Lookup NU author(s): Dr Paul Dean
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Central to the pathogenesis of many bacterial pathogens is the ability to deliver effector proteins directly into the cells of their eukaryotic host. EspF is one of many effector proteins exclusive to the attaching and effacing pathogen family that includes enteropathogenic (EPEC) and enterohemorrhagic E. coli (EHEC). Work in recent years has revealed EspF to be one of the most multi-functional effector proteins known, with defined roles in several host cellular processes including disruption of the epithelial barrier, anti-phagocytosis, microvilli effacement, host membrane remodelling, modulation of the cytoskeleton, targeting and disruption of the nucleolus, intermediate filament disruption, cell invasion, mitochondrial dysfunction, apoptosis and the inhibition of several important epithelial transporters. Surprisingly, despite this high number of functions, EspF is a relatively small effector protein and recent work has begun to decipher the molecular events that underlie its multi-functionality. This review focuses on the activities of EspF within the host cell and discusses recent findings and molecular insights relating to the virulence functions of this fascinating bacterial effector.
Author(s): Holmes A, Muhlen S, Roe AJ, Dean P
Publication type: Article
Journal: Infection and Immunity
Print publication date: 02/08/2010
ISSN (print): 0019-9567
ISSN (electronic): 1098-5522
Publisher: American Society for Microbiology
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