Autoproteolytic activity derived from the infectious bursal disease virus capsid protein.

ABSTRACT: Viral capsids are envisioned as vehicles to deliver the viral genome to the host cell. They are nonetheless dynamic protective shells, as they participate in numerous processes of the virus cycle such as assembly, genome packaging, binding to receptors, and uncoating among others. In so doing, they undergo large scale conformational changes. Capsid proteins with essential enzymatic activities are being described more frequently. Here we show that the precursor (pVP2) of the capsid protein VP2 of the infectious bursal disease virus (IBDV), an avian double-stranded RNA virus, has autoproteolytic activity. The pVP2 C-terminal region is first processed by the viral protease VP4. VP2 Asp-431, lying in a flexible loop preceding the C-terminal most alpha-helix, is responsible for the endopeptidas

SUBMITTER: Irigoyen N 

PROVIDER: S-EPMC2658100 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature