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Volume 270, Number 21, Issue of May 26, pp. 12457-12465, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Katherine G. Nickerson , Mi-Hua Tao , Hua-Tang Chen , James Larrick , Elvin A. Kabat

A human monoclonal antibody (HuA) specific for blood group A substance with two fucose groups was found to be immunochemically almost identical with that of a previously characterized mouse monoclonal anti-A, AC-1001. The V and V chain cDNAs of HuA were sequenced and compared with those of AC-1001. The human and mouse antibodies used V and V genes that came from different families and shared minimal nucleotide and amino acid sequence identity. Thus, two antibodies from two different species can use evolutionarily unrelated sequences to bind the same carbohydrate epitope.

The cloned HuA V and V genes were then transfected into a mouse myeloma cell line and re-expressed, together, and each separately with an irrelevant V or V. Only the original HuA V and V had anti-A activity, demonstrating that both the heavy and light chains contributed to specificity.

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