| 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 | ||||||||
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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.
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.
The structure of the C-terminal domain has been solved and shown to have a C-lectin type of structure.[1]
This article incorporates text from the public domain Pfam and InterPro IPR013117