Intimin

From Wikipedia, the free encyclopedia
Intimin C-type lectin domain

nmr representative structure of intimin-190 (int190) from enteropathogenic e. coli
Identifiers
Symbol Intimin_C
Pfam PF07979
Pfam clan CL0056
InterPro IPR013117

Intimin is a virulence factor (adhesin) of EPEC (e.g. E. coli O127:H6) and EHEC (e.g. E. coli O157:H7) E. coli strains. It is an attaching and effacing (A/E) protein which with other virulence factors is responsible for enteropathogenic and enterohaemorrhagic diarrhoea.[1]

Intimin is expressed on the bacterial cell surface where it can bind to its receptor Tir (Translocated intimin receptor). Tir, along with over 25 other bacterial proteins, is secreted from attaching and effacing E. coli directly into the cytoplasm of intestinal epithelial cells by a Type three secretion system. Once within the cytoplasm of the host cell, Tir is inserted into the plasma membrane, allowing surface exposure and intimin binding.[1]

The structure of the C-terminal domain has been solved and shown to have a C-lectin type of structure.[2]

References

  1. 1.0 1.1 Stevens, J. et al. (2006). "Actin-dependent movement of bacterial pathogens". Nature Reviews Microbiology 4: 91–101. doi:10.1038/nrmicro1320. PMID 16415925. 
  2. Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S (June 2000). "Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli". EMBO J. 19 (11): 2452–64. doi:10.1093/emboj/19.11.2452. PMC 212744. PMID 10835344. 

This article incorporates text from the public domain Pfam and InterPro IPR013117


This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.