T cell-derived antigen-specific humoral immune response. II. Further characterization of the response and the antigen binding T cell immunoproteins.
Murine T lymphocyte-derived proteins which bind nominal antigen specifically (TABM) were detected in serum during a humoral immune response to bovine serum albumin. The TABM response was observed only when the adjuvants polyadenylic:polyuridylic acid complex (poly(A: U)), Freund's complete adjuvant or Titermax were used concurrently with antigen to immunize. When poly(A:U) was used, higher doses of antigen were optimal to stimulate TABM production than those required to stimulate immunoglobulin production. The binding of TABM in the serum of BSA-immunized mice to BSA in solid phase was inhibited specifically by 10-fold more BSA than that required to inhibit BSA-specific immunoglobulins suggesting that TABM have much less affinity for antigen than immunoglobulins. Immunoblotting of TABM in serum from BSA-immune mice, which bind BSA, demonstrated that these serum TABM are comprised of M(r) 110,000 polypeptides linked by disulfide bonds. Antigen-specific proteins in a lysate of an NP-specific T cell hybrid inhibited the recognition of serum TABM by anti-TABM antiserum while a lysate of a B cell hybridoma was not inhibitory, and serum TABM were adsorbed by monoclonal antibodies to TCR-C beta. These results provide more evidence that serum TABM may be a soluble analogue of the T cell receptor for antigen.
Urbanski
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Department of Pathology, University of Connecticut Health Center, Farmington 06030-3105.
Cone
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D000276:Adjuvants, Immunologic; D000818:Animals; D000917:Antibody Formation; D000941:Antigens / Q000378:metabolism*; D004220:Disulfides; D000939:Epitopes; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C; D011485:Protein Binding; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology*
D000276:Adjuvants, Immunologic; D000941:Antigens; D004220:Disulfides; D000939:Epitopes; D016693:Receptors, Antigen, T-Cell, alpha-beta