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• W2321747029 abstract "Site-directed mutagenesis has been used to examine the importance of histidine-99 in the VH CDR3 region of a mouse/human chimeric anti-TAG72 antibody, cB72.3-1-3. The expression vectors mpSV2neo-EPl-Vm4–10C.γ1, containing seven different mutant VH region fragments (Vm4–10) in association with the immunoglobulin enhancer (E), promoter (P1) and human genomic Cγ1 region fragments, were transfected into a heavy chain loss mutant cell line B72.3Mut(K), respectively. Mutant chimeric antibodies cB72.3m4–10 were purified from the transfectant supernates, and their binding affinities for the TAG72 antigen relative to that of the original cB72.3-1-3 antibody were compared. Substitution of histidine-99 by glutamine resulted in a higher affinity antibody (cB72.3m4) whereas substitution by isoleucine resulted in a lower affinity antibody (cB72.3m9). The binding affinity of these mutant antibodies varied nearly eight-fold. It was concluded that the residue at position 99 in the VH CDR3 region is in a ‘contact’ position in the B72.3/TAG72 antibody-combining site. The polar side-chains of glutamine and asparagine or the ionized side-chains of histidine, arginine or glutamic acid contribute to higher binding affinity, whereas the hydrophobic side-chains of isoleucine, leucine or phenylalanine resulted in a lower binding affinity for the TAG72 antigen." @default.
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• W2321747029 date "1993-08-01" @default.
• W2321747029 modified "2023-09-26" @default.
• W2321747029 title "Differences in antigen-binding affinity caused by single amino acid substitution in the variable region of the heavy chain" @default.
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• W2321747029 doi "https://doi.org/10.1038/icb.1993.28" @default.
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