Literature DB >> 9881971

Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B.

H Li1, A Llera, D Tsuchiya, L Leder, X Ysern, P M Schlievert, K Karjalainen, R A Mariuzza.   

Abstract

Superantigens (SAGs) are a class of immunostimulatory proteins of bacterial or viral origin that activate T cells by binding to the V beta domain of the T cell antigen receptor (TCR). The three-dimensional structure of the complex between a TCR beta chain (mouse V beta8.2) and the SAG staphylococcal enterotoxin B (SEB) at 2.4 A resolution reveals why SEB recognizes only certain V beta families, as well as why only certain SAGs bind mouse V beta8.2. Models of the TCR-SEB-peptide/MHC class II complex indicate that V alpha interacts with the MHC beta chain in the TCR-SAG-MHC complex. The extent of the interaction is variable and is largely determined by the geometry of V alpha/V beta domain association. This variability can account for the preferential expression of certain V alpha regions among T cells reactive with SEB.

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Year:  1998        PMID: 9881971     DOI: 10.1016/s1074-7613(00)80646-9

Source DB:  PubMed          Journal:  Immunity        ISSN: 1074-7613            Impact factor:   31.745


  63 in total

1.  Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity.

Authors:  M Graille; E A Stura; A L Corper; B J Sutton; M J Taussig; J B Charbonnier; G J Silverman
Journal:  Proc Natl Acad Sci U S A       Date:  2000-05-09       Impact factor: 11.205

Review 2.  Exotoxins of Staphylococcus aureus.

Authors:  M M Dinges; P M Orwin; P M Schlievert
Journal:  Clin Microbiol Rev       Date:  2000-01       Impact factor: 26.132

3.  Toxoids of streptococcal pyrogenic exotoxin A are protective in rabbit models of streptococcal toxic shock syndrome.

Authors:  M Roggiani; J A Stoehr; S B Olmsted; Y V Matsuka; S Pillai; D H Ohlendorf; P M Schlievert
Journal:  Infect Immun       Date:  2000-09       Impact factor: 3.441

4.  Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha.

Authors:  Heike I Krupka; Brent W Segelke; Robert G Ulrich; Sabine Ringhofer; Mark Knapp; Bernhard Rupp
Journal:  Protein Sci       Date:  2002-03       Impact factor: 6.725

Review 5.  Bacterial superantigens.

Authors:  T Proft; J D Fraser
Journal:  Clin Exp Immunol       Date:  2003-09       Impact factor: 4.330

6.  Peptide antagonists of superantigen toxins.

Authors:  Raymond Kaempfer
Journal:  Mol Divers       Date:  2004       Impact factor: 2.943

7.  The T cell receptor beta-chain second complementarity determining region loop (CDR2beta governs T cell activation and Vbeta specificity by bacterial superantigens.

Authors:  A K M Nur-ur Rahman; Daniel A Bonsor; Christine A Herfst; Fraser Pollard; Michael Peirce; Aaron W Wyatt; Katherine J Kasper; Joaquín Madrenas; Eric J Sundberg; John K McCormick
Journal:  J Biol Chem       Date:  2010-12-02       Impact factor: 5.157

8.  The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation.

Authors:  Maria Saline; Karin E J Rödström; Gerhard Fischer; Vladislav Yu Orekhov; B Göran Karlsson; Karin Lindkvist-Petersson
Journal:  Nat Commun       Date:  2010-11-16       Impact factor: 14.919

9.  A single, engineered protein therapeutic agent neutralizes exotoxins from both Staphylococcus aureus and Streptococcus pyogenes.

Authors:  Ningyan Wang; Daiva M Mattis; Eric J Sundberg; Patrick M Schlievert; David M Kranz
Journal:  Clin Vaccine Immunol       Date:  2010-09-22

10.  Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule.

Authors:  Marisa M Fernández; Rongjin Guan; Chittoor P Swaminathan; Emilio L Malchiodi; Roy A Mariuzza
Journal:  J Biol Chem       Date:  2006-07-06       Impact factor: 5.157

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