Por favor, use este identificador para citar o enlazar este ítem: https://hdl.handle.net/20.500.12008/54522
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dc.contributor.author Autor Ansin Rando, Natalia Larisa-
dc.contributor.author Autor Guardado, Kathia-
dc.contributor.author Autor Ponce, Matías-
dc.contributor.author Autor García, María Paz-
dc.contributor.author Autor Ladra Hennig, Camila-
dc.contributor.author Autor Ferreiro Fernández, Irene-
dc.contributor.author Autor Moratorio, Gonzalo-
dc.contributor.author Autor Sarute, Nicolás-
dc.contributor.filiacion Filiación Ansin Rando Natalia Larisa, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Guardado Kathia, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Ponce Matías, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación García María Paz, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Ladra Hennig Camila, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Ferreiro Fernández Irene, Universidad de la República (Uruguay). Facultad de Ciencias. Centro de Investigaciones Nucleares.-
dc.contributor.filiacion Filiación Moratorio Gonzalo, Universidad de la República (Uruguay). Facultad de Ciencias. Centro de Investigaciones Nucleares.-
dc.contributor.filiacion Filiación Sarute Nicolás, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.-
dc.date.accessioned Fecha ingreso 2026-04-21T17:53:55Z-
dc.date.available Fecha disponible 2026-04-21T17:53:55Z-
dc.date.issued Año de publicación 2025-
dc.description.abstract Resumen Limiting virus entry is crucial to prevent infection, since this step of the virus life cycle is a major determinant of cellular tropism, host range, and pathogenesis. We recently showed that the transmembrane protein signal regulatory protein alpha (SIRPA), a negative regulator of F-actin-dependent phagocytosis, limits endocytosis of enveloped RNA viruses from unrelated families. Mechanistically, surface engagement of SIRPA recruits the SH2 domain-containing protein tyrosine phosphatases (SHP)-1 and -2, initiating a signaling cascade that dephosphorylates different pro-phagocytic proteins, including the heavy chain (MYH9) of the molecular motor non-muscle myosin IIA (NM-IIA), to ultimately suppress phagocytosis. Here, we analyzed whether MYH9 would enhance viral infection, as it does phagocytic engulfment, and how its activity in infection is regulated. We found that MYH9 expression increases the infection of viruses exploiting different endocytic pathways/mechanisms to enter cells, including flavivirus, arenavirus, rhabdovirus, and togavirus, in human and mouse cells. Furthermore, we demonstrated that MYH9 is actively translocated to the plasma membrane upon viral infection to support post-binding steps of entry, and that phosphorylation of two key tyrosine residues in its head and tail domains is essential for its function in viral infection. By using small molecule inhibitors and MYH9 knockdown cells, we suggest that members of the Src family kinases may phosphorylate/activate MYH9 to support virus entry.es
dc.format.extent Extensión 18 hes
dc.format.mimetype Formato application/pdfes
dc.identifier.citation Citación Ansin Rando, N, Guardado, K, Ponce, M [y otros autores]. "Phospho-activated non-muscle myosin IIA heavy chain supports different mechanisms of virus uptake". Journal of Virology. [en línea] 2025, 99(12): e00241-25. 18 h. DOI: 10.1128/jvi.00241-25es
dc.identifier.doi DOI 10.1128/jvi.00241-25-
dc.identifier.issn ISSN 1098-5514-
dc.identifier.uri URI https://hdl.handle.net/20.500.12008/54522-
dc.language.iso Idioma enes
dc.publisher Editorial American Society for Microbiologyes
dc.relation.ispartof EN Journal of Virology, 2025, 99(12): e00241-25.es
dc.rights Derechos Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)es
dc.rights.licence Licencia Licencia Creative Commons Atribución (CC - By 4.0)es
dc.subject Palabras clave Virus entryes
dc.subject Palabras clave MYH9es
dc.subject Palabras clave Proviral factores
dc.subject Palabras clave Tyrosine phosphorylationes
dc.title Título Phospho-activated non-muscle myosin IIA heavy chain supports different mechanisms of virus uptakees
dc.type Tipo de documento Artículoes
FicherosDescripciónTamañoFormato
10.1128.jvi.00241-25.pdf — 3.99 MB Adobe PDF