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Infect. Immun., Jun 1997, 2211-2217, Vol 65, No. 6
LC Lai, LA Wainwright, KD Stone and MS Donnenberg
Enteropathogenic Escherichia coli strains are able to signal host cells,
cause dramatic cytoskeletal rearrangements, and adhere intimately to the
cell surface in a process known as the attaching and effacing effect. A
pathogenicity island of 35 kb known as the locus of enterocyte effacement
(LEE) is necessary and sufficient for this effect. The LEE encodes an outer
membrane adhesin called intimin, a type III secretion apparatus, and the
EspA and EspB secreted proteins. The DNA sequence of the region between
espA and espB revealed a new gene, espD. The product of espD was
demonstrated by using a T7 expression system. We constructed a nonpolar
mutation in espD and found that the mutant is incapable of the signal
transduction events that lead to activation of the putative intimin
receptor in host cells and that the mutant fails to induce the attaching
and effacing effect. These phenotypes were restored to the mutant by
complementation with a plasmid containing the cloned espD locus. We
demonstrated by immunoblotting and microsequencing that the EspD protein is
secreted via the type III apparatus. Thus, we describe a novel locus
encoding a secreted protein that is required for attaching and effacing
activity.
Copyright © 1997, American Society for Microbiology
A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells
Division of Infectious Diseases, University of Maryland School of Medicine, Baltimore 21201, USA.
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