Subversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes

dc.creatorZaia, AA
dc.creatorSappington, KJ
dc.creatorNisapakultorn, K
dc.creatorChazin, WJ
dc.creatorDietrich, EA
dc.creatorRoss, KF
dc.creatorHerzberg, MC
dc.date2009
dc.dateJAN
dc.date2014-11-14T11:42:03Z
dc.date2015-11-26T17:14:37Z
dc.date2014-11-14T11:42:03Z
dc.date2015-11-26T17:14:37Z
dc.date.accessioned2018-03-29T00:02:55Z
dc.date.available2018-03-29T00:02:55Z
dc.identifierMucosal Immunology. Nature Publishing Group, v. 2, n. 1, n. 43, n. 53, 2009.
dc.identifier1933-0219
dc.identifierWOS:000261760500006
dc.identifier10.1038/mi.2008.63
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74698
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/74698
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74698
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1281853
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionExpressed by squamous mucosal keratinocytes, calprotectin is a complex of two EF-hand calcium-binding proteins of the S100 subfamily (S100A8 and S100A9) with significant antimicrobial activity. Calprotectin-expressing cells resist invasion by Porphyromonas gingivalis, Listeria monocytogenes, and Salmonella enterica serovar Typhimurium ( S. typhimurium). To understand the interactions between calprotectin and invasive bacteria, we studied the distribution of calprotectin in the cytoplasm of TR146 epithelial cells. In response to L. monocytogenes, calprotectin mobilized from a diffuse cytoplasmic distribution to a filamentous pattern and colocalized with the microtubule network. Listeria more frequently invaded cells with mobilized calprotectin. Calprotectin mobilization was listeriolysin O-dependent and required calcium ( extracellular and intracellular) and an intact microtubule network. In the presence of preformed microtubules in vitro, the anti-Listeria activity of calprotectin was abrogated. To facilitate intraepithelial survival, therefore, Listeria mobilizes calprotectin to colocalize with cytoplasmic microtubules, subverting anti-Listeria activity and autonomous cellular immunity.
dc.description2
dc.description1
dc.description43
dc.description53
dc.descriptionNIH [RO1DE11831, P30DE09737, RO1GM62112]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionThe Royal Thai government
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionNIH [RO1DE11831, P30DE09737, RO1GM62112]
dc.descriptionFAPESP [99/10079-4]
dc.languageen
dc.publisherNature Publishing Group
dc.publisherNew York
dc.publisherEUA
dc.relationMucosal Immunology
dc.relationMucosal Immunol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectCalcium-binding Proteins
dc.subjectGene-expression
dc.subjectPhosphoinositide 3-kinase
dc.subjectSalmonella-typhimurium
dc.subjectHuman Neutrophils
dc.subjectInnate Immunity
dc.subjectSmall-intestine
dc.subjectS100
dc.subjectMrp14
dc.subjectMigration
dc.titleSubversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes
dc.typeArtículos de revistas


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