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.
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.
The Staphylococcal Superantigen-Like Protein 7 Binds IgA and Complement C5 and Inhibits IgA-FcαRI Binding and Serum Killing of Bacteria1
- R. Langley, B. Wines, N. Willoughby, I. Basu, T. Proft, J. Fraser
- BiologyJournal of Immunology
- 1 March 2005
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.
Identification and Characterization of Novel Superantigens from Streptococcus pyogenes
- T. Proft, S. Louise Moffatt, Celia J. Berkahn, J. Fraser
- BiologyJournal of Experimental Medicine
- 4 January 1999
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.
Kaposi's sarcoma-associated herpesvirus infection of bone marrow dendritic cells from multiple myeloma patients.
- M. Rettig, H. Ma, J. Berenson
- Biology, MedicineScience
- 20 June 1997
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 normal…
High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR
- J. Fraser
- Biology, MedicineNature
- 18 May 1989
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.
Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II
- K. Hudson, R. Tiedemann, R. Urban, S. C. Lowe, J. Strominger, J. Fraser
- BiologyJournal of Experimental Medicine
- 1 September 1995
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.
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, B. Anderson, H. Baker, J. Fraser, E. Baker
- Biology, MedicineNature Structural Biology
- 1 August 1997
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.
Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus
- N. S. Laursen, N. Gordon, G. Andersen
- BiologyProceedings of the National Academy of Sciences…
- 23 February 2010
The results provide a conceptual and structural basis for the development of a highly specific complement inhibitor preventing only the formation of the lytic membrane attack complex without affecting the important signaling functions of C5a.
Two Novel Superantigens Found in Both Group A and Group C Streptococcus
- T. Proft, Phillip D Webb, V. Handley, J. Fraser
- BiologyInfection and Immunity
- 1 March 2003
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.
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