An integrated proteomics approach identifies phosphorylation sites on viral and host proteins that regulate West Nile virus infection.

ABSTRACT: Upon infection, viruses alter the proteome, creating a hospitable environment for infection. Cells respond to limit viral replication, including through protein regulation by post-translational modifications. We use mass spectrometry to define proteome alterations during West Nile virus (WNV) infection. Our studies identify upregulation of HERPUD1, which restricts WNV replication through a mechanism independent of its role in endoplasmic reticulum (ER)-associated degradation (ERAD). We also identify modifications on viral proteins, including a WNV NS3 phosphorylation site that impacts viral replication. Finally, we reveal activation of two host kinases with antiviral activity. We identify phosphorylation at S108 of AMPKβ1, a non-catalytic subunit that regulates activity of the AMPK complex

SUBMITTER: Walter Z 

PROVIDER: S-EPMC12180539 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature