Rocío Coloma

TL;DR: Binding and functional studies with point mutants confirm that the identified site is essential for cap binding in vitro and cap-dependent transcription in vivo by the trimeric polymerase complex, and will allow efficient structure-based design of new anti-influenza compounds inhibiting viral transcription.

TL;DR: The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP provide insight into mechanisms for influenza genome replication and transcription, and the structure of native RNPs derived from virions is described.

TL;DR: The results provide the first model for a functional negative-stranded RNA virus ribonucleoprotein complex and will serve as a framework to generate a quasi-atomic model of the molecular machine responsible for viral RNA synthesis and to test new models for virus RNA replication and transcription.

TL;DR: This review focuses on the structure of this RNA-synthesis machines and the included RNA polymerase, and on the mechanisms by which they express their genetic information as mRNAs and generate progeny ribonucleoproteins that will become incorporated into new infectious virions.

TL;DR: The results of trans-complementation experiments showed that soluble polymerase complexes can synthesise progeny RNA in trans and become incorporated into progeny vRNPs, but only transcription in cis could be detected.