IP Library Granted Patent US 9,562,098
Granted Patent B2
US 9,562,098 · App. 14/326,119 · Granted Feb 7, 2017

Anti-CD28 humanized antibodies

Inventors: Caroline Mary (Sainte Pazanne, FR); Nicolas Poirier (Nantes, FR); Bernard Vanhove (Reze, FR)
Assignees: OSE Immunotherapeutics; Institut National de la Sante et de la Recherche Medicale (INSERM)
C07K16/2818A61K39/3955A61K47/48215C07K16/2896A61K2039/505C07K2317/24C07K2317/524C07K2317/53C07K2317/55C07K2317/56C07K2317/64C07K2317/76
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Quick Facts
Patent No.
US 9,562,098
App. No.
14/326,119
Granted
Feb 7, 2017
Kind
B2
Abstract

The invention relates to humanized antibodies directed against the human lymphocyte receptor CD28. When used in a monovalent form these antibodies are antagonists, i.e. capable of blocking of the CD28/B7 interaction, without activating CD28. These antibodies can be used in particular as therapeutic agents for blocking T cell activation through the CD28 receptor.

Claims (30)

1. A method of treating a T-lymphocyte-mediated autoimmune disease in a subject in need thereof comprising administering an anti-CD28 monovalent antibody to the subject, wherein the anti-CD28 monovalent antibody is selected from the group consisting of:

(a) an antibody having a CD28-binding site consisting of:

a heavy chain variable domain of SEQ ID NO: 1; and

a light chain variable domain of SEQ ID NO: 2, and

(b) an antibody having a CD28-binding site consisting of:

a heavy chain variable domain having all three complementarity determining regions (CDRs) of the variable domain of SEQ ID NO: 1; and

a light chain variable domain having all three CDRs of the variable domain of SEQ ID NO: 2.

2. The method of claim 1 , wherein the monovalent antibody is a heterodimer of:

a first protein chain having the sequence of amino-acids 21-251 of SEQ ID NO: 4; and

a second protein chain having the sequence of amino-acids 21-234 of SEQ ID NO: 6.

3. The method of claim 1 , wherein the monovalent antibody is a heterodimer of:

(I) a first protein chain consisting essentially of, from its N-terminus to its C-terminus:

i: a region A which is a heavy chain variable domain of SEQ ID NO: 1; and

ii: a region B consisting of a peptide linker followed by the CH2 and CH3 domains of an IgG immunoglobulin, and

(II) a second protein chain consisting essentially of, from its N-terminus to its C-terminus:

i: a region A′ which is a light chain variable domain of SEQ ID NO: 2; and

ii: a region B identical to the region B of the first protein chain.

4. The method of claim 3 , wherein the peptide linker is selected from the group consisting of:

a peptide of SEQ ID NO: 7; and

a peptide of SEQ ID NO: 8.

5. The method of claim 3 , wherein the CH2 and CH3 domains are those of an immunoglobulin of the IgG4 subclass.

6. The method of claim 5 , wherein the monovalent antibody is selected from the group consisting of:

a monovalent antibody wherein the polypeptide sequence of the first protein chain is the sequence of amino-acids 21-368 of SEQ ID NO: 10, and the polypeptide sequence of the second protein chain is the sequence of amino-acids 21-355 of SEQ ID NO: 12; and

a monovalent antibody wherein the polypeptide sequence of the first protein chain is the sequence of amino-acids 21-373 of SEQ ID NO: 14, and the polypeptide sequence of the second protein chain is the sequence of amino-acids 21-360 of SEQ ID NO: 16.

7. The method of claim 2 wherein the second protein chain comprises a variable domain of SEQ ID NO: 2.

8. The method of claim 1 , wherein the monovalent antibody is administered in a composition and the composition further comprises a pharmaceutically acceptable excipient.

9. The method of claim 2 , wherein the second protein chain comprises a variable domain of SEQ ID NO: 2 where X represents an alanine or an asparagine residue.

10. The method of claim 2 , wherein the monovalent antibody is pegylated.

11. The method of claim 1 , wherein the heavy chain variable domain further comprises a Q residue at the N-terminal end.

12. The method of claim 1 , wherein the autoimmune disease is selected from the group consisting of type I diabetes, rheumatoid arthritis, and multiple sclerosis.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 17, 2017
From: MARY, CAROLINE; POIRIER, NICOLAS; VANHOVE, BERNARD
To: EFFIMUNE; INSTITUT NATIONAL DE LA SANTE ET DE LA RECHERCHE MEDICALE (INSERM)
Reel/Frame 041623/0264 →
MERGER Recorded Feb 14, 2017
From: EFFIMUNE
To: OSE IMMUNOTHERAPEUTICS
Reel/Frame 041255/0094 →
Priority Claims (2)
EP 10290080 · Feb 18, 2010 · regional
EP 10290389 · Jul 13, 2010 · regional
Continuity (2)
Division 13577103
Related Publication 20150071916A1 · Mar 12, 2015