heavy chain diseases, monoclonal gammopathy of undetermined
CC significance and smoldering multiple myeloma. The autoimmune disease is
CC systemic lupus erythematodes or rheumatoid arthritis. The invention
CC independently claims: (a) a nucleic acid sequence encoding the binding
CC molecule; (b) a vector comprising the nucleic acid sequence; (c) a host
CC cell transformed or transfected with the nucleic acid sequence; (d) a
CC pharmaceutical composition comprising the binding molecule; and (e) a
CC method for generating the antibody which is capable of binding BCMA. The
CC present sequence represents an amino acid sequence of the anti-BCMA
CC antibody light chain variable region (VL).
XX
SQ Sequence 107 AA;
Query Match 75.0%; Score 75.7; Length 107;
Best Local Similarity 25.4%;
Matches 18; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 EDIYNG-----------------GAS---------------------------------- 9
|||||| |||
Db 27 EDIYNGLAWYQQKPGKAPKLLIYGASSLQDGVPSRFSGSGSGTDYTLTISSLQPEDEATY 86
Qy 10 --AGPHKYPLT 18
|||||||||
Db 87 YCAGPHKYPLT 97
Alignment with SEQ ID NO: 112
BAO84674
(NOTE: this sequence has 34 duplicates in the database searched.
See complete list at the end of this report)
ID BAO84674 standard; protein; 121 AA.
XX
AC BAO84674;
XX
DT 18-JUL-2013 (first entry)
XX
DE Anti-BCMA antibody heavy chain variable region (VH), SEQ: 647.
XX
KW APRIL receptor; B-cell maturation antigen; BCMA; CD269; TNFRSF17 protein;
KW amyloidosis; antibody; antibody production; antibody therapy;
KW autoimmune disease; bispecific antibody; cytostatic; endocrine-gen.;
KW heavy chain disease; heavy chain variable region; hematological-gen.;
KW immunomodulator; immunosuppressive; leukemia; macroglobulinemia;
KW metabolic-gen.; multiple myeloma; osteopathic; osteosclerosis;
KW paraproteinemia; plasmacytoma; prophylactic to disease;
KW rheumatoid arthritis; systemic lupus erythematosus; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2013072415-A1.
XX
CC PD 23-MAY-2013.
XX
CC PF 15-NOV-2012; 2012WO-EP072730.
XX
PR 15-NOV-2011; 2011US-0560144P.
PR 15-NOV-2011; 2011US-0560149P.
PR 15-NOV-2011; 2011US-0560162P.
PR 15-NOV-2011; 2011US-0560178P.
PR 15-NOV-2011; 2011US-0560183P.
PR 24-MAY-2012; 2012US-0651474P.
PR 24-MAY-2012; 2012US-0651486P.
XX
CC PA (AMGE-) AMGEN RES MUNICH GMBH.
CC PA (BOEH ) BOEHRINGER INGELHEIM INT GMBH.
XX
CC PI Kufer P, Raum T, Hoffmann P, Kischel R, Lutterbuese R, Rau D;
CC PI Adam P, Borges E, Hebeis B, Hipp S;
XX
DR WPI; 2013-H93864/36.
XX
CC PT New binding molecule for B-cell maturation antigen (BCMA) and CD3, useful
CC PT for preventing, treating or ameliorating plasma cell disorders, B cell
CC PT disorders that correlate with BCMA expression and autoimmune diseases.
XX
CC PS Disclosure; SEQ ID NO 647; 272pp; English.
