Modulators of the Hop-HSP90 Protein-Protein Interaction Disrupt KSHV Lytic Replication.

ABSTRACT: The central role of the chaperome in maintaining cellular proteostasis has seen numerous viral families evolve to parasitically exploit host chaperones in their life cycle. The HSP90 chaperone protein and its cochaperone Hop have both individually been shown to be essential factors for Kaposi sarcoma-associated herpesvirus (KSHV) lytic replication. Given the fundamental regulatory role that protein-protein interactions (PPIs) play in cellular biology, we reasoned that disrupting the Hop-HSP90 PPI may provide a new host-based target for inhibiting KSHV lytic replication. This study expands upon a previous report of non-natural peptides, which were found to disrupt the association between the Hop_TPR2A domain and its interacting HSP90_CTD. Here, in addition to providing i

SUBMITTER: Okpara MO 

PROVIDER: S-EPMC11555673 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature