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Structure paper

TitleStructural mechanism of CRL4-instructed STAT2 degradation via a novel cytomegaloviral DCAF receptor.
Journal, issue, pagesEMBO J, Vol. 42, Issue 5, Page e112351, Year 2023
Publish dateMar 1, 2023
AuthorsVu Thuy Khanh Le-Trilling / Sofia Banchenko / Darius Paydar / Pia Madeleine Leipe / Lukas Binting / Simon Lauer / Andrea Graziadei / Robin Klingen / Christine Gotthold / Jörg Bürger / Thilo Bracht / Barbara Sitek / Robert Jan Lebbink / Anna Malyshkina / Thorsten Mielke / Juri Rappsilber / Christian Mt Spahn / Sebastian Voigt / Mirko Trilling / David Schwefel /
PubMed AbstractHuman cytomegalovirus (CMV) is a ubiquitously distributed pathogen whose rodent counterparts such as mouse and rat CMV serve as common infection models. Here, we conducted global proteome profiling ...Human cytomegalovirus (CMV) is a ubiquitously distributed pathogen whose rodent counterparts such as mouse and rat CMV serve as common infection models. Here, we conducted global proteome profiling of rat CMV-infected cells and uncovered a pronounced loss of the transcription factor STAT2, which is crucial for antiviral interferon signalling. Via deletion mutagenesis, we found that the viral protein E27 is required for CMV-induced STAT2 depletion. Cellular and in vitro analyses showed that E27 exploits host-cell Cullin4-RING ubiquitin ligase (CRL4) complexes to induce poly-ubiquitylation and proteasomal degradation of STAT2. Cryo-electron microscopy revealed how E27 mimics molecular surface properties of cellular CRL4 substrate receptors called DCAFs (DDB1- and Cullin4-associated factors), thereby displacing them from the catalytic core of CRL4. Moreover, structural analyses showed that E27 recruits STAT2 through a bipartite binding interface, which partially overlaps with the IRF9 binding site. Structure-based mutations in M27, the murine CMV homologue of E27, impair the interferon-suppressing capacity and virus replication in mouse models, supporting the conserved importance of DCAF mimicry for CMV immune evasion.
External linksEMBO J / PubMed:36762436 / PubMed Central
MethodsEM (single particle)
Resolution3.78 - 4.8 Å
Structure data

14802

7zn7

EMDB-14802, PDB-7zn7:
Cryo-EM structure of RCMV-E E27 bound to human DDB1 (deltaBPB) and rat STAT2 CCD
Method: EM (single particle) / Resolution: 3.78 Å

14812

7znn

EMDB-14812, PDB-7znn:
Cryo-EM structure of RCMV-E E27 bound to human DDB1 (deltaBPB) and full-length rat STAT2
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • murid betaherpesvirus 8
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsVIRUS / Interferon / ubiquitin-proteasome system / Cullin-RING ubiquitin ligases (CRL) / DDB1 / DCAFs / viral DCAF (vDCAF) / cytomegalovirus / STAT2 / IRF9

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