XX
CC The present invention relates to a novel bispecific binding molecule
CC comprising a first and a second binding domain, wherein the first binding
CC domain is capable of binding to epitope clusters of B-cell maturation
CC antigen (BCMA, TNFRSF17, CD269) and the second binding domain is capable
CC of binding to the T cell CD3 receptor complex. The binding molecule
CC herein comprises single chain Fv (scFv) 2, scFv-single domain monoclonal
CC antibody (mAb), single domain mAb 2, diabodies and oligomers. The
CC bispecific binding molecule is used in the prevention, treatment or
CC amelioration of a disease selected from the group consisting of plasma
CC cell disorders, other B cell disorders that correlate with BCMA
CC expression and autoimmune diseases. The plasma cell disorder is selected
CC from the group consisting of multiple myeloma, plasmacytoma, plasma cell
CC leukemia, macroglobulinemia, amyloidosis, Waldenstrom's macroglobulinemia
CC , solitary bone plasmacytoma, extramedullary plasmacytoma, osteosclerotic
CC myeloma, heavy chain diseases, monoclonal gammopathy of undetermined
CC significance and smoldering multiple myeloma. The autoimmune disease is
CC systemic lupus erythematodes or rheumatoid arthritis. The invention
CC independently claims: (a) a nucleic acid sequence encoding the binding
CC molecule; (b) a vector comprising the nucleic acid sequence; (c) a host
CC cell transformed or transfected with the nucleic acid sequence; (d) a
CC pharmaceutical composition comprising the binding molecule; and (e) a
CC method for generating the antibody which is capable of binding BCMA. The
CC present sequence represents an amino acid sequence of the anti-BCMA
CC antibody heavy chain variable region (VH).
XX
SQ Sequence 121 AA;
Query Match 100.0%; Score 637; Length 121;
Best Local Similarity 100.0%;
Matches 121; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYDMAWVRQAPGKGLEWVSSISTRGDITSY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYDMAWVRQAPGKGLEWVSSISTRGDITSY 60
Qy 61 RDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARQDYYTDYMGFAYWGQGTLVTVS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARQDYYTDYMGFAYWGQGTLVTVS 120
Qy 121 S 121
|
Db 121 S 121
Alignment with SEQ ID NO: 113
BAO84735
(NOTE: this sequence has 10 duplicates in the database searched.
See complete list at the end of this report)
ID BAO84735 standard; protein; 107 AA.
XX
AC BAO84735;
XX
DT 18-JUL-2013 (first entry)
XX
DE Anti-BCMA antibody light chain variable region (VL), SEQ: 708.
XX
KW APRIL receptor; B-cell maturation antigen; BCMA; CD269; TNFRSF17 protein;
KW amyloidosis; antibody; antibody production; antibody therapy;
KW autoimmune disease; bispecific antibody; cytostatic; endocrine-gen.;
KW heavy chain disease; hematological-gen.; immunomodulator;
KW immunosuppressive; leukemia; light chain variable region;
KW macroglobulinemia; metabolic-gen.; multiple myeloma; osteopathic;
KW osteosclerosis; paraproteinemia; plasmacytoma; prophylactic to disease;
KW rheumatoid arthritis; systemic lupus erythematosus; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2013072415-A1.
XX
CC PD 23-MAY-2013.
XX
CC PF 15-NOV-2012; 2012WO-EP072730.
XX
PR 15-NOV-2011; 2011US-0560144P.
PR 15-NOV-2011; 2011US-0560149P.
PR 15-NOV-2011; 2011US-0560162P.
PR 15-NOV-2011; 2011US-0560178P.
PR 15-NOV-2011; 2011US-0560183P.
PR 24-MAY-2012; 2012US-0651474P.
PR 24-MAY-2012; 2012US-0651486P.
XX
CC PA (AMGE-) AMGEN RES MUNICH GMBH.
CC PA (BOEH ) BOEHRINGER INGELHEIM INT GMBH.
XX
CC PI Kufer P, Raum T, Hoffmann P, Kischel R, Lutterbuese R, Rau D;
CC PI Adam P, Borges E, Hebeis B, Hipp S;
XX
DR WPI; 2013-H93864/36.
XX
CC PT New binding molecule for B-cell maturation antigen (BCMA) and CD3, useful
CC PT for preventing, treating or ameliorating plasma cell disorders, B cell
CC PT disorders that correlate with BCMA expression and autoimmune diseases.
XX
CC PS Disclosure; SEQ ID NO 708; 272pp; English.
