Trypanosoma cruzi nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase-1) biochemical characterization, immunolocalization and possible role in host cell adhesion

dc.contributor.authorMariotini-Moura, Christiane
dc.contributor.authorBastos, Matheus Silva e
dc.contributor.authorCastro, Felipe Freitas de
dc.contributor.authorTrindade, Mellina Lanna
dc.contributor.authorVasconcellos, Raphael de Souza
dc.contributor.authorNeves-do-Valle, Myrian Augusta Araújo
dc.contributor.authorMoreira, Bernardo Pereira
dc.contributor.authorSantos, Ramon de Freitas
dc.contributor.authorOliveira, Claudia Miranda de
dc.contributor.authorCunha, Luana Celina Seraphim
dc.contributor.authorSouto, Xênia Macedo
dc.contributor.authorBressan, Gustavo Costa
dc.contributor.authorSilva-Júnior, Abelardo
dc.contributor.authorBaqui, Munira Muhammad Abdel
dc.contributor.authorBahia, Maria Terezinha
dc.contributor.authorAlmeida, Márcia Rogéria de
dc.contributor.authorMeyer-Fernandes, José Roberto
dc.contributor.authorFietto, Juliana Lopes Rangel
dc.date.accessioned2017-11-06T15:49:59Z
dc.date.available2017-11-06T15:49:59Z
dc.date.issued2013-11-19
dc.description.abstractPrevious work has suggested that Trypanosoma cruzi diphosphohydrolase 1 (TcNTPDase-1) may be involved in the infection of mammalian cells and serve as a potential target for rational drug design. In this work, we produced recombinant TcNTPDase-1 and evaluated its nucleotidase activity, cellular localization and role in parasite adhesion to mammalian host cells. TcNTPDase-1 was able to utilize a broad range of triphosphate and diphosphate nucleosides. The enzyme's Km for ATP (0.096 mM) suggested a capability to influence the host's ATP-dependent purinergic signaling. The use of specific polyclonal antibodies allowed us to confirm the presence of TcNTPDase-1 at the surface of parasites by confocal and electron microscopy. In addition, electron microscopy revealed that TcNTPDase-1 was also found in the flagellum, flagellum insertion region, kinetoplast, nucleus and intracellular vesicles. The presence of this enzyme in the flagellum insertion region and vesicles suggests that it may have a role in nutrient acquisition, and the widespread distribution of TcNTPDase-1 within the parasite suggests that it may be involved in other biological process. Adhesion assays using anti-TcNTPDase-1 polyclonal antibodies as a blocker or purified recombinant TcNTPDase-1 as a competitor revealed that the enzyme has a role in parasite–host cell adhesion. These data open new frontiers to future studies on this specific parasite–host interaction and other unknown functions of TcNTPDase-1 related to its ubiquitous localization.en
dc.formatpdfpt-BR
dc.identifier.issn0001-706X
dc.identifier.urihttps://doi.org/10.1016/j.actatropica.2013.11.008
dc.identifier.urihttp://www.locus.ufv.br/handle/123456789/12755
dc.language.isoengpt-BR
dc.publisherActa Tropicapt-BR
dc.relation.ispartofseriesV. 130, p.140-147, February 2014pt-BR
dc.rightsOpen Accesspt-BR
dc.subjectRecombinant proteinpt-BR
dc.subjectTrypanosoma cruzipt-BR
dc.subjectNucleoside triphosphatept-BR
dc.subjectDiphosphohydrolasept-BR
dc.subjectImmunolocalizationpt-BR
dc.subjectAdhesionpt-BR
dc.titleTrypanosoma cruzi nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase-1) biochemical characterization, immunolocalization and possible role in host cell adhesionen
dc.typeArtigopt-BR

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