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 …
strain of Streptococcus pyogenes that has 60% sequence identity with staphylococcal …
Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules
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 …
lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors …
Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II
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 …
affinity site on the α chain and a high-affinity, zinc-dependent site on the β chain. Only the …
Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization
The protein toxins known as superantigens (SAgs), which are expressed primarily by the
pathogenic bacteria Staphylococcus aureus and Streptococcus pyogenes, are highly potent …
pathogenic bacteria Staphylococcus aureus and Streptococcus pyogenes, are highly potent …
Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus …
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 …
Staphylococcus aureus and Streptococcus pyogenes. They are implicated in a range of …
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 …
activate a large number of T-cells (up to 20%) by cross-linking MHC class II molecules with T …
[引用][C] Superantigens—remnants of a past process?
JD Fraser, KR Hudson - Research in immunology, 1993 - Elsevier
Superantigens (SAg) bind simultaneously to T-cell receptors (TcR) and major
histocompatibility complex (MHC) class II molecules to activate up to 20 '7'0 of all peripheral …
histocompatibility complex (MHC) class II molecules to activate up to 20 '7'0 of all peripheral …
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) …
(MHC) class II molecules and with the V beta portion of a T cell antigen receptor (TCR) …
Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
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 …
and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads …
[HTML][HTML] Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
K Petersson, M Håkansson, H Nilsson… - The EMBO …, 2001 - embopress.org
The three‐dimensional structure of a bacterial superantigen, Staphylococcus aureus
enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA …
enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA …