Paul Digard

TL;DR: It is demonstrated to the field that cellular protein chaperones may be required for maintaining the correct folding and therefore functionality of specific proteins within the virus replication complex, and demonstrates that the function of cellular proteins can be targeted as potential therapeutics to disrupt virus replication.

TL;DR: These peptides represent a class of specific inhibitors of herpes simplex virus DNA polymerase that act by blocking accessory-subunit-dependent synthesis, and may form the basis for the synthesis of clinically effective drugs.

TL;DR: Overall, the authors see no role for the ESCRT pathway in influenza virus budding and the significance of the M1-VPS28 interaction remains to be determined, indicating that influenza release is VPS4-independent.

TL;DR: Polymerase complexes assembled on pre-annealed 5' and 3' terminal viral RNA sequences have distinct properties from those assembled by sequential loading of polymerase onto the 5'-end followed by the 3'-end, which suggests a mechanism by which the virus couples transcription initiation and termination during mRNA transcription.

TL;DR: The data support the hypothesis of a host nuclear factor that interacts with the viral polymerase and modulates its activity and have implications for how such factors might operate.