IP Library › Granted Patent US 12,522,664
Granted Patent B2
US 12,522,664 · App. 18/331,855 · Granted Jan 13, 2026

Anti-CD20 antibody and uses thereof

Inventors: Isabelle Riviere (New York, NY); Ouathek Ouerfelli (New York, NY); Xiuyan Wang (New York, NY); Frances Weis-Garcia (New York, NY)
Assignee: Memorial Sloan Kettering Cancer Center
C07K16/2887A61K40/11A61K40/31A61K40/4221A61P35/00C07K14/7051C07K14/70517C07K14/70521C07K14/70578C07K14/70596G01N33/57492A61K2239/31A61K2239/38A61K2239/48C07K2317/622C07K2319/02C07K2319/03G01N2333/70596
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Quick Facts
Patent No.
US 12,522,664
App. No.
18/331,855
Granted
Jan 13, 2026
Kind
B2
Abstract

Provided herein are anti-CD20 antibodies and uses thereof for treatment and diagnosis. Also provided are CD20 antigens for the production of anti-CD20 antibodies and methods of generating anti-CD20 antibodies using the CD20 antigens.

Claims (18)

1 . A method of inhibiting tumor growth or metastasis comprising contacting a tumor cell with an effective amount of an antibody or an antigen binding portion thereof that specifically binds to a canine CD20 cyclic peptide having the sequence of SEQ ID NO: 20, wherein the cysteine at position 7 of SEQ ID NO: 20 forms a disulfide bond with the cysteine at position 23 of SEQ ID NO: 20, wherein the antibody or antigen binding portion thereof comprises a VH complementarity determining region (CDR) 1 of SEQ ID NO: 40, a VH CDR2 of SEQ ID NO: 42, and a VH CDR3 consisting of a threonine (T) residue, a VL CDR1 of SEQ ID NO: 46, a VL CDR2 of LVS, and a VL CDR3 of SEQ ID NO: 50.

2 . The method of claim 1 , wherein the tumor cell is a canine tumor cell.

3 . The method of claim 1 , wherein the antibody or antigen binding portion thereof binds to the canine CD20 cyclic peptide at a higher affinity than a linear peptide having the sequence of SEQ ID NO: 21.

4 . The method of claim 1 , wherein the antibody or antigen binding portion thereof comprises a heavy chain variable domain (VH) comprising SEQ ID NO: 4.

5 . The method of claim 1 , wherein the antibody or antigen binding portion thereof comprises a light chain variable domain (VL) comprising SEQ ID NO: 6.

6 . The method of claim 1 , wherein the antibody or antigen binding portion thereof comprises a heavy chain variable domain (VH) that is at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 4.

7 . The method of claim 1 , wherein the antibody or antigen binding portion thereof comprises a light chain variable domain (VL) that is at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 6.

8 . The method of claim 1 , wherein the antibody or antigen binding portion thereof is a full length antibody, a Fab fragment, a F(ab′)2 fragment, or a single chain variable fragment (scFV).

9 . The method of claim 1 , wherein the antibody or antigen binding portion thereof is a scFv.

10 . The method of claim 1 , wherein the antibody or antigen binding portion thereof comprises SEQ ID NO: 8, or is at least 85%, 90%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 8.

11 . The method of claim 1 , wherein the antibody or antigen binding portion thereof is a bispecific antibody.

12 . The method of claim 1 , wherein the antibody or antigen binding portion thereof is a scFv-Fc fusion protein.

13 . The method of claim 1 , wherein the antibody or antigen binding portion thereof is an immunoconjugate.

14 . The method of claim 13 , wherein the antibody or antigen binding portion thereof comprises a second component selected from the group consisting of a cytotoxin, a detectable label, a radioisotope, a therapeutic agent, a liposome, a nanoparticle, a binding protein, or an antibody.

