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TitleVirome-wide ubiquitin ligase discovery reveals diverse mechanisms of immune evasion.
Journal, issue, pagesScience, Year 2026
Publish dateJul 9, 2026
AuthorsCaleb R Glassman / Kheewoong Baek / Gaopeng Hou / Qiru Zeng / Christopher Nardone / Kate B Juergens / Eric Fujimura / Colin N O'Leary / Mamie Z Li / Joao A Paulo / Eric S Fischer / Siyuan Ding / J Wade Harper / Stephen J Elledge /
PubMed AbstractViruses are intracellular parasites that reprogram the host proteome to promote replication and evade immune recognition. We applied a virome-wide library of ~10,000 open reading frames to discover ...Viruses are intracellular parasites that reprogram the host proteome to promote replication and evade immune recognition. We applied a virome-wide library of ~10,000 open reading frames to discover viral ubiquitin ligases, mapping their mechanisms of degradation and host substrates using targeted CRISPR screens and proteomics. These viral effectors could be classified as canonical ligases that mimic host E3s, hijackers that redirect host E3s, and non-canonical ligases that rewire Cullin-RING ligase machinery. These diverse strategies of virus-mediated degradation converged on immune-related substrates, including JAK1 and CUL1, underscoring immune evasion as a major driver of viral ubiquitin ligase evolution. Our findings elucidate viral strategies for exploiting the ubiquitin-proteasome system with potential for therapeutic targeting.
External linksScience / PubMed:42424437
MethodsEM (single particle)
Resolution3.3 Å
Structure data

72190

9q3e

EMDB-72190, PDB-9q3e:
Cryo-EM structure of RotavirusA NSP1-ELOB-ELOC-CUL3
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • rotavirus a
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / Viral effector / E3 ligase / NSP1 / CUL3

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