Superantigens: interaction of staphylococcal enterotoxins with MHC class II molecules.

RR Rich, JA Mollick, RG Cook - Transactions of the American …, 1990 - ncbi.nlm.nih.gov
We have shown that the staphylococcal enterotoxins and TSST specifically bind to MHC
class II molecules. This binding to class II molecules is a prerequisite for the function of these …

Staphylococcal enterotoxin A and toxic shock syndrome toxin compete with CD4 for human major histocompatibility complex class II binding

S Bavari, RG Ulrich - Infection and immunity, 1995 - Am Soc Microbiol
We have examined the role of the CD4 molecule in primary T-lymphocyte responses to the
staphylococcal enterotoxins SEA, SEB, SEC1, and the toxic shock syndrome toxin TSST-1 …

Inhibition of antigen-specific T cell activation by staphylococcal enterotoxins.

JE Dowd, RN Jenkins, DR Karp - Journal of immunology (Baltimore …, 1995 - journals.aai.org
The staphylococcal enterotoxins SEA, SEB, SEC2, and TSST-1 bind to MHC class II
molecules and stimulate polyclonal T cell populations on the basis of the expression of …

Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site

AC Papageorgiou, KR Acharya, R Shapiro… - Structure, 1995 - cell.com
Background: Staphylococcus aureus enterotoxin C2 (SEC2) belongs to a family of proteins,
termed 'superantigens', that form complexes with class II MHC molecules enabling them to …

Molecular structure of staphylococcus and streptococcus superantigens

PM Schlievert, GA Bohach, DH Ohlendorf… - Journal of clinical …, 1995 - Springer
Staphylococcus aureus and streptococci, notably those belonging to group A, make up a
large family of true exotoxins referred to as pyrogenic toxin superantigens. These toxins …

Biochemical and mutational analysis of the histidine residues of staphylococcal enterotoxin A

M Hoffman, M Tremaine, J Mansfield… - Infection and …, 1996 - Am Soc Microbiol
The goal of this study was to examine the role of histidine residues in the biological activities
of staphylococcal enterotoxin A (SEA). Carboxymethylated SEA was unable to stimulate …

Multiple Binding-Sites on the Superantigen, Staphylococcal Enterotoxin B, Imparts Versatility in Binding to MHC Class II Molecules

JM Soos, HM Johnson - Biochemical and biophysical research …, 1994 - Elsevier
To determine MHC class II molecule binding regions of staphylococcal enterotoxin B (SEB),
we employed a structurally based approach in which eight overlapping peptides of the entire …

A mutational analysis of the binding of staphylococcal enterotoxins B and C3 to the T cell receptor β chain and major histocompatibility complex class II

L Leder, A Llera, PM Lavoie, MI Lebedeva… - The Journal of …, 1998 - rupress.org
The three-dimensional structure of the complex between a T cell receptor (TCR) β chain
(mouse Vβ8. 2Jβ2. 1Cβ1) and the superantigen (SAG) staphylococcal enterotoxin C3 …

Localization of the immunologic activity in the superantigen Staphylococcal enterotoxin B using truncated recombinant fusion proteins.

R Buelow, RE O'Hehir, R Schreifels… - … (Baltimore, Md.: 1950 …, 1992 - journals.aai.org
The exotoxins of certain strains of Staphylococcus aureus strains are able both to stimulate
potent proliferation and induce anergy in T lymphocytes expressing the appropriate T cell Ag …

Staphylococcus aureus.

GC Stewart - 2005 - cabidigitallibrary.org
Staphylococcus aureus is a common cause of confirmed bacterial foodborne disease
worldwide. Food poisoning episodes are characterized by symptoms of vomiting and …