Phosphatidylinositol-specific phospholipase C (PI-PLC) cleavage of GPI-anchored surface molecules of Trypanosoma cruzi triggers in vitro morphological reorganization of trypomastigotes

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dc.contributor.authorMortara, R. A.
dc.contributor.authorMinelli, LMS
dc.contributor.authorVandekerchove, F.
dc.contributor.authorNussenzweig, V
dc.contributor.authorRamalho-Pinto, F. J.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionNYU Med Ctr
dc.date.accessioned2016-01-24T12:31:16Z
dc.date.available2016-01-24T12:31:16Z
dc.date.issued2001-01-01
dc.description.abstractTrypanosoma cruzi trypomastigotes treated with phosphatidylinositol-specific phospholipase C (PI-PLC) in vitro are rapidly induced to differentiate into round forms. Using confocal microscopy, we were able to show that trypomastigotes treated with PI-PLC initiate the process of flagellum remodeling by 30 sec after contact with the enzyme and amastigote-like forms are detected as early as 10 min after PI-PLC treatment. Scanning and transmission electron microscopy indicate that trypomastigotes undergo a previously undescribed process of flagellum circularization and internalization. Analysis of the flagellar complex with monoclonal antibody 4D9 shows heterogeneous labeling among the parasites, suggesting a remodeling of these molecules. After PI-PLC treatment, parasites rapidly lose the surface marker Ssp-3 and 24 h post-treatment they begin to exhibit a circular nucleus and a rod-shaped kinetoplast. By flow cytometry analysis and confocal microscopy, the Ssp-4 amastigote-specific epitope can be detected on the parasite surface. This indicates that thr release of trypomastigote GPI-anchored molecules by exogenous PI-PLC in vitro can trigger morphological changes.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Ctr Microscopia Eletron, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Fac Med Ribeirao Preto, Dept Paasitol Microbiol & Imunol, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationNYU Med Ctr, Dept Pathol, Div Immunol, New York, NY 10016 USA
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Ctr Microscopia Eletron, BR-04023062 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent27-37
dc.identifierhttp://dx.doi.org/10.1111/j.1550-7408.2001.tb00413.x
dc.identifier.citationJournal of Eukaryotic Microbiology. Lawrence: Soc Protozoologists, v. 48, n. 1, p. 27-37, 2001.
dc.identifier.doi10.1111/j.1550-7408.2001.tb00413.x
dc.identifier.issn1066-5234
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26460
dc.identifier.wosWOS:000167286400007
dc.language.isoeng
dc.publisherSoc Protozoologists
dc.relation.ispartofJournal of Eukaryotic Microbiology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectconfocal microscopyen
dc.subjectflagellumen
dc.subjectGPIen
dc.subjectPI-PLCen
dc.subjectprotozoaen
dc.subjectTrypanosoma cruzien
dc.subjecttrypomastigoteen
dc.titlePhosphatidylinositol-specific phospholipase C (PI-PLC) cleavage of GPI-anchored surface molecules of Trypanosoma cruzi triggers in vitro morphological reorganization of trypomastigotesen
dc.typeinfo:eu-repo/semantics/article
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