title: Antigen-binding mutants of mouse myeloma cells.
abstract: A cultured mouse myeloma cell line, S107, that secretes an IgA phosphocholine-binding immunoglobulin has been cloned in soft agar and overlaid with phosphocholine-hemocyanin. Spontaneous mutants that secrete immunoglobulin with a decreased ability to precipitate antigen were detected with this plate assay and occur at a very high frequency. From one such mutant, phenotypic revertants arise spontaneously with a frequency of 0.28-2.8%. This mutant and one of its revertants were studied, and they were found to differ from the parent and from each other serologically and in antigen binding. While it is not yet clear whether these findings bear any relationship to the normal generation of antibody diversity, they do indicate that it is possible to generate antigen binding diversity in somatic cells.
mesh_terms: D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D001666:Binding Sites, Antibody; D002352:Carrier Proteins / Q000276:immunology; D002460:Cell Line; D006433:Hemocyanins / Q000276:immunology; D007070:Immunoglobulin A / Q000235:genetics*; D009154:Mutation; D009194:Myeloma Proteins / Q000235:genetics* / Q000276:immunology; D010767:Phosphorylcholine / Q000276:immunology
chemical_list: D002352:Carrier Proteins; D007070:Immunoglobulin A; D009194:Myeloma Proteins; D010767:Phosphorylcholine; D006433:Hemocyanins
references.citation: Nature. 1977 Jan 27;265(5592):299-304
references.pmid: 401950
references.citation: Immunochemistry. 1976 Nov;13(11):945-9
references.pmid: 827496
references.citation: Eur J Immunol. 1976 Jul;6(7):511-9
references.pmid: 825377
references.citation: J Exp Med. 1976 Nov 2;144(5):1254-62
references.pmid: 1086883
references.citation: Proc Natl Acad Sci U S A. 1974 Sep;71(9):3478-82
references.pmid: 4139712
references.citation: J Exp Med. 1974 Sep 1;140(3):673-86
references.pmid: 4137581
references.citation: Essays Biochem. 1974;10:73-103
references.pmid: 4140089
references.citation: Nature. 1973 Oct 12;245(5424):320-2
references.pmid: 4128217
references.citation: J Exp Med. 1970 Oct 1;132(4):737-51
references.pmid: 4101363
references.citation: Biochemistry. 1968 Jul;7(7):2682-8
references.pmid: 4173394
references.citation: Immunochemistry. 1969 Jan;6(1):111-23
references.pmid: 4180087
references.citation: J Exp Med. 1970 Mar 1;131(3):515-41
references.pmid: 4189836
references.citation: Science. 1973 Oct 12;182(4108):164-6
references.pmid: 4354174
references.citation: J Cell Physiol. 1972 Jun;79(3):429-40
references.pmid: 4625122
references.citation: J Immunol. 1975 Jan;114(1 Pt 1):70-5
references.pmid: 46246
references.citation: Physiol Rev. 1972 Jul;52(3):631-719
references.pmid: 4555516
references.citation: Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298-302
references.pmid: 4530984
references.citation: J Biol Chem. 1974 Oct 25;249(20):6605-10
references.pmid: 4472818
references.citation: Biochemistry. 1972 Feb 29;11(5):766-71
references.pmid: 5059886
references.citation: J Natl Cancer Inst. 1972 Jul;49(1):305-8
references.pmid: 5037438
references.citation: J Immunol. 1972 Jan;108(1):126-34
references.pmid: 5010390
references.citation: Proc Natl Acad Sci U S A. 1976 Jun;73(6):2109-12
references.pmid: 819932
references.citation: J Mol Biol. 1976 Apr 5;102(2):237-52
references.pmid: 818392
references.citation: Annu Rev Biochem. 1975;44:639-67
references.pmid: 806253
references.citation: Nature. 1975 Jul 31;256(5516):373-6
references.pmid: 806814
references.citation: Proc Natl Acad Sci U S A. 1975 Apr;72(4):1427-30
references.pmid: 805428
references.citation: J Immunol. 1971 Jan;106(1):41-50
references.pmid: 5543726
references.citation: J Exp Med. 1970 Aug 1;132(2):211-50
references.pmid: 5508247