Recombinant antibody

• US 5,677,425 A
• Filed: 08/18/1994
• Issued: 10/14/1997
• Est. Priority Date: 09/04/1987
• Status: Expired due to Term

• Current Assignee: Celltech Group Limited (UCB SA)
• Original Assignee: Celltech Group Limited (UCB SA)
• Inventors: Whittle, Nigel Richard, Adair, John Robert, Bodmer, Mark William
• Primary Examiner(s): Ziska, Suzanne E.
• Application Number:
  US08/292,356
• Time in Patent Office: 1,153 Days
• Field of Search: 530/387.3, 530/391.3, 435/172.3
• US Class Current: 530/387.1
• CPC Class Codes: C07K 16/00 Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies antibodies with enzymatic activity, e.g. abzymes C12N9/0002
• CPC Class Codes: C07K 16/30 from tumour cells
• CPC Class Codes: Y10S 530/866 involving immunoglobulin or antibody fragment, e.g. fab', fab, fv, fc, heavy chain or light chain
• CPC Class Codes: Y10S 530/867 involving immunoglobulin or antibody produced via recombinant dna technology

Abstract

The present invention provides an altered antibody molecule (AAM) having a hinge region which has a different number of cysteine residues from that found in the hinge region normally associated with the CH1 domain of the antibody molecule and a process for producing the same using recombinant DNA technology.

Claims

1. An antibody molecule comprising heavy and light chains, each heavy chain having a hinge region, said hinge region having only one cysteine residue capable of forming a heavy chain to heavy chain disulphide bond, provided that the heavy chain is of a subclass which does not naturally contain a single cysteine residue capable of forming a heavy chain to heavy chain disulphide bond.

7. The antibody molecule of claim 1, further comprising an effector or reporter molecule attached to said hinge region.

2. An antibody molecule comprising heavy and light chains, each heavy chain having a hinge region, said hinge region having from 2 to about 11 cysteine residues capable of forming heavy chain to heavy chain disulphide bonds, the number of hinge region cysteine residues being different than occurs naturally for heavy chains of the same subclass.

8. The antibody molecule of claim 2, further comprising an effector or reporter molecule attached to said hinge region.

3. An Fab'"'"' fragment comprising a heavy chain and a light chain, said heavy chain having a hinge region, said hinge region having only one cysteine residue capable of forming a heavy chain to heavy chain disulphide bond, provided that the heavy chain is of a subclass which does not naturally contain a single cysteine residue capable of forming a heavy chain to heavy chain disulphide bond.

5. An F(ab'"'"')₂ fragment comprising two Fab'"'"' fragments according to claim 3 linked together directly via said one hinge region cysteine residues.

9. The Fab'"'"' fragment of claims 3, further comprising an effector or reporter molecule attached to said hinge region.

11. The F(ab'"'"')₂ fragment of claim 5, further comprising an effector or reporter molecule attached to said hinge region.

4. An Fab'"'"' fragment comprising a heavy chain and a light chain, said heavy chain having a hinge region, said hinge region having from 2 to about 11 cysteine residues capable of forming heavy chain to heavy chain disulphide bonds, the number of hinge region cysteine residues being different than occurs naturally for heavy chains of the same subclass.

6. An F(ab'"'"')₂ fragment comprising two Fab'"'"' fragments according to claim 4 linked together directly via said hinge region cysteine residues.

10. The Fab'"'"' fragment of claim 4, further comprising an effector or reporter molecule attached to said hinge region.

12. The F(ab'"'"')₂ fragment of claim 6, further comprising an effector or reporter molecule attached to said hinge region.

13. A humanised antibody molecule comprising heavy and light chains, each heavy chain having a hinge region, said hinge region having only one cysteine residue capable of forming a heavy chain to heavy chain disulphide bond "provided that the heavy chain is of a subclass which does not naturally contain a single cysteine residue capable of forming a heavy chain to heavy chain disulphide bond".