The TRiC chaperonin controls reovirus replication through outer-capsid folding.

ABSTRACT: Viruses are molecular machines sustained through a life cycle that requires replication within host cells. Throughout the infectious cycle, viral and cellular components interact to advance the multistep process required to produce progeny virions. Despite progress made in understanding the virus-host protein interactome, much remains to be discovered about the cellular factors that function during infection, especially those operating at terminal steps in replication. In an RNA interference screen, we identified the eukaryotic chaperonin T-complex protein-1 (TCP-1) ring complex (TRiC; also called CCT for chaperonin containing TCP-1) as a cellular factor required for late events in the replication of mammalian reovirus. We discovered that TRiC functions in reovirus replication through a me

SUBMITTER: Knowlton JJ 

PROVIDER: S-EPMC5874176 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature