Staphylococcal enterotoxins A and B share a common structural motif for binding class II major histocompatibility complex molecules

RG Ulrich, S Bavari, MA Olson - Nature structural biology, 1995 - nature.com
A comparative site-directed mutagenesis study of staphylococcal enterotoxins A and B was
undertaken to identify key amino-acid residues which govern interactions with major …

Identification of HLA-DR1 beta chain residues critical for binding staphylococcal enterotoxins A and E.

DR Karp, EO Long - The Journal of experimental medicine, 1992 - rupress.org
Superantigens are thought to make external contacts with major histocompatibility complex
(MHC) class II molecules and with the V beta portion of a T cell antigen receptor (TCR) …

Identification of the staphylococcal enterotoxin A superantigen binding site in the beta 1 domain of the human histocompatibility antigen HLA-DR.

A Herman, N Labrecque, J Thibodeau… - Proceedings of the …, 1991 - National Acad Sciences
The staphylococcal enterotoxin A (SEA) is a superantigen that must bind to class II
molecules of the major histocompatibility complex to be recognized by T cells. In humans …

Crystal structure of the superantigen staphylococcal enterotoxin type A.

EM Schad, I Zaitseva, VN Zaitsev, M Dohlsten… - The EMBO …, 1995 - embopress.org
Staphylococcal enterotoxins are prototype superantigens characterized by their ability to
bind to major histocompatibility complex (MHC) class II molecules and subsequently activate …

Crystal structure of staphylococcal enterotoxin B, a superantigen

S Swaminathan, W Furey, J Pletcher, M Sax - Nature, 1992 - nature.com
The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a
super-antigen, has been determined to a resolution of 2.5 Å. The unusual main-chain fold …

Isolation of HLA-DR1.(staphylococcal enterotoxin A) 2 trimers in solution.

RE Tiedemann, RJ Urban… - Proceedings of the …, 1995 - National Acad Sciences
Mutational studies indicate that the superantigen staphylococcal enterotoxin A (SEA) has
two separate binding sites for major histocompatibility complex (MHC) class II molecules …

[引用][C] Crystal and solution structures of superantigenic staphylococcal enterotoxins compared

BR Singh, FN Fu, DN Ledoux - Nature Structural Biology, 1994 - nature.com
Sir–The crystal structure of the superantigen staphylococcal enterotoxin B has recently been
published". On the basis of sequence homology and conserved amino-acid positions, a …

Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II.

KR Hudson, RE Tiedemann, RG Urban… - The Journal of …, 1995 - rupress.org
The superantigen staphylococcal enterotoxin A (SEA) binds to major histocompatibility
complex (MHC) class II molecules at two sites on either side of the peptide groove. Two …

Staphylococcal toxins bind to different sites on HLA-DR.

MM Chintagumpala, JA Mollick… - Journal of immunology …, 1991 - journals.aai.org
Staphylococcal enterotoxins (SE) and toxic shock syndrome toxin 1 (TSST-1) bind to MHC
class II molecules and the toxin-class II complexes induce proliferation of T cells bearing …

Molecular characterization and role in T cell activation of staphylococcal enterotoxin A binding to the HLA-DR alpha-chain.

J Thibodeau, M Dohlsten, I Cloutier… - … (Baltimore, Md.: 1950 …, 1997 - journals.aai.org
Superantigens bind to MHC class II-positive cells and stimulate T lymphocytes expressing
specific V beta regions of the TCR. Two distinct regions of staphylococcal enterotoxin A …