Enterohaemorrhagic

The structural properties of EspB, a virulence factor of theEscherichia coli O157 type III secretion system, were characterized. Far-UV and near-UV CD spectra, recorded between pH 1.0 and pH 7.0, show that the protein assumesa-helical structures and that some tyrosine tertiary contacts may exist. All tyrosine side-chains are exposed to water, as determined by acryl-amide fluorescence quenching spectroscopy.

13p awards 05-04-2013 27 4   Download

EspB is a multifunctional protein associated with the type III secretion system of enterohaemorrhagic Escherichia coli, and interacts with various biomolecules includinga-catenin in the host cell. The binding of EspB to a-catenin is thought be involved in actin reorganization during bacterial infection, although the precise mechanism of this phenomenon is still unclear.

8p vinaphone15 28-02-2013 29 4   Download

A variety of microbes manipulate the cytoskeleton of mammalian cells to promote their internalization, motility and⁄or spread. Among such bacte-ria, enteropathogenic Escherichia coliand enterohemorrhagic Escherichia coliare closely related pathogens that adhere to human intestinal cells and reorganize the underlying actin cytoskeleton into ‘pedestals’.

13p mobifone23 21-01-2013 40 5   Download