The expressed lysozyme-specific B cell repertoire. I. Heterogeneity in the monoclonal anti-hen egg white lysozyme specificity repertoire, and its difference from the in situ repertoire.
A panel of closely and distantly related lysozymes and lysozyme-peptide fragments were utilized in assessing the specificity repertoire of murine anti-hen egg white lysozyme hybridomas. The 44 monoclonal antibodies could be divided into a minimum of 18 fine specificity groups in tests using the lysozyme panel. Two hybridoma products were specific for epitopes containing amino acids 68 and 121, respectively; and another was specific for an epitopes containing amino acids 113-114. Several hybridomas demonstrated unique heteroclitic binding, for example, to bob-white lysozyme (BEL), but not other closely related lysozymes, suggesting lysine at position 68 in BEL as an important residue of recognition. Radioimmunoassay using lysozyme peptides bound to plastic plates specified the regional specificity of 6 additional antibodies of the 44. A comparison of the specificities of monoclonal antibodies with antibody produced in vivo showed some major differences suggesting that those cells proceeding on to antibody formation in the regulatory milieu of the whole animal are a selected subpopulation.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D001402:B-Lymphocytes / Q000276:immunology*; D001666:Binding Sites, Antibody; D002645:Chickens; D005260:Female; D006825:Hybridomas; D051379:Mice; D009113:Muramidase / Q000276:immunology*; D010047:Ovalbumin / Q000276:immunology; D010455:Peptides / Q000276:immunology
D000911:Antibodies, Monoclonal; D010455:Peptides; D010047:Ovalbumin; D009113:Muramidase