Department of Structural Biology and Chemistry
Vendredi 11 Oct. 2019 at 11:30
Pr. James Conway
University of Pittsburgh – USA
Probing the common architectures of bacteriophage T5 and herpesvirus by cryo-electron microscopy
The capsid protein fold of double-stranded DNA tailed bacteriophages was first detailed for phage HK97 and has since been observed in all members of this extraordinarily diverse and large family of viruses. For the past 15 years we have also been studying phage T5 whose capsid is larger than that of HK97 and offers insights into how the common fold of the major capsid protein can be directed to different icosahedral geometries. The tractability of these phage systems has been instrumental in understanding the architecture of the more directly biomedically important herpesvirus capsid, where the much larger major capsid protein also adopts the HK97 fold, and in particular in understanding the structure of the unique DNA-packaging vertex. Advances in cryo-electron microscopy have had a major impact on these studies and recent results on the capsid structures of both phage T5 and herpesvirus will be reviewed.