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Título: | A G-quadruplex-binding macrodomain within the >SARS-unique domain> is essential for the activity of the SARS-coronavirus replication-transcription complex |
Autor: | Kusov, Yuri; Tan, Jinzhi; Álvarez, Enrique ; Enjuanes Sánchez, Luis CSIC ORCID ; Hilgenfeld, Rolf | Palabras clave: | SARS-CoV replicon SARS-unique domain Macrodomain X-domain Reverse genetics G-quadruplex MERS-CoV |
Fecha de publicación: | oct-2015 | Editor: | Elsevier BV | Citación: | Virology 484: 313-322 (2015) | Resumen: | The multi-domain non-structural protein 3 of SARS-coronavirus is a component of the viral replication/transcription complex (RTC). Among other domains, it contains three sequentially arranged macrodomains: the X domain and subdomains SUD-N as well as SUD-M within the >SARS-unique domain>. The X domain was proposed to be an ADP-ribose-1>-phosphatase or a poly(ADP-ribose)-binding protein, whereas SUD-NM binds oligo(G)-nucleotides capable of forming G-quadruplexes. Here, we describe the application of a reverse genetic approach to assess the importance of these macrodomains for the activity of the SARS-CoV RTC. To this end, Renilla luciferase-encoding SARS-CoV replicons with selectively deleted macrodomains were constructed and their ability to modulate the RTC activity was examined. While the SUD-N and the X domains were found to be dispensable, the SUD-M domain was crucial for viral genome replication/transcription. Moreover, alanine replacement of charged amino-acid residues of the SUD-M domain, which are likely involved in G-quadruplex-binding, caused abrogation of RTC activity. | Versión del editor: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4567502/ | URI: | http://hdl.handle.net/10261/204265 | DOI: | 10.1016/j.virol.2015.06.016 | Identificadores: | doi: 10.1016/j.virol.2015.06.016 issn: 1096-0341 |
Aparece en las colecciones: | (CBM) Artículos (CNB) Artículos (PTI Salud Global) Colección Especial COVID-19 |
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