Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules

A Roussel, BF Anderson, HM Baker, JD Fraser… - Nature Structural …, 1997 - nature.com
Bacterial superantigens are small proteins that have a very potent stimulatory effect on T
lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors …

Structural basis for HLA–DQ binding by the streptococcal superantigen SSA

E Sundberg, TS Jardetzky - nature structural biology, 1999 - nature.com
Streptococcal superantigen (SSA) is a 28,000 M r toxin originally isolated from a pathogenic
strain of Streptococcus pyogenes that has 60% sequence identity with staphylococcal …

[HTML][HTML] Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II

Y Li, H Li, N Dimasi, JK McCormick, R Martin, P Schuck… - Immunity, 2001 - cell.com
MHC class II molecules possess two binding sites for bacterial superantigens (SAGs): a low-
affinity site on the α chain and a high-affinity, zinc-dependent site on the β chain. Only the …

Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 Å resolution: implications for superantigen recognition by MHC class II molecules and T …

AC Papageorgiou, HS Tranter, KR Acharya - Journal of molecular biology, 1998 - Elsevier
Staphylococcal enterotoxin B is a member of a family of toxins known as superantigens that
activate a large number of T-cells (up to 20%) by cross-linking MHC class II molecules with T …

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens

JNP Brouillard, S Günther, AK Varma, I Gryski… - Journal of molecular …, 2007 - Elsevier
Superantigens (SAgs) are potent microbial toxins that bind simultaneously to T cell receptors
(TCRs) and class II major histocompatibility complex molecules, resulting in the activation …

Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1

KR Acharya, EF Passalacqua, EY Jones, K Harlos… - Nature, 1994 - nature.com
SUPERANTIGENS stimulate T cells bearing particular T-cell receptor Vβ sequences1, 2, so
they are extremely potent polyclonal T-cell mitogens. T-cell activation is preceded by binding …

Crystal structure of a T-cell receptor β-chain complexed with a superantigen

BA Fields, EL Malchiodi, H Li, X Ysern, CV Stauffacher… - Nature, 1996 - nature.com
SUPERANTIGENS (SAgs) are viral or bacterial proteins that act as potent T-cell stimulants
and have been implicated in a number of human diseases, including toxic shock …

[HTML][HTML] Three-dimensional structure of the complex between a T cell receptor β chain and the superantigen staphylococcal enterotoxin B

H Li, A Llera, D Tsuchiya, L Leder, X Ysern… - Immunity, 1998 - cell.com
Superantigens (SAGs) are a class of immunostimulatory proteins of bacterial or viral origin
that activate T cells by binding to the Vβ domain of the T cell antigen receptor (TCR). The …

[HTML][HTML] Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule

MM Fernández, R Guan, CP Swaminathan… - Journal of Biological …, 2006 - ASBMB
Superantigens are bacterial or viral proteins that elicit massive T cell activation through
simultaneous binding to major histocompatibility complex (MHC) class II and T cell …

The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action

PL Li, RE Tiedemann, SL Moffat… - The Journal of …, 1997 - rupress.org
Recombinant streptococcal pyrogenic exotoxin C (SPE-C) is a potent superantigen that
stimulates Vβ2-bearing human T cells, but is inactive in mice. SPE-C binds with high affinity …