The Potyviridae P1a leader protease contributes to host range specificity
[EN] The P1a protein of the ipomovirus Cucumber vein yellowing virus is one of the self-cleavage serine proteases present in Potyviridae family members. P1a is located at the N-terminal end of the viral polyprotein, and is closely related to potyviral P1 protease. For its proteolytic activity, P1a r...
| Autores: | , , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2015 |
| País: | España |
| Institución: | Universitat Politècnica de València (UPV) |
| Repositorio: | RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
| Idioma: | inglés |
| OAI Identifier: | oai:riunet.upv.es:10251/162361 |
| Acceso en línea: | https://riunet.upv.es/handle/10251/162361 |
| Access Level: | acceso abierto |
| Palabra clave: | Potyviriadae P1a Host range P1 proteases RNA silencing suppression Plum pox virus Cucumber vein yellowing virus |
| Sumario: | [EN] The P1a protein of the ipomovirus Cucumber vein yellowing virus is one of the self-cleavage serine proteases present in Potyviridae family members. P1a is located at the N-terminal end of the viral polyprotein, and is closely related to potyviral P1 protease. For its proteolytic activity, P1a requires a still unknown host factor; this might be linked to involvement in host specificity. Here we built a series of constructs and chimeric viruses to help elucidate the role of P1a cleavage in host range definition. We demonstrate that host-dependent separation of P1a from the remainder of the polyprotein is essential for suppressing RNA silencing defenses and for efficient viral infection. Intergenus replacement of leader proteases could broaden host range definition, as shown by the local infection capacity of viral chimeras. These findings support the role of viral proteases as important determinants in host adaptation. |
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