XX
CC The present invention relates to a novel bispecific binding molecule
CC comprising a first and a second binding domain, wherein the first binding
CC domain is capable of binding to epitope clusters of B-cell maturation
CC antigen (BCMA, TNFRSF17, CD269) and the second binding domain is capable
CC of binding to the T cell CD3 receptor complex. The binding molecule
CC herein comprises single chain Fv (scFv) 2, scFv-single domain monoclonal
CC antibody (mAb), single domain mAb 2, diabodies and oligomers. The
CC bispecific binding molecule is used in the prevention, treatment or
CC amelioration of a disease selected from the group consisting of plasma
CC cell disorders, other B cell disorders that correlate with BCMA
CC expression and autoimmune diseases. The plasma cell disorder is selected
CC from the group consisting of multiple myeloma, plasmacytoma, plasma cell
CC leukemia, macroglobulinemia, amyloidosis, Waldenstrom's macroglobulinemia
CC , solitary bone plasmacytoma, extramedullary plasmacytoma, osteosclerotic
CC myeloma, heavy chain diseases, monoclonal gammopathy of undetermined
CC significance and smoldering multiple myeloma. The autoimmune disease is
CC systemic lupus erythematodes or rheumatoid arthritis. The invention
CC independently claims: (a) a nucleic acid sequence encoding the binding
CC molecule; (b) a vector comprising the nucleic acid sequence; (c) a host
CC cell transformed or transfected with the nucleic acid sequence; (d) a
CC pharmaceutical composition comprising the binding molecule; and (e) a
CC method for generating the antibody which is capable of binding BCMA. The
CC present sequence represents an amino acid sequence of the anti-BCMA
CC antibody light chain variable region (VL).
XX
SQ Sequence 107 AA;
Query Match 100.0%; Score 558; Length 107;
Best Local Similarity 100.0%;
Matches 107; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 AIQMTQSPSSLSASVGDRVTITCRASEDIYNGLAWYQQKPGKAPKLLIYGASSLQDGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 AIQMTQSPSSLSASVGDRVTITCRASEDIYNGLAWYQQKPGKAPKLLIYGASSLQDGVPS 60
Qy 61 RFSGSGSGTEFTLTISSLQPEDEATYYCAGPHKYPLTFGGGTKVEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTEFTLTISSLQPEDEATYYCAGPHKYPLTFGGGTKVEIK 107
Alignment with SEQ ID NOs: 29 – 31
BDI57124
(NOTE: this sequence has 30 duplicates in the database searched.
See complete list at the end of this report)
ID BDI57124 standard; protein; 120 AA.
XX
AC BDI57124;
XX
DT 29-DEC-2016 (first entry)
XX
DE Anti-CD16A antibody heavy chain variable region, SEQ ID 2.
XX
KW CD16A; antibody; cancer; cytostatic; heavy chain variable region;
KW hematological-gen.; hodgkins disease; immunomodulator; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2016177846-A1.
XX
CC PD 10-NOV-2016.
XX
CC PF 04-MAY-2016; 2016WO-EP060113.
XX
PR 04-MAY-2015; 2015EP-00166303.
PR 25-JAN-2016; 2016EP-00152650.
XX
CC PA (AFFI-) AFFIMED GMBH.
XX
CC PI Treder M, Reusch U, Marschner J, Knackmuss S, Rajasekaran N;
CC PI Kohrt H;
XX
DR WPI; 2016-699668/81.
XX
CC PT New combination of multifunctional antibody having specificity for
CC PT cluster of differentiation 30 (CD30), and CD16A, and anti-programmed
CC PT death 1 antibody used for treating tumor, preferably Hodgkin lymphoma.
XX
CC PS Disclosure; SEQ ID NO 2; 29pp; English.
XX
CC The present invention relates to a novel combination of (i) a
CC multifunctional antibody having specificity for CD30, and CD16A, and (ii)
CC an anti-programmed death ligand-1 (PD-1) antibody, useful for treating
CC tumor, preferably Hodgkin lymphoma. The combination is useful for
CC increasing innate immune response as compared with that of
CC multifunctional antibody having specificity for CD30 and CD16A alone. The
CC increased innate immune response is an increased intratumoral cell
CC infiltration of innate cells into tumor. The combination is also used for
CC increasing intratumoral infiltration of macrophages, dendritic cells and
CC natural killer (NK)-cells, and CD4 positive and CD8 positive cells. The
CC present sequence is an anti-CD16A antibody heavy chain variable region,
CC which is used in the combination of the invention for treating tumor.
XX
SQ Sequence 120 AA;
Query Match 84.3%; Score 136.5; Length 120;
Best Local Similarity 34.5%;
Matches 29; Conservative 0; Mismatches 0; Indels 55; Gaps 2;
Qy 1 GYTFTSYY-----------------INPSGGST--------------------------- 16
|||||||| ||||||||
Db 26 GYTFTSYYMHWVRQAPGQGLEWMGIINPSGGSTSYAQKFQGRVTMTRDTSTSTVYMELSS 85
Qy 17 -----------ARGSAYYYDFADY 29
|||||||||||||
Db 86 LRSEDTAVYYCARGSAYYYDFADY 109
Alignment with SEQ ID NO: 35
BDI57124
(NOTE: this sequence has 30 duplicates in the database searched.
See complete list at the end of this report)
ID BDI57124 standard; protein; 120 AA.
XX
AC BDI57124;
XX
DT 29-DEC-2016 (first entry)
XX
DE Anti-CD16A antibody heavy chain variable region, SEQ ID 2.
XX
KW CD16A; antibody; cancer; cytostatic; heavy chain variable region;
KW hematological-gen.; hodgkins disease; immunomodulator; therapeutic.
XX
OS Unidentified.
XX
CC PN WO2016177846-A1.
XX
CC PD 10-NOV-2016.
XX
CC PF 04-MAY-2016; 2016WO-EP060113.
XX
PR 04-MAY-2015; 2015EP-00166303.
PR 25-JAN-2016; 2016EP-00152650.
XX
CC PA (AFFI-) AFFIMED GMBH.
XX
CC PI Treder M, Reusch U, Marschner J, Knackmuss S, Rajasekaran N;
CC PI Kohrt H;
XX
DR WPI; 2016-699668/81.
XX
CC PT New combination of multifunctional antibody having specificity for
CC PT cluster of differentiation 30 (CD30), and CD16A, and anti-programmed
CC PT death 1 antibody used for treating tumor, preferably Hodgkin lymphoma.
XX
CC PS Disclosure; SEQ ID NO 2; 29pp; English.
XX
CC The present invention relates to a novel combination of (i) a
CC multifunctional antibody having specificity for CD30, and CD16A, and (ii)
CC an anti-programmed death ligand-1 (PD-1) antibody, useful for treating
CC tumor, preferably Hodgkin lymphoma. The combination is useful for
CC increasing innate immune response as compared with that of
CC multifunctional antibody having specificity for CD30 and CD16A alone. The
CC increased innate immune response is an increased intratumoral cell
CC infiltration of innate cells into tumor. The combination is also used for
CC increasing intratumoral infiltration of macrophages, dendritic cells and
CC natural killer (NK)-cells, and CD4 positive and CD8 positive cells. The
CC present sequence is an anti-CD16A antibody heavy chain variable region,
CC which is used in the combination of the invention for treating tumor.
XX
SQ Sequence 120 AA;
Query Match 100.0%; Score 635; Length 120;
Best Local Similarity 100.0%;
Matches 120; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVQSGAEVKKPGESLKVSCKASGYTFTSYYMHWVRQAPGQGLEWMGIINPSGGSTSY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAEVKKPGESLKVSCKASGYTFTSYYMHWVRQAPGQGLEWMGIINPSGGSTSY 60
Qy 61 AQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARGSAYYYDFADYWGQGTLVTVSS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARGSAYYYDFADYWGQGTLVTVSS 120
Alignment with SEQ ID NO: 32, QDN, SEQ ID NO: 34
BDI57125
(NOTE: this sequence has 38 duplicates in the database searched.
See complete list at the end of this report)
ID BDI57125 standard; protein; 106 AA.
XX
AC BDI57125;
XX
DT 29-DEC-2016 (first entry)
XX
DE Anti-CD16A antibody light chain variable region, SEQ ID 5.
XX
KW CD16A; antibody; cancer; cytostatic; hematological-gen.;
KW hodgkins disease; immunomodulator; light chain variable region;
KW therapeutic.
XX
OS Unidentified.
XX
CC PN WO2016177846-A1.
XX
CC PD 10-NOV-2016.
XX
CC PF 04-MAY-2016; 2016WO-EP060113.
XX
PR 04-MAY-2015; 2015EP-00166303.
PR 25-JAN-2016; 2016EP-00152650.
XX
CC PA (AFFI-) AFFIMED GMBH.
XX
CC PI Treder M, Reusch U, Marschner J, Knackmuss S, Rajasekaran N;
CC PI Kohrt H;
XX
DR WPI; 2016-699668/81.
XX
CC PT New combination of multifunctional antibody having specificity for
CC PT cluster of differentiation 30 (CD30), and CD16A, and anti-programmed
CC PT death 1 antibody used for treating tumor, preferably Hodgkin lymphoma.
XX
CC PS Claim 9; SEQ ID NO 5; 29pp; English.
XX
CC The present invention relates to a novel combination of (i) a
CC multifunctional antibody having specificity for CD30, and CD16A, and (ii)
CC an anti-programmed death ligand-1 (PD-1) antibody, useful for treating
CC tumor, preferably Hodgkin lymphoma. The combination is useful for
CC increasing innate immune response as compared with that of
CC multifunctional antibody having specificity for CD30 and CD16A alone. The
CC increased innate immune response is an increased intratumoral cell
CC infiltration of innate cells into tumor. The combination is also used for
CC increasing intratumoral infiltration of macrophages, dendritic cells and
CC natural killer (NK)-cells, and CD4 positive and CD8 positive cells. The
CC present sequence is an anti-CD16A antibody light chain variable region,
CC which is used in the combination of the invention for treating tumor.
XX
SQ Sequence 106 AA;
Query Match 74.4%; Score 73.7; Length 106;
Best Local Similarity 25.4%;
Matches 18; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 NIGSKN-----------------QDN---------------------------------- 9
|||||| |||
Db 26 NIGSKNVHWYQQRPGQSPVLVIYQDNKRPSGIPERFSGSNSGNTATLTISGTQAMDEADY 85
Qy 10 --QVWDNYSVL 18
|||||||||
Db 86 YCQVWDNYSVL 96
Alignment with SEQ ID NO: 36
BDI57125
(NOTE: this sequence has 38 duplicates in the database searched.
See complete list at the end of this report)
ID BDI57125 standard; protein; 106 AA.
XX
AC BDI57125;
XX
DT 29-DEC-2016 (first entry)
XX
DE Anti-CD16A antibody light chain variable region, SEQ ID 5.
XX
KW CD16A; antibody; cancer; cytostatic; hematological-gen.;
KW hodgkins disease; immunomodulator; light chain variable region;
KW therapeutic.
XX
OS Unidentified.
XX
CC PN WO2016177846-A1.
XX
CC PD 10-NOV-2016.
XX
CC PF 04-MAY-2016; 2016WO-EP060113.
XX
PR 04-MAY-2015; 2015EP-00166303.
PR 25-JAN-2016; 2016EP-00152650.
XX
CC PA (AFFI-) AFFIMED GMBH.
XX
CC PI Treder M, Reusch U, Marschner J, Knackmuss S, Rajasekaran N;
CC PI Kohrt H;
XX
DR WPI; 2016-699668/81.
XX
CC PT New combination of multifunctional antibody having specificity for
CC PT cluster of differentiation 30 (CD30), and CD16A, and anti-programmed
CC PT death 1 antibody used for treating tumor, preferably Hodgkin lymphoma.
XX
CC PS Claim 9; SEQ ID NO 5; 29pp; English.
XX
CC The present invention relates to a novel combination of (i) a
CC multifunctional antibody having specificity for CD30, and CD16A, and (ii)
CC an anti-programmed death ligand-1 (PD-1) antibody, useful for treating
CC tumor, preferably Hodgkin lymphoma. The combination is useful for
CC increasing innate immune response as compared with that of
CC multifunctional antibody having specificity for CD30 and CD16A alone. The
CC increased innate immune response is an increased intratumoral cell
CC infiltration of innate cells into tumor. The combination is also used for
CC increasing intratumoral infiltration of macrophages, dendritic cells and
CC natural killer (NK)-cells, and CD4 positive and CD8 positive cells. The
CC present sequence is an anti-CD16A antibody light chain variable region,
CC which is used in the combination of the invention for treating tumor.
XX
SQ Sequence 106 AA;
Query Match 100.0%; Score 566; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SYVLTQPSSVSVAPGQTATISCGGHNIGSKNVHWYQQRPGQSPVLVIYQDNKRPSGIPER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 SYVLTQPSSVSVAPGQTATISCGGHNIGSKNVHWYQQRPGQSPVLVIYQDNKRPSGIPER 60
Qy 61 FSGSNSGNTATLTISGTQAMDEADYYCQVWDNYSVLFGGGTKLTVL 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSGSNSGNTATLTISGTQAMDEADYYCQVWDNYSVLFGGGTKLTVL 106
Alignment with SEQ ID NOs: 106, 107 and 109
US-16-714-396-61
Sequence 61, US/16714396
Patent No. 11001633
GENERAL INFORMATION
APPLICANT: AFFIMED GMBH
TITLE OF INVENTION: NK CELL ENGAGING ANTIBODY FUSION CONSTRUCTS
FILE REFERENCE: 087353.0106
CURRENT APPLICATION NUMBER: US/16/714,396
CURRENT FILING DATE: 2019-12-13
PRIOR APPLICATION NUMBER: PCT/IB2019/053040
PRIOR FILING DATE: 2019-04-12
PRIOR APPLICATION NUMBER: EP 18190661.1
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18190662.9
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18167384.9
PRIOR FILING DATE: 2018-04-13
PRIOR APPLICATION NUMBER: EP 18167385.6
PRIOR FILING DATE: 2018-04-13
NUMBER OF SEQ ID NOS: 136
SEQ ID NO 61
LENGTH: 727
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Description of Artificial Sequence: Synthetic
polypeptide"
Query Match 84.5%; Score 139.5; Length 727;
Best Local Similarity 35.3%;
Matches 30; Conservative 0; Mismatches 0; Indels 55; Gaps 2;
Qy 1 GFTFSNYD-----------------ISTRGDIT--------------------------- 16
|||||||| ||||||||
Db 26 GFTFSNYDMAWVRQAPGKGLEWVSSISTRGDITSYRDSVKGRFTISRDNSKNTLYLQMNS 85
Qy 17 -----------ARQDYYTDYMGFAY 30
||||||||||||||
Db 86 LRAEDTAVYYCARQDYYTDYMGFAY 110
US-16-714-396-65
Filing date in PALM: 2019-12-13
Sequence 65, US/16714396
Patent No. 11001633
GENERAL INFORMATION
APPLICANT: AFFIMED GMBH
TITLE OF INVENTION: NK CELL ENGAGING ANTIBODY FUSION CONSTRUCTS
FILE REFERENCE: 087353.0106
CURRENT APPLICATION NUMBER: US/16/714,396
CURRENT FILING DATE: 2019-12-13
PRIOR APPLICATION NUMBER: PCT/IB2019/053040
PRIOR FILING DATE: 2019-04-12
PRIOR APPLICATION NUMBER: EP 18190661.1
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18190662.9
