The effect of somatic mutation on antibody affinity

P. J. Gearhart

Research output: Contribution to journalArticle

Abstract

Antibody variable region diversity is produced by a variety of mechanisms acting on genes during the developmental stages of B cells. In early B cells, multiple variable (V), diversity (D), and joining (J) gene segments join to produce complete variable regions. This phenomenon represents the germ line repertoire of V regions for heavy and light chains, which is expressed in IgM molecules. At a later stage in B-cell development, a mutational mechanism mutates V genes. This somatically generated repertoire is frequently expressed in IgG and IgA molecules. Thus, the repertoire of secondary B cells contains both germ line-encoded and variant antibodies. To determine the effect of somatic mutation on the affinity of antibodies, we compared the affinities of several germ line and variant anti-phosphorylcholine antibodies taken from immunized mice. The hybridoma protein sequences were defined by nucleotide and amino acid sequencing, and association constants for diazophenylphosphorylcholine were obtained by fluorescence quenching. The affinities of the variant immunoglobulins were fivefold higher than their germ line-encoded counterparts.

Original languageEnglish (US)
Pages (from-to)171-176
Number of pages6
JournalAnnals of the New York Academy of Sciences
VolumeVOL. 418
StatePublished - 1983

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Antibody Affinity
Germ Cells
B-Lymphocytes
Cells
Mutation
Antibodies
Genes
Developmental Genes
Molecules
Phosphorylcholine
Protein Sequence Analysis
Hybridomas
Joining
Immunoglobulin A
Immunoglobulin M
Immunoglobulins
Anti-Idiotypic Antibodies
Quenching
Nucleotides
Immunoglobulin G

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

The effect of somatic mutation on antibody affinity. / Gearhart, P. J.

In: Annals of the New York Academy of Sciences, Vol. VOL. 418, 1983, p. 171-176.

Research output: Contribution to journalArticle

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