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

International Journal of Medical Microbiology : IJMM
C DeibelF Ebel

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.

Citations

May 5, 2001·Trends in Microbiology·G FrankelS Matthews
May 30, 2003·Proceedings of the National Academy of Sciences of the United States of America·Joshua R FischerJohn M Leong
Apr 22, 2003·Infection and Immunity·Nathalie S GonçalvesThomas T MacDonald
Nov 8, 2003·Journal of Clinical Microbiology·Vidiya RamachandranSteven P Djordjevic
Jun 27, 2006·BMC Veterinary Research·Tim StakenborgJohan Peeters
Jun 5, 2003·Cellular Microbiology·Jean-Philippe NougayrèdeMichael S Donnenberg
Nov 1, 2005·EcoSal Plus·Mark P Stevens, Timothy S Wallis

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