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18167384.9
PRIOR FILING DATE: 2018-04-13
PRIOR APPLICATION NUMBER: EP 18167385.6
PRIOR FILING DATE: 2018-04-13
NUMBER OF SEQ ID NOS: 136
SEQ ID NO 65
LENGTH: 121
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Description of Artificial Sequence: Synthetic
polypeptide"
ALIGNMENT:
Query Match 84.5%; Score 139.5; Length 121;
Best Local Similarity 35.3%;
Matches 30; Conservative 0; Mismatches 0; Indels 55; Gaps 2;
Qy 1 GFTFSNYD-----------------ISTRGDIT--------------------------- 16
|||||||| ||||||||
Db 26 GFTFSNYDMAWVRQAPGKGLEWVSSISTRGDITSYRDSVKGRFTISRDNSKNTLYLQMNS 85
Qy 17 -----------ARQDYYTDYMGFAY 30
||||||||||||||
Db 86 LRAEDTAVYYCARQDYYTDYMGFAY 110
Alignment with SEQ ID NO: 109, GAS and 111
US-16-714-396-62
Sequence 62, US/16714396
Patent No. 11001633
GENERAL INFORMATION
APPLICANT: AFFIMED GMBH
TITLE OF INVENTION: NK CELL ENGAGING ANTIBODY FUSION CONSTRUCTS
FILE REFERENCE: 087353.0106
CURRENT APPLICATION NUMBER: US/16/714,396
CURRENT FILING DATE: 2019-12-13
PRIOR APPLICATION NUMBER: PCT/IB2019/053040
PRIOR FILING DATE: 2019-04-12
PRIOR APPLICATION NUMBER: EP 18190661.1
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18190662.9
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18167384.9
PRIOR FILING DATE: 2018-04-13
PRIOR APPLICATION NUMBER: EP 18167385.6
PRIOR FILING DATE: 2018-04-13
NUMBER OF SEQ ID NOS: 136
SEQ ID NO 62
LENGTH: 214
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Description of Artificial Sequence: Synthetic
polypeptide"
Query Match 75.0%; Score 75.7; Length 214;
Best Local Similarity 25.4%;
Matches 18; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 EDIYNG-----------------GAS---------------------------------- 9
|||||| |||
Db 27 EDIYNGLAWYQQKPGKAPKLLIYGASSLQDGVPSRFSGSGSGTEFTLTISSLQPEDEATY 86
Qy 10 --AGPHKYPLT 18
|||||||||
Db 87 YCAGPHKYPLT 97
US-16-714-396-66
Filing date in PALM: 2019-12-13
Sequence 66, US/16714396
Patent No. 11001633
GENERAL INFORMATION
APPLICANT: AFFIMED GMBH
TITLE OF INVENTION: NK CELL ENGAGING ANTIBODY FUSION CONSTRUCTS
FILE REFERENCE: 087353.0106
CURRENT APPLICATION NUMBER: US/16/714,396
CURRENT FILING DATE: 2019-12-13
PRIOR APPLICATION NUMBER: PCT/IB2019/053040
PRIOR FILING DATE: 2019-04-12
PRIOR APPLICATION NUMBER: EP 18190661.1
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18190662.9
PRIOR FILING DATE: 2018-08-24
PRIOR APPLICATION NUMBER: EP 18167384.9
PRIOR FILING DATE: 2018-04-13
PRIOR APPLICATION NUMBER: EP 18167385.6
PRIOR FILING DATE: 2018-04-13
NUMBER OF SEQ ID NOS: 136
SEQ ID NO 66
LENGTH: 107
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
NAME/KEY: source
OTHER INFORMATION: /note="Description of Artificial Sequence: Synthetic
polypeptide"
ALIGNMENT:
Query Match 75.0%; Score 75.7; Length 107;
Best Local Similarity 25.4%;
Matches 18; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 EDIYNG-----------------GAS---------------------------------- 9
|||||| |||
Db 27 EDIYNGLAWYQQKPGKAPKLLIYGASSLQDGVPSRFSGSGSGTEFTLTISSLQPEDEATY 86
Qy 10 --AGPHKYPLT 18
|||||||||
Db 87 YCAGPHKYPLT 97
Prosecution Insights