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© Research
Publication : International journal of cancer. Supplement = Journal international du cancer. Supplement

Modulation of antibody binding affinity by somatic mutation

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in International journal of cancer. Supplement = Journal international du cancer. Supplement - 01 Jan 1988

Allen D, Cumano A, Simon T, Sablitzky F, Rajewsky K

Link to Pubmed [PMID] – 3264819

Int. J. Cancer Suppl. 1988;3:1-8

The affinity of hapten binding of monoclonal antibodies (MAbs) specific for 4-hydroxy-3-nitrophenylacetyl (NP) has been investigated at the molecular level by both site-specific mutagenesis and recombinant antibody construction, followed by expression in myeloma cells. We have shown that a single point mutation (trp—-leu at codon 33) in the variable region of the heavy chain (VH) is sufficient to endow a primary-response, germline-encoded antibody with an affinity for antigen typical of a secondary-response antibody carrying the same mutation. We have also demonstrated that mutations additional to the trp—-leu exchange in the heavy chain and further mutations in the light chain are irrelevant to the high-affinity phenotype of secondary-response antibodies. Since some of these are “parallel” mutations common to clonally unrelated antibodies, this suggests that the mutation rate is not constant across the entire immunoglobulin variable region. Although antibodies with a trp—-leu exchange at position 33 are positively selected because of improved hapten binding affinity, we have found that, under rare circumstances, other patterns of mutations may be selected through particular D-JH combinations; we have demonstrated one case where this has generated an antibody with very efficient hapten binding ability.

http://www.ncbi.nlm.nih.gov/pubmed/3264819