We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A C-terminal class I PDZ binding motif of EspI/NleA modulates the virulence of attaching and effacing Escherichia coli and Citrobacter rodentium.
- Authors
Sau Fung Lee; Kelly, Michelle; McAlister, Adrian; Luck, Shelley N.; Garcia, Erin L.; Hall, Randy A.; Robins-Browne, Roy M.; Frankel, Gad; Hartland, Elizabeth L.
- Abstract
Enteropathogenic Escherichia coli induces characteristic attaching–effacing (A/E) lesions on the intestinal mucosa during infection. The locus of enterocyte effacement is essential for A/E lesion formation and encodes a type III secretion system that translocates multiple effector proteins into the host cell. Following translocation, EspI/NleA localizes to the Golgi. Using the yeast two-hybrid system (Y2HS) and PSD-95/Disk-large/ZO-1 (PDZ)-domain protein array overlays, we identified 15 putative host-interacting partners of EspI. All but two of the target proteins contained PDZ domains. Examination of the EspI amino acid sequence revealed a C-terminal consensus class I PDZ binding motif. Deletion of the last 7 amino acids of EspI to generate EspIΔC7 abrogated the Y2HS interaction between EspI and 5 of the 6 putative host cell target proteins tested. Deletion of the EspI PDZ binding motif also resulted in delayed trafficking of EspI to the Golgi. Using a mouse model of infection, we showed that Citrobacter rodentium expressing truncated EspIΔC7 was attenuated when in competition with C. rodentium expressing full-length EspI. Overall, these results suggested that EspI may modulate the virulence of A/E pathogens by binding host PDZ-domain proteins.
- Subjects
ESCHERICHIA coli; ENTEROBACTERIACEAE; MICROBIAL virulence; INTESTINAL mucosa; GOLGI apparatus; PROTEINS; AMINO acid sequence; INFECTION; BACTERIA
- Publication
Cellular Microbiology, 2008, Vol 10, Issue 2, p499
- ISSN
1462-5814
- Publication type
Article
- DOI
10.1111/j.1462-5822.2007.01065.x