Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/24011
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | HIV- 1 Protease Inhibits Cap- and Poly(A)-Dependent Translation upon elF4GI and PABP Cleavage |
Autor: | Castelló, Alfredo; Franco, David; Moral-López, Pablo; Berlanga, Juan José; Álvarez, Enrique ; Wimmer, Eckard; Carrasco Llamas, Luis CSIC ORCID | Palabras clave: | HIV- 1 PR elF4GI PABP |
Fecha de publicación: | 24-nov-2009 | Editor: | Public Library of Science | Citación: | PLoS ONE 4(11): e7997. | Resumen: | A number of viral proteases are able to cleave translation initiation factors leading to the inhibition of cellular translation. This is the case of human immunodeficiency virus type 1 protease (HIV-1 PR), which hydrolyzes eIF4GI and poly(A)-binding protein (PABP). Here, the effect of HIV-1 PR on cellular and viral protein synthesis has been examined using cell-free systems. HIV-1 PR strongly hampers translation of pre-existing capped luc mRNAs, particularly when these mRNAs contain a poly(A) tail. In fact, HIV-1 PR efficiently blocks cap- and poly(A)-dependent translation initiation in HeLa extracts. Addition of exogenous PABP to HIV-1 PR treated extracts partially restores the translation of polyadenylated luc mRNAs, suggesting that PABP cleavage is directly involved in the inhibition of poly(A)-dependent translation. In contrast to these data, PABP cleavage induced by HIV-1 PR has little impact on the translation of polyadenylated encephalomyocarditis virus internal ribosome entry site (IRES)-containing mRNAs. In this case, the loss of poly(A)-dependent translation is compensated by the IRES transactivation provided by eIF4G cleavage. Finally, translation of capped and polyadenylated HIV-1 genomic mRNA takes place in HeLa extracts when eIF4GI and PABP have been cleaved by HIV-1 PR. Together these results suggest that proteolytic cleavage of eIF4GI and PABP by HIV-1 PR blocks cap- and poly(A)-dependent initiation of translation, leading to the inhibition of cellular protein synthesis. However, HIV-1 genomic mRNA can be translated under these conditions, giving rise to the production of Gag polyprotein. | Versión del editor: | http://dx.doi.org/10.1371/journal.pone.0007997 | URI: | http://hdl.handle.net/10261/24011 | DOI: | 10.1371/journal.pone.0007997 | ISSN: | 1932-6203 |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
ACastello_PlosOne_7997.pdf | 744,87 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
42
checked on 30-mar-2024
SCOPUSTM
Citations
51
checked on 18-abr-2024
WEB OF SCIENCETM
Citations
53
checked on 24-feb-2024
Page view(s)
499
checked on 24-abr-2024
Download(s)
331
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.