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The bacterial superantigen and superantigen‐like proteins
This family of structurally related molecules highlights how a common pathogenic organism has employed a simple but adaptable protein to generate an armamentarium of potent defense molecules designed to target of the innate and adaptive immune response. Expand
Bacterial superantigens
A review provides a summary of the field to date with some of the more recent discoveries that shed light on the how superantigens are able to trigger such strong T cell responses and the diseases related to SAg intoxication. Expand
The Staphylococcal Superantigen-Like Protein 7 Binds IgA and Complement C5 and Inhibits IgA-FcαRI Binding and Serum Killing of Bacteria1
RSSL7 is a superantigen-like protein secreted from Staphylococcus aureus that blocks IgA-FcR interactions and inhibits complement, leading to increased survival of a sensitive bacterium in blood. Expand
Kaposi's sarcoma-associated herpesvirus infection of bone marrow dendritic cells from multiple myeloma patients.
Kaposi's sarcoma-associated herpesvirus (KSHV) was found in the bone marrow dendritic cells of multiple myeloma patients but not in malignant plasma cells or bone marrow dendritic cells from normalExpand
Identification and Characterization of Novel Superantigens from Streptococcus pyogenes
Evidence from modeled protein structures and competitive binding experiments suggest that high affinity binding of each toxin is to the major histocompatibility complex class II β chain, which might reflect a specific role for this subset of Vβs in the immune defense of gram-positive bacteria. Expand
High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR
Examining the initial events in SEA and SEB T-cell activation shows that MHC restriction results from a direct high affinity binding by intact SEA andSEB to the same site on MHC class II HLA-DR antigens. Expand
The Superantigen Streptococcal Pyrogenic Exotoxin C (SPE-C) Exhibits a Novel Mode of Action
Nondenaturing sodium dodecyl sulfate electrophoresis and size exclusion chromatography revealed that both wild-type and recombinant SPE-C exist in a stable dimer at neutral or alkaline pH and reveal yet another mechanism by which bacterial superantigens ligate and cross-link MHC class II. Expand
Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II
SEA requires two separate binding sites for optimal activity, which may allow it to stabilize SEA interaction with T cell receptors, as well as to activate the antigen-presenting cell by cross-linking MHC class II. Expand
Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules
The three-dimensional structure of a Streptococcal superantigen, SPE-C, is determined and consideration of the SPe-C dimer suggests a novel mechanism for promotion of MHC aggregation and T-cell activation. Expand
Two Novel Superantigens Found in Both Group A and Group C Streptococcus
The results suggest that both genes are located on a mobile element that enables gene transfer between individual isolates and between streptococci from different Lancefield groups, and both proteins bind major histocompatibility complex class II at the β-chain, but not at the α-chain. Expand