NASA Logo

NTRS

NTRS - NASA Technical Reports Server

Back to Results
Complex high affinity interactions occur between MHCI and superantigensStaphylococcal enterotoxins A and C1 (SEA or SEC1) bound to major histocompatibility-I (MHCI) molecules with high affinity (binding constants ranging from 1.1 microM to 79 nM). SEA and SEC1 directly bound MHCI molecules that had been captured by monoclonal antibodies specific for H-2Kk, H-2Dk, or both. In addition, MHCI-specific antibodies inhibited the binding of SEC1 to LM929 cells and SEA competitively inhibited SEC1 binding; indicating that the superantigens bound to MHCI on the cell surface. The affinity and number of superantigen binding sites differed depending on whether MHCI was expressed in the membrane of LM929 cells or whether it was captured. These data support the hypothesis that MHCI molecules can serve as superantigen receptors.
Document ID
20040142162
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Chapes, S. K.
(Kansas State University Manhattan 66506-4901, United States)
Herpich, A. R.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
November 1, 1998
Publication Information
Publication: Journal of leukocyte biology
Volume: 64
Issue: 5
ISSN: 0741-5400
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Cell Biology
Non-NASA Center

Available Downloads

There are no available downloads for this record.
No Preview Available