Structure and function relationship of the autotransport and proteolytic activity of EspP from Shiga toxin-producing Escherichia coli.

ABSTRACT:

Background

The serine protease autotransporter EspP is a proposed virulence factor of Shiga toxin-producing Escherichia coli (STEC). We recently distinguished four EspP subtypes (EspPalpha, EspPbeta, EspPgamma, and EspPdelta), which display large differences in transport and proteolytic activities and differ widely concerning their distribution within the STEC population. The mechanisms underlying these functional variations in EspP subtypes are, however, unknown.

Methodology/principal findings

The structural basis of proteolytic and autotransport activity was investigated using transposon-based linker scanning mutagenesis, site-directed mutagenesis and structure-function analysis derived from homology modelling of the EspP passenger domain. Transposon mutagenesis of the pas

SUBMITTER: Brockmeyer J 

PROVIDER: S-EPMC2700255 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature