Enterotoxin

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Stap_Strp_tox_C
PDB 1uns EBI.jpg
identification of a secondary zinc-binding site in staphylococcal enterotoxin c2: implications for superantigen recognition
Identifiers
Symbol Stap_Strp_tox_C
Pfam PF02876
Pfam clan CL0386
InterPro IPR006123
PROSITE PDOC00250
SCOP 1se3
SUPERFAMILY 1se3
OPM superfamily 429
OPM protein 1dyq

An enterotoxin (not to be confused with endotoxin) is a protein exotoxin released by a microorganism that targets the intestines. Its target site is indicated within its name.[1][clarification needed]

Enterotoxins are chromosomally encoded exotoxins that are produced and secreted from several bacterial organisms. They are often heat-stable, and are of low molecular weight and water-soluble. Enterotoxins are frequently cytotoxic and kill cells by altering the apical membrane permeability of the mucosal (epithelial) cells of the intestinal wall. They are mostly pore-forming toxins (mostly chloride pores), secreted by bacteria, that assemble to form pores in cell membranes. This causes the cells to die.

Clinical significance[edit]

Enterotoxins have a particularly marked effect upon the gastrointestinal tract, causing vomiting, diarrhea, and abdominal pain. The action of enterotoxins leads to increased chloride ion permeability of the apical membrane of intestinal mucosal cells. These membrane pores are activated either by increased cAMP or by increased calcium ion concentration intracellularly. The pore formation has a direct effect on the osmolarity of the luminal contents of the intestines. Increased chloride permeability leads to leakage into the lumen followed by sodium and water movement. This leads to a secretory diarrhea within a few hours of ingesting enterotoxin. Several microbial organisms contain the necessary enterotoxin to create such an effect, such as Staphylococcus aureus and E. coli.

Classification and 3D structures of enterotoxins[edit]

Bacterial[edit]

Staphylococcal enterotoxins and streptococcal pyrogenic exotoxins constitute a family of biologically and structurally related toxins produced by Staphylococcus aureus and Streptococcus pyogenes.[2][3] These toxins share the ability to bind to the major histocompatibility complex proteins of their hosts. A more distant relative of the family is the S. aureus toxic shock syndrome toxin, which shares only a low level of sequence similarity with this group.

All of these toxins share a similar two-domain fold (N and C-terminal domains) with a long alpha-helix in the middle of the molecule, a characteristic beta-barrel known as the "oligosaccharide/oligonucleotide fold" at the N-terminal domain and a beta-grasp motif at the C-terminal domain. Examples include enterotoxin type B. Each superantigen possesses slightly different binding mode(s) when it interacts with MHC class II molecules or the T-cell receptor.[4]

The beta-grasp domain has some structural similarities to the beta-grasp motif present in immunoglobulin-binding domains, ubiquitin, 2Fe-2 S ferredoxin and translation initiation factor 3 as identified by the SCOP database.

Viral[edit]

See also[edit]

References[edit]

  1. ^ "enterotoxin" at Dorland's Medical Dictionary
  2. ^ Iandolo JJ (1989). "Genetic analysis of extracellular toxins of Staphylococcus aureus". Annu. Rev. Microbiol. 43: 375–402. doi:10.1146/annurev.mi.43.100189.002111. PMID 2679358. 
  3. ^ Marrack P, Kappler J (May 1990). "The staphylococcal enterotoxins and their relatives". Science 248 (4956): 705–11. doi:10.1126/science.2185544. PMID 2185544. 
  4. ^ Papageorgiou AC, Tranter HS, Acharya KR (March 1998). "Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors". J. Mol. Biol. 277 (1): 61–79. doi:10.1006/jmbi.1997.1577. PMID 9514739. 
  5. ^ Katahira J, Sugiyama H, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N (October 1997). "Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo". The Journal of Biological Chemistry 272 (42): 26652–8. doi:10.1074/jbc.272.42.26652. PMID 9334247. 
  6. ^ a b Enterotoxins at the US National Library of Medicine Medical Subject Headings (MeSH)
  7. ^ "eMedicine - CBRNE - Staphylococcal Enterotoxin B : Article by Danielle M Pesce". Retrieved 2008-11-08. 

This article incorporates text from the public domain Pfam and InterPro IPR006123