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B cell responses to a peptide epitope. II: Multiple levels of selection during maturation of primary responses
Author(s) -
Tuteja Renu,
Agarwal Anshu,
Vijayakrishnan Lalitha,
Nayak Bishnu P,
Gupta Satish K,
Kumar Vijay,
Rao Kanury VS
Publication year - 1997
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.1997.38
Subject(s) - epitope , biology , antigen , antibody , immune system , immunology , phenotype , microbiology and biotechnology , genetics , gene
This report analyses murine primary humoral recognition of a linear domain (MEP 17–31) within a 100 amino acid polypeptide. MEP‐I. An analysis of the early primary IgM response revealed that MEP 17–31 presented at least two distinct domains for pre‐immune B cell recognition represented by MEP‐1 residues 19–23 and 26–28. However, subsequent maturation into an IgG response saw an exclusive selection for the anti‐MEP 19–23 component with loss of all alternate specificities. The IgM response to MEP 19–23 was oligoclonal and composed of diverse paratope phenotypes as evidenced by varied heavy chains of immunoglobulin V–D‐J combinations and CDR3 sequences. In contrast to the oligoclonality of IgM niAb. the mature IgG response to MEP 19–23 appeared to derive predominantly from a single progenitor. It therefore appears that maturation of primary humoral responses to polypeptide antigens involves two distinct levels of selection. While there is selection for a restricted subset of the initially induced antibody fine‐specificities, progression of the response also entails a reduction in clonal heterogeneity of B cells responding to the dominant epitope.