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Staphylococcal enterotoxins bind H-2Db molecules on macrophagesWe screened a panel of monoclonal antibodies against selected macrophage cell surface molecules for their ability to inhibit enterotoxin binding to major histocompatibility complex class II-negative C2D (H-2b) macrophages. Two monoclonal antibodies, HB36 and TIB126, that are specific for the alpha 2 domain of major histocompatibility complex class I, blocked staphylococcal enterotoxins A and B (SEA and SEB, respectively) binding to C2D macrophages in a specific and concentration-dependent manner. Inhibitory activities were haplotype-specific in that SEA and SEB binding to H-2k or H-2d macrophages was not inhibited by either monoclonal antibody. HB36, but not TIB126, inhibited enterotoxin-induced secretion of cytokines by H-2b macrophages. Lastly, passive protection of D-galactosamine-sensitized C2D mice by injection with HB36 antibody prevented SEB-induced death. Therefore, SEA and SEB binding to the alpha 2 domain of the H-2Db molecule induces biological activity and has physiological consequences.
Document ID
20050000170
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Beharka, A. A.
(Kansas State University Manhattan 66506, United States)
Iandolo, J. J.
Chapes, S. K.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
July 3, 1995
Publication Information
Publication: Proceedings of the National Academy of Sciences of the United States of America
Volume: 92
Issue: 14
ISSN: 0027-8424
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: AI-17474
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Cell Biology

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