Mapping and Engineering Functional Domains of the Assembly-Activating Protein of Adeno-associated Viruses.

ABSTRACT: Adeno-associated viruses (AAVs) encode a unique assembly-activating protein (AAP) within their genomes that is essential for capsid assembly. Studies to date have focused on establishing the role of AAP as a chaperone that mediates the stability, nucleolar transport, and assembly of AAV capsid proteins. Here, we map structure-function correlates of AAP using secondary structure analysis, followed by deletion and substitutional mutagenesis of specific domains, namely, the N-terminal hydrophobic region (HR), conserved core (CC), proline-rich region (PRR), threonine/serine-rich region (T/S), and basic region (BR). First, we establish that the centrally located PRR and T/S are flexible linker domains that can either be deleted completely or replaced by heterologous functional domains that enab

SUBMITTER: Tse LV 

PROVIDER: S-EPMC6026743 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature