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A Vh region synthetic peptide induces antibodies which bind native immunoglobulins and augment an immune response to
F A Bonilla1, R S Anderson, M Z Atassi
1Department of Microbiology, Mount Sinai School of Medicine, City University of New York, NY 10029.
The BALB/c myeloma protein ABPC48 (A48) binds the polysaccharide bacterial levan; its Vh is encoded by a gene derived from the VhX24 family. This antibody has been shown to cross-react idiotypically with the phosphorylcholine-binding BALB/c myeloma protein MOPC167 whose Vh shares homology with A48 from residues 32-44. We have synthesized a peptide corresponding to residues 32-44 of the Vh encoded by a germline gene of the VhX24 family. Anti-peptide antisera from rabbits were purified by affinity chromatography with peptide or intact antibody. Several myeloma proteins and monoclonal antibodies with varying degrees of homology to the peptide have been analyzed for reactivity with purified rabbit antibodies in solid-phase RIA. We observed that the specificities within rabbit antisera are heterogeneous, and that purification with antibody versus peptide yields preparations containing different specificities, albeit demonstrably peptide-related. We also show that injection of mice at birth with small amounts of purified rabbit antibodies can affect the magnitude of the response to bacterial levan and the expression of A48 idiotopes in that response.
The BALB/c myeloma protein ABPC48 (A48) binds the polysaccharide bacterial levan; its Vh is encoded by a gene derived from the VhX24 family. This antibody has been shown to cross-react idiotypically with the phosphorylcholine-binding BALB/c myeloma protein MOPC167 whose Vh shares homology with A48 from residues 32-44. We have synthesized a peptide corresponding to residues 32-44 of the Vh encoded by a germline gene of the VhX24 family. Anti-peptide antisera from rabbits were purified by affinity chromatography with peptide or intact antibody. Several myeloma proteins and monoclonal antibodies with varying degrees of homology to the peptide have been analyzed for reactivity with purified rabbit antibodies in solid-phase RIA. We observed that the specificities within rabbit antisera are heterogeneous, and that purification with antibody versus peptide yields preparations containing different specificities, albeit demonstrably peptide-related. We also show that injection of mice at birth with small amounts of purified rabbit antibodies can affect the magnitude of the response to bacterial levan and the expression of A48 idiotopes in that response.