Tethered release of the pseudorabies virus deubiquitinase from the capsid promotes enzymatic activity.

ABSTRACT: Herpesviruses carry an assortment of proteins in the interstitial space between the capsid and membrane envelope, collectively referred to as the tegument. Upon virion fusion with a cell, envelope integrity is disrupted, and many tegument constituents disperse into the cytosol to carry out individual effector functions, while others direct transport of the capsid to the nucleus. To gain insight into the tegument dynamics that occur with disruption of envelope integrity, we used a combination of single-particle fluorescence and biochemical approaches that leveraged the previously established use of n-ethylmaleimide to inhibit virion dynamics. We document that the large tegument protein (pUL36), which is stably bound to the capsid surface at its C-terminus, is also conditionally bound to the

SUBMITTER: Antinone SE 

PROVIDER: S-EPMC11784296 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature