Título:
Phospho-activated non-muscle myosin IIA heavy chain supports different mechanisms of virus uptake
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Autor:
Ansin Rando, Natalia Larisa
Guardado, Kathia
Ponce, Matías
García, María Paz
Ladra Hennig, Camila
Ferreiro Fernández, Irene
Moratorio, Gonzalo
Sarute, Nicolás
Guardado, Kathia
Ponce, Matías
García, María Paz
Ladra Hennig, Camila
Ferreiro Fernández, Irene
Moratorio, Gonzalo
Sarute, Nicolás
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Tipo de documento:
Artículo
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Palabras clave:
Virus entry
MYH9
Proviral factor
Tyrosine phosphorylation
MYH9
Proviral factor
Tyrosine phosphorylation
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Año de publicación:
2025
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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.
Descripción:
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Editorial:
American Society for Microbiology
EN:
Journal of Virology, 2025, 99(12): e00241-25.
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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.00241-25
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1098-5514
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Licencia Creative Commons Atribución (CC - By 4.0)
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| Ficheros | Descripción | Tamaño | Formato | ||
|---|---|---|---|---|---|
| 10.1128.jvi.00241-25.pdf | — | 3.99 MB | Adobe PDF |