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Cross‐reacting Xenoantibodies to the Heavy Chain of H‐2 and HLA‐A, B Antigens: Serologic and Immunochemical Characterization
Author(s) -
CALLAHAN G. N.,
PELLEGRINO M. A.,
FERRONE S.
Publication year - 1980
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1980.tb00070.x
Subject(s) - antiserum , antigen , immunoprecipitation , radioimmunoassay , antibody , microbiology and biotechnology , human leukocyte antigen , chemistry , serology , epitope , biology , biochemistry , immunology
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 coaled with Fab 2 fragments from a cow anti‐human β 2 ‐microglobulin (β 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 β 2 m and allo‐anti‐H‐2K k , Ia k 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 β 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 β 2 m. These data show for the first time that H‐2 and HLA‐A, B antigens share properties that probably depend upon their tertiary structure.