T-cell recognition and antigen presentation of myoglobin.
Determination of the T-cell recognition profile of Mb by the overlapping peptide strategy revealed that the protein has six T sites. Five of these coincide with the antigenic sites while one site was recognized exclusively by T cells and not by any detectable levels of antibody. Recognition of the synthetic T sites by protein-primed T cell lines or clones indicated that T cells display an unusual peptide size requirement beyond the essential contact residues of the T site. The antigen presentation of Mb has been examined with the significant advantage of knowing the full profiles of T- and B-cell recognition of this multi-determinant antigen. Significant differences in the patterns of T-cell recognition were observed following protein-priming as compared to peptide-priming. The absence of a clear relationship between these patterns of recognition presents a strong evidence against a mechanism of antigen presentation which is dependent on the generation of peptide fragments with the latter being the 'presented' species. From this new perspective, the protein molecule must be predominantly presented in its intact form.
Atassi
M Z
MZ
Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
Bixler
G S
GS
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology; D000949:Histocompatibility Antigens Class II / Q000032:analysis*; D006801:Humans; D009211:Myoglobin / Q000276:immunology*; D013601:T-Lymphocytes / Q000276:immunology*
D000949:Histocompatibility Antigens Class II; D009211:Myoglobin