dc.creatorPuente Rivera, Jonathan
dc.creatorVillaplando, José Luis
dc.creatorVillalobos Osnaya, Alma
dc.creatorVázquez Carrillo, Laura Isabel
dc.creatorLeón Ávila, Gloria
dc.creatorPonce Regalado, María Dolores
dc.creatorLópez Camarillo, César
dc.creatorElizalde Contreras, José Miguel
dc.creatorRuiz May, Eliel
dc.creatorArroyo, Rossana Arroyo
dc.creatorÁlvarez Sánchez, María Elizbeth
dc.date2022-06-20T18:25:09Z
dc.date2022-06-20T18:25:09Z
dc.date2017-10
dc.date.accessioned2023-07-21T21:45:23Z
dc.date.available2023-07-21T21:45:23Z
dc.identifierJonathan Puente-Rivera, José Luis Villalpando, Alma Villalobos-Osnaya, Laura Isabel Vázquez-Carrillo, Gloria León-Ávila, María Dolores Ponce-Regalado, César López-Camarillo, Jose Miguel Elizalde-Contreras, Eliel Ruiz-May, Rossana Arroyo, María Elizbeth Alvarez-Sánchez, The 50kDa metalloproteinase TvMP50 is a zinc-mediated Trichomonas vaginalis virulence factor, Molecular and Biochemical Parasitology, Volume 217, 2017, Pages 32-41, ISSN 0166-6851, https://doi.org/10.1016/j.molbiopara.2017.09.001.
dc.identifier0166-6851
dc.identifierhttps://doi.org/10.1016/j.molbiopara.2017.09.001
dc.identifierhttp://repositorio.cualtos.udg.mx:8080/jspui/handle/123456789/1346
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7752820
dc.descriptionArtículo
dc.descriptionTrichomonas vaginalis is a protozoan parasite that can adapt to the trichomonicidal Zn2+ concentrations of the male urogenital tract microenvironment. This adaptation is mediated by molecular mechanisms, including proteinase expression, that are regulated by cations such as Zn2+. Herein, we characterized the previously identified 50kDa metalloproteinase aminopeptidase P (M24 family) member TvMP50 as a new Zn2+-mediated parasite virulence factor. Quantitative RT-PCR and indirect immunofluorescence assays corroborated the positive regulation of both mp50 gene expression and native TvMP50 protein overexpression in the cytoplasm and secretion products of parasites grown in the presence of Zn2+. Furthermore, this active metalloproteinase was characterized as a new virulence factor by assaying cytotoxicity toward prostatic DU145 cell monolayers as well as the inhibition of parasite and secreted soluble protein proteolytic activity in the 50kDa proteolytic region by the specific metalloproteinase inhibitor 1,10-phenanthroline and the chelating agents EDTA and EGTA. Parasite and secreted soluble protein cytotoxicity toward DU145 cells were reduced by treatment with an α-rTvMP50 polyclonal antibody. Our results show that the metalloproteinase TvMP50 is a new virulence factor modulated by Zn2+, which is present during male trichomoniasis, possibly explaining T. vaginalis survival even within the adverse conditions of the male urogenital microenvironment.
dc.languageen
dc.publisherElsevier - Science Direct
dc.relationMolecular and Biochemical Parasitology;Volume 217, October 2017, Pages 32-41
dc.subjecttrichomonas vaginalis
dc.subjectZn2+
dc.subjectTvMP50
dc.subjectcytotoxicity
dc.subjectDU145 cells
dc.subjectvirulence factor
dc.titleThe 50kDa metalloproteinase TvMP50 is a zinc-mediated Trichomonas vaginalis virulence factor
dc.typeArticle


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