Showing papers by "Cristina Romero-López published in 2013"
TL;DR: This review summarises the knowledge of the functional RNA domains of human RNA viruses and examines the achievements made in the design of antiviral compounds that interfere with their folding and therefore their function.
Abstract: RNA viruses show enormous capacity to evolve and adapt to new cellular and molecular contexts, a consequence of mutations arising from errors made by viral RNA-dependent RNA polymerase during replication. Sequence variation must occur, however, without compromising functions essential for the completion of the viral cycle. RNA viruses are safeguarded in this respect by their genome carrying conserved information that does not code only for proteins but also for the formation of structurally conserved RNA domains that directly perform these critical functions. Functional RNA domains can interact with other regions of the viral genome and/or proteins to direct viral translation, replication and encapsidation. They are therefore potential targets for novel therapeutic strategies. This review summarises our knowledge of the functional RNA domains of human RNA viruses and examines the achievements made in the design of antiviral compounds that interfere with their folding and therefore their function.
21 citations
TL;DR: The ability of two RNA aptamers, P‐58 and P‐78, to interfere with HCV replication by targeting the essential 5BSL3.2 domain within this CRE is reported, highlighting the potential of this CRE as a target for the development of anti‐HCV therapies and underscore the Potential of antiviral agents based on RNA aptamer molecules.
Abstract: The RNA genome of hepatitis C virus (HCV)contains multiple conserved structural RNA domains thatplay key roles in essential viral processes. A conservedstructural component within the 3¢ end of the region codingfor viral RNA-dependent RNA polymerase (NS5B) has beencharacterized as a functional cis-acting replication element(CRE). This study reports the ability of two RNA aptamers,P-58 and P-78, to interfere with HCV replication by tar-geting the essential 5BSL3.2 domain within this CRE.Structure-probing assays showed the binding of the apta-mers to the CRE results in a structural reorganization of theapical portion of the 5BSL3.2 stem-loop domain. Thisinterfered with the binding of the NS5B protein to the CREand induced a significant reduction in HCV replication(»50%) in an autonomous subgenomic HCV replicationsystem. These results highlight the potential of this CRE as atarget for the development of anti-HCV therapies andunderscore the potential of antiviral agents based on RNAaptamer molecules.Keywords: CRE, HCV genome, RNA aptamers, RNA structurefunction.
18 citations