Molecular Mechanism of Adenovirus Late Protein L4-100K Chaperones the Trimerization of Hexon.

ABSTRACT: Assembly of the adenovirus capsid protein hexon depends on the assistance of the molecular chaperone L4-100K. However, the chaperone mechanisms remain unclear. In this study, we found that L4-100K was involved in the hexon translation process and could prevent hexon degradation by the proteasome in cotransfected human cells. Two nonadjacent domains, 84-133 and 656-697, at the N-terminal and C-terminal regions of human adenovirus type 5 L4-100K, respectively, were found to be crucial and cooperatively responsible for hexon trimer expression and assembly. These two chaperone-related domains were conserved in the sequence of L4-100K and in the function of hexon assembly across different adenovirus serotypes. Different degrees of cross-activity of hexon trimerization with different serotypes w

SUBMITTER: Zhu R 

PROVIDER: S-EPMC9888260 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature