Florence Dô

TL;DR: It is shown that short transcripts produced in the presence of inhibitor in vitro do not contain a 5′ cap but, instead, are triphosphorylated, confirming the hypothesis that this class of inhibitors may block synthesis of RSV mRNAs by inhibiting guanylylation of viral transcripts.

TL;DR: The finding that an antiviral specifically targeting the NS3 protease activity inhibits HCV RNA replication further validates the NS2 enzyme as a prime target for drug discovery and supports the development of NS3rotease inhibitors as a novel therapeutic approach for HCV infection.

TL;DR: A specific inhibitor of RSV transcriptase with antiviral activity was identified through screening of this assay and could interfere at any step required for the production of complete RSV mRNAs, including transcription, polyadenylation and, potentially, co-transcriptional guanylylation.

TL;DR: The crystal structure of HIV-2 protease in complex with a reduced amide inhibitor [BI-LA-398; Phe-Val-Phe-psi (CH2NH)-Leu-Glu-Ile-amide] has been determined and the shapes of the S1 and S2 pockets in the presence of this inhibitor are essentially unperturbed by the amino acid differences between HIV-1 and HIV- 2 proteases.

TL;DR: In contrast to macrocyclic and covalent protease inhibitors, changes at V36, T54, F43, and Q80 did not confer resistance to BI 201335.