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- W1529976343 abstract "Enteropathogenic E. coli (EPEC) infection is a major cause of infantile diarrhea in the developing world. Using a type‐three secretion system, bacterial effector proteins are transferred to the host cell cytosol where they affect multiple physiological functions, ultimately leading to diarrheal disease. Disruption of intestinal epithelial cell tight junctions is a major consequence of EPEC infection and is mediated by multiple effector proteins, among them EspG1 and its homologue EspG2. EspG1/G2 contribute to loss of barrier function via an undefined mechanism that may be linked to their disruption of microtubule networks. Recently new investigations have identified additional roles for EspG. Sequestration of active ADP‐ribosylating factor (ARF) proteins and promotion of p21‐activated kinase (PAK) activity as well as inhibition of Golgi‐mediated protein secretion have all been linked to EspG. In this review, we examine the functions of EspG1/G2 and discuss potential mechanisms of EspG‐mediated tight junction disruption." @default.
- W1529976343 created "2016-06-24" @default.
- W1529976343 creator A5027111971 @default.
- W1529976343 creator A5078669671 @default.
- W1529976343 date "2012-06-25" @default.
- W1529976343 modified "2023-09-24" @default.
- W1529976343 title "Enteropathogenic E. coli effectors EspG1/G2 disrupt tight junctions: new roles and mechanisms" @default.
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- W1529976343 doi "https://doi.org/10.1111/j.1749-6632.2012.06563.x" @default.
- W1529976343 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4063556" @default.
- W1529976343 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22731728" @default.
- W1529976343 hasPublicationYear "2012" @default.
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