Abstract
Central issues of current immunology are the molecular basis of antibody specificity and the origin of antibody diversity. While it is clear that antibody specificity is a consequence of the amino acid sequence of the variable regions of light and heavy polypeptide chains of the immunoglobulin molecule, for which the methodology is straight forward (by the determination of the amino acid sequence and X-ray crystallography), the second problem still escapes direct attack. This question is referring to two points: (1) How did antibody diversity arise, and (2) How is antibody diversity maintained? The structural data available from immunoglobulins of different species, and the fact that low vertebrates, having less than 106 lymphocytes (Du Pasquier, 1970), i.e. a lower number of different variable regions, manage to cope with antigenic determinants known to date, appear to be in support of the view that antibody variability in vertebrates is achieved mainly by evolutionary processes (Hilschmann et al., 1970; Hood and Talmage, 1970; Hood and Prahl, 1971). The problem which we would like to discuss is: How is antibody diversity maintained in different species?
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Braun, D.G., Jaton, JC. (1974). Homogeneous Antibodies: Induction and Value as Probe for the Antibody Problem. In: Arber, W., et al. Current Topics in Microbiology and Immunology. Current Topics in Microbiology and Immunology, vol 66. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65908-9_2
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