Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain

MM Fernández, S Cho, MC De Marzi, MC Kerzic… - Journal of Biological …, 2011 - ASBMB
Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules
and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads …

Superantigen natural affinity maturation revealed by the crystal structure of staphylococcal enterotoxin G and its binding to T‐cell receptor Vβ8. 2

MM Fernández, S Bhattacharya… - PROTEINS …, 2007 - Wiley Online Library
The illnesses associated with bacterial superantigens (SAgs) such as food poisoning and
toxic shock syndrome, as well as the emerging threat of purpura fulminans and community …

Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization

HM Baker, T Proft, PD Webb, VL Arcus… - Journal of Biological …, 2004 - ASBMB
The protein toxins known as superantigens (SAgs), which are expressed primarily by the
pathogenic bacteria Staphylococcus aureus and Streptococcus pyogenes, are highly potent …

Structure of staphylococcal enterotoxin N: Implications for binding properties to its cellular proteins

C Zeng, Z Liu, Z Han - International Journal of Molecular Sciences, 2019 - mdpi.com
Staphylococcus aureus strains produce a unique family of immunostimulatory exotoxins
termed as bacterial superantigens (SAgs), which cross-link major histocompatibility complex …

[HTML][HTML] The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation

M Saline, KEJ Rödström, G Fischer, VY Orekhov… - Nature …, 2010 - nature.com
Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor
(TCR) and major histocompatibility complex (MHC) class II, conventionally through the …

A novel loop domain in superantigens extends their T cell receptor recognition site

S Günther, AK Varma, B Moza, KJ Kasper… - Journal of molecular …, 2007 - Elsevier
Superantigens (SAGs) interact with host immune receptors to induce a massive release of
inflammatory cytokines that can lead to toxic shock syndrome and death. Bacterial SAGs can …

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 …

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 …

Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus …

VL Arcus, T Proft, JA Sigrell, HM Baker… - Journal of molecular …, 2000 - Elsevier
Bacterial superantigens (SAgs) are a structurally related group of protein toxins secreted by
Staphylococcus aureus and Streptococcus pyogenes. They are implicated in a range 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 …