15 . A method of treating a condition mediated by B-cells in a subject in need thereof comprising administering to the subject an effective amount of an isolated antibody or an antigen binding portion thereof that specifically binds to a canine CD20 cyclic peptide having the sequence of SEQ ID NO: 20, wherein the cysteine at position 7 of SEQ ID NO: 20 forms a disulfide bond with the cysteine at position 23 of SEQ ID NO: 20,

wherein the antibody or antigen binding portion thereof comprises a VH complementarity determining region (CDR) 1 of SEQ ID NO: 40, a VH CDR2 of SEQ ID NO: 42, and a VH CDR3 consisting of a threonine (T) residue, a VL CDR1 of SEQ ID NO: 46, a VL CDR2 of LVS, and a VL CDR3 of SEQ ID NO: 50,

wherein the isolated antibody or antigen binding portion thereof is selected from the group consisting of a full immunoglobulin, a Fab, a F(ab′)2, a recombinantly produced single chain variable fragment (scFv), a scFv-Fc fusion protein, or a bispecific antibody, and wherein the isolated antibody or antigen binding portion thereof is not part of a chimeric antigen receptor,

wherein the condition mediated by B-cells is a B cell lymphoma or an immune mediated disease.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 8, 2025
From: OUERFELLI, OUATHEK; RIVIERE, ISABELLE; WANG, XIUYAN; WEIS-GARCIA, FRANCES
To: MEMORIAL SLOAN KETTERING CANCER CENTER
Reel/Frame 073140/0434 →
Continuity (3)
Division 16970805
Provisional Application 62633034 · Feb 20, 2018
Related Publication 20240124601A1 · Apr 18, 2024
References Cited (26)
US 11673961B2 · Riviere · 2023 [cited by examiner]
US 20040197328A1 · Young · 2004 [cited by examiner]
US 20070280882A1 · Wu · 2007 [cited by examiner]
US 20110091483A1 · Beall · 2011 [cited by applicant]
US 20160220665A1 · Cobbold et al. · 2016 [cited by applicant]
US 20230416392A1 · Riviere · 2023 [cited by examiner]
JP 2016208934A2 · 2016 [cited by applicant]
WO WO2010117448A2 · 2010 [cited by applicant]
WO WO2013054127A1 · 2013 [cited by applicant]
WO WO2017011316A1 · 2017 [cited by applicant]
Gura (Science, 1997, 278:1041-1042) (Year: 1997). [cited by examiner]
Kaiser (Science, 2006, 313: 1370) (Year: 2006). [cited by examiner]
Chames et al (British J. of Pharmacology, 2009, 157, 220-233) (Year: 2009). [cited by examiner]
Rudikoff et al. (PNAS, USA, 1982, 79: 1979-1983) (Year: 1982). [cited by examiner]
Coleman et al. (Research in Immunology, 1994; 145(1): 33-36) (Year: 1994). [cited by examiner]
Abaza et al. (Journal of Protein Chemistry, vol. 11, No. 5, 1992, pp. 433-444) (Year: 1992). [cited by examiner]
Jena et al. (Blood Aug. 19, 2010 116 (7): 1035-1044) (Year: 2010). [cited by examiner]
Almagro & Fransson, “Humanization of antibodies”, Frontiers in Bioscience 2008; 13:1619-33 (Year: 2008). [cited by applicant]
Ernst J. A. et al. “Isolation and Characterization of the B-Cell Marker CD20” Biochemistry 44: 15150 (2005)) (Year: 2005). [cited by applicant]
International Search Report and Written Opinion, PCT/US2019/018535, Memorial Sloan Kettering Cancer Center (Jul. 5, 2019). [cited by applicant]
UniProtKB Accession No. A0A026WD16_OOCBI “Glycerate kinase”, Jul. 9, 2014 (online]. [Retrieved on Jun. 17, 2019]. Retrieved from the internet: <URL:https://www.uniprot.org/uniprot/AOA026WD 16> Entire document. [cited by applicant]
UniProtKB Accession No. A0A1X4N0U5_9PROT “Glycerol-3-phosphate dehydrogenase”, Jul. 5, 2017 [online]. [Retrieved on Jun. 17, 2019]. Retrieved from the internet: <URL: https://www.uniprot.org/uniprot/AOA 1 X4N0U5> Entire… [cited by applicant]
Dudley, et al., “Adoptive-Cell-Transfer Therapy for the Treatment of Patients with Cancer,” Nature Reviews Cancer, 2003, (11 pages). [cited by applicant]
Jena, et al., “Redirecting T-cell specificity by introducing a tumor-specific chin1eric antigen receptor,” Blood, Aug. 19, 2010, vol. 116 No. 7, (11 pages). [cited by applicant]
Kaiser, et al., “Reveals Complex Landscape,” Science, vol. 331, Sep. 8, 2006 (1 page). [cited by applicant]
Marincola, et al., “Redirecting T-cell specificity by introducing a tumnor-specific chin1eric antigen receptor,” Trends in Immunology, Jun. 2003, (8 pages). [cited by applicant]