Conformational changes in the adenovirus hexon subunit responsible for regulating cytoplasmic dynein recruitment.

ABSTRACT:

Unlabelled

Virus capsids provide genome protection from environmental challenges but are also poised to execute a program of compositional and conformational changes to facilitate virion entry and infection. The most abundant adenovirus serotype 5 (AdV5) capsid protein, hexon, directly recruits the motor protein cytoplasmic dynein following virion entry. Dynein recruitment is crucial for capsid transport to the nucleus and requires the transient exposure of AdV5 hexon to low pH, presumably mimicking passage through the endosomal compartment. These results suggest a pH-dependent capsid modification during early infection. The changes to hexon structure controlling this behavior have not been explored. We report that hexon remains trimeric at low pH but undergoes more subtle conforma

SUBMITTER: Scherer J 

PROVIDER: S-EPMC4300621 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature