dc.creatorMartins, Thaís Viana Fialho
dc.creatorZeraik, Ana Eliza
dc.creatorAlves, Natália Oliveira
dc.creatorOliveira, Leandro Licursi de
dc.creatorMendes, Tiago Antônio de Oliveira
dc.creatorDeMarco, Ricardo
dc.creatorMarques-da-Silva, Eduardo de Almeida
dc.date2018-04-19T17:22:29Z
dc.date2018-04-19T17:22:29Z
dc.date2018-02-14
dc.date.accessioned2023-09-27T21:55:22Z
dc.date.available2023-09-27T21:55:22Z
dc.identifier11779322
dc.identifierhttp://dx.doi.org/10.1177/1177932218763363
dc.identifierhttp://www.locus.ufv.br/handle/123456789/18880
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8968122
dc.descriptionLeishmania infantum chagasi is an intracellular protozoan parasite responsible for visceral leishmaniasis, a fatal disease in humans. Heparin-binding proteins (HBPs) are proteins that bind to carbohydrates present in glycoproteins or glycolipids. Evidence suggests that HBPs present on Leishmania surface participate in the adhesion and invasion of parasites to tissues of both invertebrate and vertebrate hosts. In this study, we identified the product with an HSP90 (heat shock protein 90) domain encoded by lipophosphoglycan (LPG3) gene as a L infantum chagasi HBP (HBPLc). Structural analysis using the LPG3 recombinant protein suggests that it is organized as a tetramer. Binding analysis confirms that it is capable of binding heparin with micromolar affinity. Inhibition of adenosine triphosphatase activity in the presence of heparin, molecular modeling, and in silico docking analysis suggests that heparin-binding site superimposes with the adenosine triphosphate–binding site. Together, these results show new properties of LPG3 and suggest an important role in leishmaniasis.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherBioinformatics and Biology Insights
dc.relationv. 12, p. 01–12, march 2018
dc.rightsOpen Access
dc.subjectHeparin
dc.subjectATPase
dc.subjectLPG3
dc.titleLipophosphoglycan 3 From Leishmania infantum chagasi Binds Heparin With Micromolar Affinity
dc.typeArtigo


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