The role of capsid maturation on adenovirus priming for sequential uncoating.

ABSTRACT: Adenovirus assembly concludes with proteolytic processing of several capsid and core proteins. Immature virions containing precursor proteins lack infectivity because they cannot properly uncoat, becoming trapped in early endosomes. Structural studies have shown that precursors increase the network of interactions maintaining virion integrity. Using different biophysical techniques to analyze capsid disruption in vitro, we show that immature virions are more stable than the mature ones under a variety of stress conditions and that maturation primes adenovirus for highly cooperative DNA release. Cryoelectron tomography reveals that under mildly acidic conditions mimicking the early endosome, mature virions release pentons and peripheral core contents. At higher stress levels, both mature an

SUBMITTER: Perez-Berna AJ 

PROVIDER: S-EPMC3438990 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature