Immune evasion strategy involving propionylation by the KSHV interferon regulatory factor 1 (vIRF1).
Ontology highlight
ABSTRACT: Post-translational modifications (PTMs) are essential for host antiviral immune response and viral immune evasion. Among a set of novel acylations, lysine propionylation (Kpr) has been detected in both histone and non-histone proteins. However, whether protein propionylation occurs in any viral proteins and whether such modifications regulate viral immune evasion remain elusive. Here, we show that Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded viral interferon regulatory factor 1 (vIRF1) can be propionylated in lysine residues, which is required for effective inhibition of IFN-β production and antiviral signaling. Mechanistically, vIRF1 promotes its own propionylation by blocking SIRT6's interaction with ubiquitin-specific peptidase 10 (USP10) leading to its degradation via a ubiqu
SUBMITTER: Shi J
PROVIDER: S-EPMC10112802 | biostudies-literature | 2023 Apr
REPOSITORIES: biostudies-literature
ACCESS DATA