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Thus, the goal of this study was to identify the novel functions of the surface-associated<jats:italic>Tv<\/jats:italic>TIM in<jats:named-content content-type=\"genus-species\">T. vaginalis<\/jats:named-content>and to assess the effect of glucose as an environmental factor that regulates its expression and localization. Reverse transcription-PCR (RT-PCR) showed that the<jats:italic>tvtim<\/jats:italic>genes were differentially expressed in response to glucose concentration.<jats:italic>tvtim1<\/jats:italic>was overexpressed under glucose-restricted (GR) conditions, whereas<jats:italic>tvtim2<\/jats:italic>was overexpressed under glucose-rich, or high-glucose (HG), conditions. Western blot and indirect immunofluorescence assays also showed that glucose positively affected the amount and surface localization of<jats:italic>Tv<\/jats:italic>TIM in<jats:named-content content-type=\"genus-species\">T. vaginalis<\/jats:named-content>. Affinity ligand assays demonstrated that the recombinant<jats:italic>Tv<\/jats:italic>TIM1 and<jats:italic>Tv<\/jats:italic>TIM2 proteins bound to laminin (Lm) and fibronectin (Fn) but not to plasminogen. Moreover, higher levels of adherence to Lm and Fn were detected in parasites grown under HG conditions than in those grown under GR conditions. Furthermore, pretreatment of trichomonads with an anti-<jats:italic>Tv<\/jats:italic>TIMr polyclonal antibody or pretreatment of Lm- or Fn-coated wells with both recombinant proteins (<jats:italic>Tv<\/jats:italic>TIM1r and<jats:italic>Tv<\/jats:italic>TIM2r) specifically reduced the binding of live parasites to Lm and Fn in a concentration-dependent manner. Moreover,<jats:named-content content-type=\"genus-species\">T. vaginalis<\/jats:named-content>was exposed to different glucose concentrations during vaginal infection of women with trichomoniasis. Our data indicate that<jats:italic>Tv<\/jats:italic>TIM is a surface-associated protein under HG conditions that mediates specific binding to Lm and Fn as a novel virulence factor of<jats:named-content content-type=\"genus-species\">T. vaginalis<\/jats:named-content>.<\/jats:p>","DOI":"10.1128\/iai.00538-16","type":"journal-article","created":{"date-parts":[[2016,8,2]],"date-time":"2016-08-02T03:05:13Z","timestamp":1470107113000},"page":"2878-2894","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":43,"title":["The Glycolytic Enzyme Triosephosphate Isomerase of Trichomonas vaginalis Is a Surface-Associated Protein Induced by Glucose That Functions as a Laminin- and Fibronectin-Binding Protein"],"prefix":"10.1128","volume":"84","author":[{"given":"Jes\u00fas F. 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