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Related Experiment Videos

Structure and function of natural antibodies

P Casali1, E W Schettino

  • 1Department of Pathology, Cornell University Medical College, New York, New York 10021-4896, USA.

Current Topics in Microbiology and Immunology
|January 1, 1996
PubMed
Summary

Natural antibodies, primarily IgM produced by B-1 cells, defend against infections and can bind self and foreign antigens. Their structure, particularly the H chain CDR3, dictates antigen binding and polyreactivity, influencing the B cell repertoire.

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Area of Science:

  • Immunology
  • Molecular Biology

Background:

  • Natural antibodies are primarily IgM, polyreactive, and encoded by germline V genes, arising without antigenic stimulation.
  • Produced mainly by B-1 cells, they are crucial in neonates and play a role in the human B cell repertoire's development and physiology.
  • These antibodies bind both self-antigens and exogenous antigens, including those on bacteria and viruses, forming a primary defense against infections.

Purpose of the Study:

  • To investigate whether B-1 lymphocytes, precursors of natural antibodies, undergo antigen-driven clonal selection.
  • To elucidate the structural correlates of natural antibody polyreactivity and antigen binding.
  • To propose and test a structure-function model for natural antibody antigen-binding properties.

Main Methods:

  • Analysis of B-1 cell hypermutation mechanisms.

Related Experiment Videos

  • Gene shuffling, site-directed mutagenesis, and in vitro human Ig gene expression.
  • Structural analysis of antibody polyreactivity and antigen-induced autoantibodies.

    • Main Results:

    • B-1 cells possess hypermutation mechanisms similar to conventional B-2 cells.
    • The somatically generated H chain CDR3 is the primary structural determinant of antibody polyreactivity.
    • The Ig V region, particularly H chain CDR3, dictates antigen binding in monoreactive autoantibodies.

    Conclusions:

    • A structure-function model proposes that somatically generated H chain CDR3 dictates germline antibody antigen-binding features.
    • Antigen-driven affinity maturation primarily affects Ig V gene-encoded segments.
    • Further research on structurally reverted autoantibodies will clarify repertoire shaping mechanisms in development and disease.