Source:http://linkedlifedata.com/resource/pubmed/id/19732055
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-1-11
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pubmed:abstractText |
Type III secretion system-mediated injection of a cocktail of bacterial proteins drives actin rearrangements, frequently adopting the shape of prominent protuberances of ruffling membrane, and culminating in host cell invasion of Gram-negative pathogens like Salmonella typhimurium. Different Salmonella effectors are able to bind actin and activate Rho-family GTPases, which have previously been implicated in mediating actin-dependent Salmonella entry by interacting with N-WASP or WAVE-complex, well-established activators of the actin nucleation machine Arp2/3-complex. Using genetic deletion and RNA interference studies, we show here that neither individual nor collective removal of these Arp2/3- complex activators affected host cell invasion as efficiently as Arp2/3-complex knock-down, although the latter was also not essential. However, interference with WAVE-complex function abrogated Salmonella-induced membrane ruffling without significantly affecting entry efficiency, actin or Arp2/3-complex accumulation. In addition, scanning electron microscopy images captured entry events in the absence of prominent membrane ruffles. Finally, localization and RNA interference studies indicated a relevant function in Salmonella entry for the novel Arp2/3-complex regulator WASH. These data establish for the first time that Salmonella invasion is separable from bacteria-induced membrane ruffling, and uncover an additional Arp2/3-complex activator as well as an Arp2/3-complex-independent actin assembly activity that contribute to Salmonella invasion.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actin-Related Protein 2-3 Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/C9orf156 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/WASL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1462-5822
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pubmed:author |
pubmed-author:BosseTanjaT,
pubmed-author:BumannDirkD,
pubmed-author:DeriveryEmmanuelE,
pubmed-author:EhingerJuliaJ,
pubmed-author:GautreauAlexisA,
pubmed-author:HänischJanJ,
pubmed-author:HardtWolf-DietrichWD,
pubmed-author:LadweinMarkusM,
pubmed-author:MisselwitzBenjaminB,
pubmed-author:RohdeManfredM,
pubmed-author:RottnerKlemensK,
pubmed-author:SteffenAnikaA,
pubmed-author:StradalTheresia E BTE
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pubmed:issnType |
Electronic
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
84-98
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pubmed:meshHeading |
pubmed-meshheading:19732055-Actin-Related Protein 2-3 Complex,
pubmed-meshheading:19732055-Bacterial Proteins,
pubmed-meshheading:19732055-Blotting, Western,
pubmed-meshheading:19732055-Cell Line,
pubmed-meshheading:19732055-Cell Membrane,
pubmed-meshheading:19732055-Fibroblasts,
pubmed-meshheading:19732055-Humans,
pubmed-meshheading:19732055-Microscopy, Electron, Scanning,
pubmed-meshheading:19732055-Microscopy, Fluorescence,
pubmed-meshheading:19732055-Proteins,
pubmed-meshheading:19732055-RNA Interference,
pubmed-meshheading:19732055-Salmonella typhimurium,
pubmed-meshheading:19732055-Wiskott-Aldrich Syndrome Protein, Neuronal
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pubmed:year |
2010
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pubmed:articleTitle |
Molecular dissection of Salmonella-induced membrane ruffling versus invasion.
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pubmed:affiliation |
Helmholtz Centre for Infection Research, Braunschweig, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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