Affiliation:
1. Division of Infectious Diseases, Department of Medicine and Graduate Program in Molecular and Cell Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201
Abstract
ABSTRACT
Adherence of enteropathogenic
Escherichia coli
(EPEC) to epithelial cells is dependent on a type IV fimbria, termed the bundle-forming pilus (BFP). A cluster of 14 genes is required for expression of BFP. The eighth gene in the cluster,
bfpF
, encodes a putative nucleotide-binding protein which resembles the PilT protein of
Pseudomonas aeruginosa
. It has been proposed that PilT is required for the retraction of the
P. aeruginosa
pilus, which results in twitching motility. To test the role of BfpF in BFP function and EPEC pathogenesis, two different mutations were constructed in the
bfpF
gene, one in the cloned gene cluster in a laboratory
E. coli
strain and one in wild-type EPEC. Neither mutation affected prepilin synthesis, leader sequence processing, or pilus biogenesis. However, both mutations resulted in increased localized adherence. In addition, the EPEC
bfpF
mutant displayed increased aggregation. The EPEC
bfpF
mutant was not deficient in attaching and effacing activity or invasion capacity. These results suggest that BfpF decreases aggregation and adherence by EPEC but that subsequent steps in EPEC pathogenesis do not require this protein.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
66 articles.
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