Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 Å resolution: Implications for superantigen recognition by MHC class II molecules and T-cell receptors

Anastassios C. Papageorgiou, Howard S. Tranter, K. Ravi Acharya

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

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-cell receptors in a Vβ-restricted fashion. The crystal structure of staphylococcal enterotoxin B presented here has been determined at 1.5 Å resolution, the highest resolution so far for a superantigen. The final model contains 1948 protein atoms and 177 water molecules and has excellent geometry with root-mean-square (rms) deviation of 0.007 Å and 1.73°in bond lengths and bond angles, respectively. The overall fold is similar to that of other microbial superantigens, but as it lacks the zinc-binding site found in other members of this family, such as staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC class II binding site. Comparison of the crystal structure of free SEE and in complex with an MHC class II molecule revealed no major changes in the MHC-binding site upon complex formation. However, a number of water molecules found in the free SEB may be displaced in the complex or contribute further to its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2 shows significant differences which may account for the ability of each superantigen to bind specific Vβ sequences.

Original languageEnglish
Pages (from-to)61-79
Number of pages19
JournalJournal of Molecular Biology
Volume277
Issue number1
DOIs
Publication statusPublished - 20 Mar 1998

Keywords

  • Major histocompatibility complex
  • Staphylococcal enterotoxin B
  • Superantigens
  • T-cell receptor
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

@article{3871ee26771e4d598734f548be99db2f,
title = "Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 {\AA} resolution: Implications for superantigen recognition by MHC class II molecules and T-cell receptors",
abstract = "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-cell receptors in a Vβ-restricted fashion. The crystal structure of staphylococcal enterotoxin B presented here has been determined at 1.5 {\AA} resolution, the highest resolution so far for a superantigen. The final model contains 1948 protein atoms and 177 water molecules and has excellent geometry with root-mean-square (rms) deviation of 0.007 {\AA} and 1.73°in bond lengths and bond angles, respectively. The overall fold is similar to that of other microbial superantigens, but as it lacks the zinc-binding site found in other members of this family, such as staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC class II binding site. Comparison of the crystal structure of free SEE and in complex with an MHC class II molecule revealed no major changes in the MHC-binding site upon complex formation. However, a number of water molecules found in the free SEB may be displaced in the complex or contribute further to its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2 shows significant differences which may account for the ability of each superantigen to bind specific Vβ sequences.",
keywords = "Major histocompatibility complex, Staphylococcal enterotoxin B, Superantigens, T-cell receptor, X-ray crystallography",
author = "Papageorgiou, {Anastassios C.} and Tranter, {Howard S.} and Acharya, {K. Ravi}",
year = "1998",
month = "3",
day = "20",
doi = "10.1006/jmbi.1997.1577",
language = "English",
volume = "277",
pages = "61--79",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 Å resolution

T2 - Implications for superantigen recognition by MHC class II molecules and T-cell receptors

AU - Papageorgiou, Anastassios C.

AU - Tranter, Howard S.

AU - Acharya, K. Ravi

PY - 1998/3/20

Y1 - 1998/3/20

N2 - 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-cell receptors in a Vβ-restricted fashion. The crystal structure of staphylococcal enterotoxin B presented here has been determined at 1.5 Å resolution, the highest resolution so far for a superantigen. The final model contains 1948 protein atoms and 177 water molecules and has excellent geometry with root-mean-square (rms) deviation of 0.007 Å and 1.73°in bond lengths and bond angles, respectively. The overall fold is similar to that of other microbial superantigens, but as it lacks the zinc-binding site found in other members of this family, such as staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC class II binding site. Comparison of the crystal structure of free SEE and in complex with an MHC class II molecule revealed no major changes in the MHC-binding site upon complex formation. However, a number of water molecules found in the free SEB may be displaced in the complex or contribute further to its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2 shows significant differences which may account for the ability of each superantigen to bind specific Vβ sequences.

AB - 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-cell receptors in a Vβ-restricted fashion. The crystal structure of staphylococcal enterotoxin B presented here has been determined at 1.5 Å resolution, the highest resolution so far for a superantigen. The final model contains 1948 protein atoms and 177 water molecules and has excellent geometry with root-mean-square (rms) deviation of 0.007 Å and 1.73°in bond lengths and bond angles, respectively. The overall fold is similar to that of other microbial superantigens, but as it lacks the zinc-binding site found in other members of this family, such as staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC class II binding site. Comparison of the crystal structure of free SEE and in complex with an MHC class II molecule revealed no major changes in the MHC-binding site upon complex formation. However, a number of water molecules found in the free SEB may be displaced in the complex or contribute further to its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2 shows significant differences which may account for the ability of each superantigen to bind specific Vβ sequences.

KW - Major histocompatibility complex

KW - Staphylococcal enterotoxin B

KW - Superantigens

KW - T-cell receptor

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=0032549518&partnerID=8YFLogxK

U2 - 10.1006/jmbi.1997.1577

DO - 10.1006/jmbi.1997.1577

M3 - Article

C2 - 9514739

AN - SCOPUS:0032549518

VL - 277

SP - 61

EP - 79

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -