NZ807450A - Antibodies binding to gprc5d - Google Patents
Antibodies binding to gprc5dInfo
- Publication number
- NZ807450A NZ807450A NZ807450A NZ80745019A NZ807450A NZ 807450 A NZ807450 A NZ 807450A NZ 807450 A NZ807450 A NZ 807450A NZ 80745019 A NZ80745019 A NZ 80745019A NZ 807450 A NZ807450 A NZ 807450A
- Authority
- NZ
- New Zealand
- Prior art keywords
- seq
- antigen binding
- amino acid
- acid sequence
- lcdr
- Prior art date
Links
- 239000000427 antigen Substances 0.000 claims abstract 72
- 102000036639 antigens Human genes 0.000 claims abstract 72
- 108091007433 antigens Proteins 0.000 claims abstract 72
- 201000010099 disease Diseases 0.000 claims abstract 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract 8
- 238000000034 method Methods 0.000 claims abstract 7
- 102100021197 G-protein coupled receptor family C group 5 member D Human genes 0.000 claims abstract 5
- 101001040713 Homo sapiens G-protein coupled receptor family C group 5 member D Proteins 0.000 claims abstract 5
- 102000040430 polynucleotide Human genes 0.000 claims abstract 5
- 108091033319 polynucleotide Proteins 0.000 claims abstract 5
- 239000002157 polynucleotide Substances 0.000 claims abstract 5
- 239000013598 vector Substances 0.000 claims abstract 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 43
- 108010047041 Complementarity Determining Regions Proteins 0.000 claims 10
- 230000000295 complement effect Effects 0.000 claims 10
- 235000001014 amino acid Nutrition 0.000 claims 5
- 239000008194 pharmaceutical composition Substances 0.000 claims 5
- 239000002253 acid Substances 0.000 claims 4
- 125000000539 amino acid group Chemical group 0.000 claims 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 3
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 claims 2
- 239000004475 Arginine Substances 0.000 claims 2
- 208000023275 Autoimmune disease Diseases 0.000 claims 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 2
- 239000004472 Lysine Substances 0.000 claims 2
- 208000034578 Multiple myelomas Diseases 0.000 claims 2
- 206010028980 Neoplasm Diseases 0.000 claims 2
- 206010035226 Plasma cell myeloma Diseases 0.000 claims 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 2
- 201000011510 cancer Diseases 0.000 claims 2
- 239000003814 drug Substances 0.000 claims 2
- 235000013922 glutamic acid Nutrition 0.000 claims 2
- 239000004220 glutamic acid Substances 0.000 claims 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 2
- 102000009109 Fc receptors Human genes 0.000 claims 1
- 108010087819 Fc receptors Proteins 0.000 claims 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 239000012636 effector Substances 0.000 claims 1
- 239000013604 expression vector Substances 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 239000000203 mixture Substances 0.000 claims 1
- 108090000765 processed proteins & peptides Proteins 0.000 claims 1
- 238000006467 substitution reaction Methods 0.000 claims 1
- 210000001744 T-lymphocyte Anatomy 0.000 abstract 1
- 230000003213 activating effect Effects 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 abstract 1
Abstract
The present invention generally relates to antibodies that bind to GPRC5D, including bispecific antigen binding molecules e.g. for activating T cells. In addition, the present invention relates to polynucleotides encoding such antibodies, and vectors and host cells comprising such polynucleotides. The invention further relates to methods for producing the antibodies, and to methods of using them in the treatment of disease.
Claims (42)
1. An antibody that binds to GPRC5D, wherein the antibody comprises (i) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 83, a HCDR 2 of SEQ ID NO: 84, and a HCDR 3 of SEQ ID 5 NO: 86, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 87, a LCDR 2 of SEQ ID NO: 88 and a LCDR 3 of SEQ ID NO: 89; (ii) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 83, a HCDR 2 of SEQ ID NO: 85, and a HCDR 3 of SEQ ID 10 NO: 86, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 87, a LCDR 2 of SEQ ID NO: 88 and a LCDR 3 of SEQ ID NO: 89, (iii) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 91, and a HCDR 3 of SEQ ID 15 NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 95 and a LCDR 3 of SEQ ID NO: 97; (iv) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 91, and a HCDR 3 of SEQ ID 20 NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 96 and a LCDR 3 of SEQ ID NO: 97; or (v) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 92, and a HCDR 3 of SEQ ID 25 NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 95 and a LCDR 3 of SEQ ID NO: 97.
2. The antibody of claim 1, (i) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 13, and the VL comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 14; or 5 (ii) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 15, and the VL comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 16; or (iii) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 10 98%, 99% or 100% identical to the sequence of SEQ ID NO: 48, and the VL comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 53; or (iv) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 49, and the VL comprises an amino 15 acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 52; or (v) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 57, and the VL comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino 20 acid sequence of SEQ ID NO: 64; or (vi) wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 58, and the VL comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 63. 25
3. The antibody of claim 1 or 2, wherein the antibody is an IgG antibody.
4. The antibody of claim 3, wherein the antibody is an IgG antibody.
5. The antibody of any one of claims 1 to 4, wherein the antibody is a full-length antibody.
6. The antibody of any one of claims 1 to 4, wherein the antibody is an antibody fragment selected from the group of an Fv molecule, a scFv molecule, a Fab molecule, and a F(ab')2 molecule.
7. The antibody of any one of claims 1 to 6, wherein the antibody is a multispecific 5 antibody.
8. A bispecific antigen binding molecule, comprising (a) a first antigen binding moiety that binds to a first antigen, wherein the first antigen is GPRC5D and the first antigen binding moiety comprises a (i) a heavy chain variable region (VH) comprising a heavy chain complementary determining 10 region (HCDR) 1 of SEQ ID NO: 83, a HCDR 2 of SEQ ID NO: 84, and a HCDR 3 of SEQ ID NO: 86, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 87, a LCDR 2 of SEQ ID NO: 88 and a LCDR 3 of SEQ ID NO: 89; (ii) a heavy chain variable region (VH) comprising a heavy chain complementary determining 15 region (HCDR) 1 of SEQ ID NO: 83, a HCDR 2 of SEQ ID NO: 85, and a HCDR 3 of SEQ ID NO: 86, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 87, a LCDR 2 of SEQ ID NO: 88 and a LCDR 3 of SEQ ID NO: 89, (iii) a heavy chain variable region (VH) comprising a heavy chain complementary determining 20 region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 91, and a HCDR 3 of SEQ ID NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 95 and a LCDR 3 of SEQ ID NO: 97; (iv) a heavy chain variable region (VH) comprising a heavy chain complementary determining 25 region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 91, and a HCDR 3 of SEQ ID NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 96 and a LCDR 3 of SEQ ID NO: 97; or (v) a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 of SEQ ID NO: 90, a HCDR 2 of SEQ ID NO: 92, and a HCDR 3 of SEQ ID NO: 93, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 of SEQ ID NO: 94, a LCDR 2 of SEQ ID NO: 95 and a LCDR 3 5 of SEQ ID NO: 97; and (b) a second antigen binding moiety which specifically binds to a second antigen.
9. The bispecific antigen binding molecule of claim 8, (i) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 13, 10 and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 14; or (ii) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 15, 15 and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 16; or (iii) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 48, 20 and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 53; or (iv) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 49, 25 and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 52; or (v) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 57, and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 64; or (vi) wherein the VH of the first antigen binding moiety comprises an amino acid sequence that is 5 at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 58, and wherein the VL of the first antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 63.
10. The bispecific antigen binding molecule of claim 8 or 9, wherein the second antigen is 10 CD3.
11. The bispecific antigen binding molecule of claim 10, wherein the second antigen is CD3?.
12. The bispecific antigen binding molecule of claim 10 or 11, wherein the second antigen binding moiety comprises a VH comprising a HCDR 1 of SEQ ID NO: 29, a HCDR 2 of SEQ 15 ID NO: 30, and a HCDR 3 of SEQ ID NO: 31, and a VL comprising a LCDR 1 of SEQ ID NO: 32, a LCDR 2 of SEQ ID NO: 33 and a LCDR 3 of SEQ ID NO: 34.
13. The bispecific antigen binding molecule of claim 12, wherein the VH of the second antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 35, and the VL of the 20 second antigen binding moiety comprises an amino acid sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 36.
14. The bispecific antigen binding molecule of any one of claims 8 to 13, wherein the first and/or the second antigen binding moiety is a Fab molecule.
15. The bispecific antigen binding molecule of any one of claims 8 to 14, wherein the second 25 antigen binding moiety is a Fab molecule wherein the variable domains VL and VH or the constant domains CL and CH1, particularly the variable domains VL and VH, of the Fab light chain and the Fab heavy chain are replaced by each other.
16. The bispecific antigen binding molecule of any one of claims 8 to 15, wherein the first antigen binding moiety is a Fab molecule wherein in the constant domain the amino acid at position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat) and the amino acid at position 123 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat), and in the constant domain CH1 the amino acid at position 147 is substituted independently by glutamic acid (E), or aspartic 5 acid (D) (numbering according to Kabat EU index) and the amino acid at position 213 is substituted independently by glutamic acid (E), or aspartic acid (D) (numbering according to Kabat EU index).
17. The bispecific antigen binding molecule of any one of claims 8 to 16, wherein the first and the second antigen binding moiety are fused to each other, optionally via a peptide linker. 10
18. The bispecific antigen binding molecule of any one of claims 8 to 17, wherein the first and the second antigen binding moiety are each a Fab molecule and wherein either (i) the second antigen binding moiety is fused at the C-terminus of the Fab heavy chain to the N-terminus of the Fab heavy chain of the first antigen binding moiety, or (ii) the first antigen binding moiety is fused at the C-terminus of the Fab heavy chain to the N-terminus of the Fab heavy chain of the 15 second antigen binding moiety.
19. The bispecific antigen binding molecule of any one of claims 8 to 18, comprising a third antigen binding moiety.
20. The bispecific antigen binding molecule of claim 19, wherein the third antigen moiety is identical to the first antigen binding moiety. 20
21. The bispecific antigen binding molecule of any one of claims 8 to 20, comprising an Fc domain composed of a first and a second subunit.
22. The bispecific antigen binding molecule of claim 21, wherein the first, the second and, where present, the third antigen binding moiety are each a Fab molecule; and wherein either (i) the second antigen binding moiety is fused at the C-terminus of the Fab 25 heavy chain to the N-terminus of the Fab heavy chain of the first antigen binding moiety and the first antigen binding moiety is fused at the C-terminus of the Fab heavy chain to the N-terminus of the first subunit of the Fc domain, or (ii) the first antigen binding moiety is fused at the Cterminus of the Fab heavy chain to the N-terminus of the Fab heavy chain of the second antigen binding moiety and the second antigen binding moiety is fused at the C-terminus of the Fab 30 heavy chain to the N-terminus of the first subunit of the Fc domain; and wherein the third antigen binding moiety, where present, is fused at the C-terminus of the Fab heavy chain to the N-terminus of the second subunit of the Fc domain.
23. The bispecific antigen binding molecule of claim 21 or 22, wherein the Fc domain is an IgG Fc domain. 5
24. The bispecific antigen binding molecule of claim 23, wherein the Fc domain is an IgG1 Fc domain.
25. The bispecific antigen binding molecule of any one of claims 21 to 24, wherein the Fc domain is a human Fc domain.
26. The bispecific antigen binding molecule of any one of claims 21 to 25, wherein an amino 10 acid residue in the CH3 domain of the first subunit of the Fc domain is replaced with an amino acid residue having a larger side chain volume, thereby generating a protuberance within the CH3 domain of the first subunit which is positionable in a cavity within the CH3 domain of the second subunit, and an amino acid residue in the CH3 domain of the second subunit of the Fc domain is replaced with an amino acid residue having a smaller side chain volume, thereby 15 generating a cavity within the CH3 domain of the second subunit within which the protuberance within the CH3 domain of the first subunit is positionable.
27. The bispecific antigen binding molecule of any one of claims 21 to 26, wherein the Fc domain comprises one or more amino acid substitution that reduces binding to an Fc receptor and/or effector function. 20
28. One or more isolated polynucleotide encoding the antibody or bispecific antigen binding molecule of any one of claims 1 to 27.
29. One or more vector, particularly expression vector, comprising the polynucleotide(s) of claim 28.
30. A host cell comprising the polynucleotide(s) of claim 28 or the vector(s) of claim 29. 25
31. A method of producing an antibody that binds to GPRC5D, comprising the steps of a) culturing the host cell of claim 30 under conditions suitable for the expression of the antibody and b) optionally recovering the antibody.
32. An antibody that binds to GPRC5D, produced by the method of claim 31.
33. A pharmaceutical composition comprising the antibody or bispecific antigen binding molecule of any one of claims 1 to 27 or 32 and a pharmaceutically acceptable carrier.
34. The antibody or bispecific antigen binding molecule of any one of claims 1 to 27 or 32 or the pharmaceutical composition of claim 33 for use as a medicament. 5
35. The antibody or bispecific antigen binding molecule of any one of claims 1 to 27 or 32 or the pharmaceutical composition of claim 33 for use in the treatment of a disease.
36. The antibody, bispecific antigen binding molecule or pharmaceutical composition of claim 35, wherein the disease is cancer or an autoimmune disease.
37. The antibody, bispecific antigen binding molecule or pharmaceutical composition of claim 10 35, wherein the disease is multiple myeloma.
38. Use of the antibody or bispecific antigen binding molecule of any one of claims 1 to 27 or 32 in the manufacture of a medicament for the treatment of a disease.
39. A method of treating a disease in an individual, comprising administering to said individual a therapeutically effective amount of a composition comprising the antibody or bispecific antigen 15 binding molecule of any one of claims 1 to 27 or 32 in a pharmaceutically acceptable form.
40. The use of claim 38 or the method of claim 39, wherein said disease is cancer or an autoimmune disease.
41. The use of claim 38 or the method of claim 39, wherein said disease is multiple myeloma.
42. The invention as described herein.
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ807450A true NZ807450A (en) |
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