Affiliation:
1. Department of Microbiology, University of Iowa College of Medicine, Iowa City, Iowa 52242
Abstract
ABSTRACT
Pathogenic
Salmonella
species initiate infection of a host by inducing their own uptake into intestinal epithelial cells. An invasive phenotype is conferred to this pathogen by a number of proteins that are components of a type III secretion system. During the invasion process, the bacteria utilize this secretion system to release proteins that enter the host cell and apparently interact with unknown host cell components that induce alterations in the actin cytoskeleton. To investigate the role of secreted proteins as direct modulators of invasion, we have evaluated the ability of
Salmonella typhimurium
to enter mammalian cells that express portions of the
Salmonella
invasion proteins SipB and SipC. Plasma membrane localization of SipB and SipC was achieved by fusing carboxyl- and amino-terminal portions of each invasion protein to the intracellular carboxyl-terminal tail of a membrane-bound eukaryotic receptor. Expression of receptor chimeras possessing the carboxyl terminus of SipB or the amino terminus of SipC blocked
Salmonella
invasion, whereas expression of their chimeric counterparts had no effect on invasion. The effect on invasion was specific for
Salmonella
since the perturbation of uptake was not extended to other invasive bacterial species. These results suggest that
Salmonella
invasion can be competitively inhibited by preventing the intracellular effects of SipB or SipC. In addition, these experiments provide a model for examining interactions between bacterial invasion proteins and their host cell targets.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
14 articles.
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