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Int J Med Microbiol. 2001 Mar;290(8):683-91.

Intimin from Shiga toxin-producing Escherichia coli and its isolated C-terminal domain exhibit different binding properties for Tir and a eukaryotic surface receptor.

Author information

1
Institut f├╝r Medizinische Mikrobiologie, Justus-Liebig-Universit├Ąt, Giessen, Germany.

Abstract

The outer membrane protein intimin plays a crucial role in the attaching and effacing process employed by different enteropathogens to colonize the epithelial surface of their hosts. In this study we have characterized the C-terminal binding domain of intimin from the Shiga toxin-producing Escherichia coli strain 413/89-1, that belongs to the beta-subtype of intimins. We found that a fusion of this domain to the maltose-binding protein binds efficiently to both the translocated intimin receptor (Tir) and the surface of uninfected eukaryotic host cells. In contrast, no such binding was observed with the full-length protein localized on the bacterial surface. As the C-terminal domain of intimin and the full-length protein differ in their binding activity, we suggest that the intimin-binding domain might be controlled by the N-terminal portion of the molecule to prevent unproductive interactions with molecules in the lumen of the gut.

PMID:
11310447
DOI:
10.1016/S1438-4221(01)80007-2
[Indexed for MEDLINE]

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