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|Title:||Host cell invasion mediated by Trypanosoma cruzi surface molecule gp82 is associated with F-actin disassembly and is inhibited by enteroinvasive Escherichia coli|
Universidade Federal de São Paulo (UNIFESP)
host cell invasion
|Citation:||Microbes and Infection. Amsterdam: Elsevier B.V., v. 8, n. 6, p. 1502-1512, 2006.|
|Abstract:||The target cell F-actin disassembly, induced by a Ca2+-signaling Trypanosoma cruzi factor of unknown molecular identity, 2 has been reported to promote parasite invasion. We investigated whether the metacyclic trypomastigote stage-specific surface molecule gp82, a Ca2+-signal-inducing molecule implicated in host cell invasion, displayed the ability to induce actin cytoskeleton disruption, using a recombinant protein (J18) containing the full-length gp82 sequence fused to GST. J18, but not GST, induced F-actin disassembly in HeLa cells, significantly reducing the number as well as the length of stress fibers. the number of cells with typical stress fibers scored similar to 70% in untreated and GST-treated cells, as opposed to similar to 30% in J18-treated samples, which also showed decreased F-actin content. J18, but not GST, inhibited similar to 6-fold the HeLa cell entry of enteroinvasive Escherichia coli (EIEC), which depends on actin cytoskeleton. Not only were fewer cells infected with bacteria in the presence of J18, there were also fewer bacteria per cell. the inhibitory activity of J18 was Ca2+ dependent. in co-infection experiments, pre-incubation of HeLa cells with EIEC drastically reduced gp82-dependent internalization of T. cruzi metacyclic forms. All these data, plus the finding that gp82-mediated penetration of metacyclic forms was associated with disrupted HeLa cell cytoskeletal architecture, indicate that gp82 promotes parasite invasion by disassembling the cortical actin cytoskeleton. (c) 2006 Elsevier SAS. All rights reserved.|
|Appears in Collections:||Em verificação - Geral|
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