PMID: 6162196Jan 1, 1980Paper

Cross-reacting xenoantibodies to the heavy chain of H-2 and HLA-A,B antigens: serologic and immunochemical characterization

Scandinavian Journal of Immunology
G N CallahanS Ferrone

Abstract

H-2 cross-reactive antibodies present in HLA xenoantisera were purified by absorption on and elution from murine cells. Antibodies isolated from one of these antisera, 78-E48, were found to mediate complement-dependent lysis of both human and murine lymphoid cells but not of Daudi cells or of human lymphoid cells coated with Fab2 fragments from a cow anti-human beta 2-microglobulin (beta 2 m) antiserum. In indirect immunoprecipitation analyses 78-E48 reacted only with proteins of approximately 45,000 and 12,000 MW present in NP-40 extracts of both human and murine lymphoid cells. Sequential precipitation experiments with rabbit anti-human beta 2 m and allo-anti-H-2Kk, Iak sera established that these proteins were in fact H-2 and HLA-A,B antigens. It was also found that 78-E48 reacted only with the heavy chain of HLA-A,b and H-2 antigens, since this eluate was unreactive with beta 2 m in a radioimmunoassay, and its capacity to immunoprecipitate the 45,000 and 12,000 MW proteins from human cell extracts was unaffected by prior reaction with purified human beta 2 m. These data show for the first time that H-2 and HLA-A,B antigens share properties that probably depend upon their teritary structure.

References

Mar 1, 1976·Somatic Cell Genetics·H E FaberO Smithies
Jan 1, 1978·Advances in Immunology·E S Vitetta, J D Capra
Jul 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·O HenriksenE Appella
Dec 1, 1973·The Journal of Experimental Medicine·H M GreyJ L Strominger

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