Artículos de revistas
Subversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes
Registro en:
Mucosal Immunology. Nature Publishing Group, v. 2, n. 1, n. 43, n. 53, 2009.
1933-0219
WOS:000261760500006
10.1038/mi.2008.63
Autor
Zaia, AA
Sappington, KJ
Nisapakultorn, K
Chazin, WJ
Dietrich, EA
Ross, KF
Herzberg, MC
Institución
Resumen
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Expressed 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. 2 1 43 53 NIH [RO1DE11831, P30DE09737, RO1GM62112] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) The Royal Thai government Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) NIH [RO1DE11831, P30DE09737, RO1GM62112] FAPESP [99/10079-4]