In Vitro Responses of Myoglobin-Primed Lymph Node Cells to Myoglobin and Myoglobin Synthetic Antigenic Peptides

Abstract

The ultimate objective of the newer immunology is to understand various immune responses and reactions in cellular and molecular terms. The relevant molecules include various antigenic determinants, receptors and antigen-binding molecules on lymphocytic surfaces, molecules produced and secreted by lymphocytes, and lymphocytic surface molecules that recognize and are triggered by helper and/or regulatory molecules produced by other cells (Cold Spring Harbor Symposia, 1976). These cellular and molecular mechanisms have been illuminated by studies with hapten-protein and synthetic peptide systems in inbred strains of mice. Beginning in the early 1970’s Goodman utilized glucagon, Benjamini Tobacco mosaic virus protein and then Levy ferredoxin to obtain much new information about the relationships between antigenic structure of these proteins and their peptides and the capacity of these molecules to induce various immune reactions. We assumed that many questions about such relationships could be approached incisively with peptides derived from proteins of known molecular and antigenic structure. It was also hoped that the complexity of immune responses would be reduced by studying the results of adding single peptides to lymphocytes; this was based on the assumption that some of this complexity was due to the response of different clones of T and/or B lymphocytes to the different antigenic determinants on a protein. We proposed to utilize small peptides approximating in size one antigenic determinant, i.e., a tetrapeptide (Schechter et al., 1966) because such peptides would not effect the cross-linkage of receptors considered necessary for lymphocytic activation (Fanger et al., 1970).