Abstract
Enteropathogenic Escherichia coli (EPEC) destroys intestinal microvilli and suppresses phagocytosis by injecting effectors into infected cells through a type III secretion system (TTSS). EspB, a component of the TTSS, is also injected into the cytoplasm of host cells. However, the physiological functions of EspB within the host cell cytoplasm remain unclear. We show that EspB binds to myosins, which are a superfamily of proteins that interact with actin filaments and mediate essential cellular processes, including microvillus formation and phagocytosis. EspB inhibits the interaction of myosins with actin, and an EspB mutant that lacks the myosin-binding region maintained its TTSS function but could not induce microvillus effacing or suppress phagocytosis. Moreover, the myosin-binding region of EspB is essential for Citrobacter rodentium, an EPEC-related murine pathogen, to efficiently infect mice. These results suggest that EspB inhibits myosin functions and thereby facilitates efficient infection by EPEC.
Original language | English (US) |
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Pages (from-to) | 383-392 |
Number of pages | 10 |
Journal | Cell Host and Microbe |
Volume | 2 |
Issue number | 6 |
DOIs | |
State | Published - Dec 13 2007 |
Keywords
- CELLBIO
- MICROBIO
ASJC Scopus subject areas
- Parasitology
- Microbiology
- Virology