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Enterohaemorrhagic Escherichia coli requires the spectrin cytoskeleton for efficient attachment and pedestal formation on host cells.

TitleEnterohaemorrhagic Escherichia coli requires the spectrin cytoskeleton for efficient attachment and pedestal formation on host cells.
Publication TypeJournal Article
Year of Publication2012
AuthorsRuetz T, Lin AEn-Ju, Guttman JAndrew
JournalMicrob Pathog
Volume52
Issue3
Pagination149-56
Date Published2012 Mar
ISSN1096-1208
KeywordsBacterial Adhesion, Calmodulin-Binding Proteins, Enterohemorrhagic Escherichia coli, Gene Silencing, HeLa Cells, Host-Pathogen Interactions, Humans, Membrane Proteins, Microfilament Proteins, Nerve Tissue Proteins, Protein Binding, RNA, Small Interfering, Spectrin
Abstract

Recent work has demonstrated that the spectrin cytoskeleton is a host cell target, exploited during intestinal bacterial disease. Here we show that the highly virulent intestinal pathogen enterohaemorrhagic Escherichia coli (EHEC) is also reliant upon the spectrin cytoskeleton during key pathogenic events. Immunofluorescent microscopy demonstrated that the core components of the spectrin cytoskeleton (spectrin, adducin, and protein 4.1 [p4.1]) are recruited to sites of EHEC attachment and localized at pedestal structures along with the EHEC pedestal specific proteins IRSp53 and IRTKS. Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of EHEC to host cells, are involved in recruiting IRSp53 to the pedestal and are necessary for pedestal formation. These findings identify the spectrin cytoskeleton as a major host cell cytoskeletal network involved in critical EHEC pathogenic events.

DOI10.1016/j.micpath.2011.12.001
Alternate JournalMicrob. Pathog.
PubMed ID22197999
Grant List / / Canadian Institutes of Health Research / Canada
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