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© Research
Publication : The EMBO journal

Antibody engineering for the analysis of affinity maturation of an anti-hapten response

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The EMBO journal - 01 Jul 1988

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

Link to Pubmed [PMID] – 3138111

EMBO J. 1988 Jul;7(7):1995-2001

The influence of structural variation, previously observed in a panel of V186.2 VH/V lambda 1-expressing anti-NP antibodies from the secondary response, on the affinity of these antibodies was examined by site-specific mutagenesis and recombinant antibody construction. A tryptophan—-leucine exchange at position 33 in the VH segment of all but one of the high-affinity antibodies is the most frequently observed somatic mutation and by itself leads to a 10-fold higher affinity; all other somatic exchanges are irrelevant for affinity selection. In the single case of a high-affinity antibody without this common exchange, high affinity is mediated by a combination of mutations (including a one-codon deletion) in VH and the particular D-JH rearrangement carried by this antibody. The data indicate that the pattern of somatic diversification through hypermutation is shaped by affinity selection, but that only a single point mutation is available in the VH and the VL gene of lambda 1 chain-bearing anti-NP antibodies which by itself leads to an increase of hapten-binding affinity. Based on the analysis of two secondary response antibodies from which somatic mutations in VH and VL have been eliminated, it is also concluded that the recruitment of B cell clones into the pathway of hypermutation involves a mechanism which is not based upon affinity differences towards the antigen.

http://www.ncbi.nlm.nih.gov/pubmed/3138111