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Role of a novel uropod-like cell membrane protrusion in the pathogenesis of the parasite Trichomonas vaginalis.
Blasco Pedreros, Manuela; Salas, Nehuen; Dos Santos Melo, Tuanne; Miranda-Magalhães, Abigail; Almeida-Lima, Thainá; Pereira-Neves, Antonio; de Miguel, Natalia.
Afiliación
  • Blasco Pedreros M; Laboratorio de Parásitos Anaerobios, Instituto Tecnológico Chascomús (INTECH), CONICET-UNSAM, Buenos Aires CP 7130, Argentina.
  • Salas N; Escuela de Bio y Nanotecnologías (UNSAM), Chascomús CP 1650, Argentina.
  • Dos Santos Melo T; Laboratorio de Parásitos Anaerobios, Instituto Tecnológico Chascomús (INTECH), CONICET-UNSAM, Buenos Aires CP 7130, Argentina.
  • Miranda-Magalhães A; Escuela de Bio y Nanotecnologías (UNSAM), Chascomús CP 1650, Argentina.
  • Almeida-Lima T; Departamento de Microbiologia, Instituto Aggeu Magalhães, Fiocruz, Recife, Pernambuco CEP 50740-465, Brazil.
  • Pereira-Neves A; Departamento de Microbiologia, Instituto Aggeu Magalhães, Fiocruz, Recife, Pernambuco CEP 50740-465, Brazil.
  • de Miguel N; Departamento de Microbiologia, Instituto Aggeu Magalhães, Fiocruz, Recife, Pernambuco CEP 50740-465, Brazil.
J Cell Sci ; 137(20)2024 Oct 15.
Article en En | MEDLINE | ID: mdl-39129707
ABSTRACT
Trichomonas vaginalis causes trichomoniasis, the most common non-viral sexually transmitted disease worldwide. As an extracellular parasite, adhesion to host cells is essential for the development of infection. During attachment, the parasite changes its tear ovoid shape to a flat ameboid form, expanding the contact surface and migrating through tissues. Here, we have identified a novel structure formed at the posterior pole of adherent parasite strains, resembling the previously described uropod, which appears to play a pivotal role as an anchor during the attachment process. Moreover, our research demonstrates that the overexpression of the tetraspanin T. vaginalis TSP5 protein (TvTSP5), which is localized on the cell surface of the parasite, notably enhances the formation of this posterior anchor structure in adherent strains. Finally, we demonstrate that parasites that overexpress TvTSP5 possess an increased ability to adhere to host cells, enhanced aggregation and reduced migration on agar plates. Overall, these findings unveil novel proteins and structures involved in the intricate mechanisms of T. vaginalis interactions with host cells.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trichomonas vaginalis / Proteínas Protozoarias Límite: Animals / Humans Idioma: En Revista: J Cell Sci Año: 2024 Tipo del documento: Article País de afiliación: Argentina Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trichomonas vaginalis / Proteínas Protozoarias Límite: Animals / Humans Idioma: En Revista: J Cell Sci Año: 2024 Tipo del documento: Article País de afiliación: Argentina Pais de publicación: Reino Unido