Host cell invasion mediated by Trypanosoma cruzi surface molecule gp82 is associated with F-actin disassembly and is inhibited by enteroinvasive Escherichia coli

Show simple item record

dc.contributor.author Cortez, Mauro
dc.contributor.author Atayde, Vanessa
dc.contributor.author Yoshida, Nobuko
dc.date.accessioned 2016-01-24T12:41:09Z
dc.date.available 2016-01-24T12:41:09Z
dc.date.issued 2006-05-01
dc.identifier http://dx.doi.org/10.1016/j.micinf.2006.01.007
dc.identifier.citation Microbes and Infection. Amsterdam: Elsevier B.V., v. 8, n. 6, p. 1502-1512, 2006.
dc.identifier.issn 1286-4579
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/28887
dc.description.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. en
dc.format.extent 1502-1512
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Microbes and Infection
dc.rights Acesso restrito
dc.subject Trypanosoma cruzi en
dc.subject metacyclic trypomastigote en
dc.subject gp82 en
dc.subject host cell invasion en
dc.subject F-actin disassembly en
dc.title Host cell invasion mediated by Trypanosoma cruzi surface molecule gp82 is associated with F-actin disassembly and is inhibited by enteroinvasive Escherichia coli en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.identifier.doi 10.1016/j.micinf.2006.01.007
dc.description.source Web of Science
dc.identifier.wos WOS:000239253100010



File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search


Browse

Statistics

My Account