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TitleMolecular architecture of coronavirus double-membrane vesicle pore complex.
Journal, issue, pagesNature, Vol. 633, Issue 8028, Page 224-231, Year 2024
Publish dateAug 14, 2024
AuthorsYixin Huang / Tongyun Wang / Lijie Zhong / Wenxin Zhang / Yu Zhang / Xiulian Yu / Shuofeng Yuan / Tao Ni /
PubMed AbstractCoronaviruses remodel the intracellular host membranes during replication, forming double-membrane vesicles (DMVs) to accommodate viral RNA synthesis and modifications. SARS-CoV-2 non-structural ...Coronaviruses remodel the intracellular host membranes during replication, forming double-membrane vesicles (DMVs) to accommodate viral RNA synthesis and modifications. SARS-CoV-2 non-structural protein 3 (nsp3) and nsp4 are the minimal viral components required to induce DMV formation and to form a double-membrane-spanning pore, essential for the transport of newly synthesized viral RNAs. The mechanism of DMV pore complex formation remains unknown. Here we describe the molecular architecture of the SARS-CoV-2 nsp3-nsp4 pore complex, as resolved by cryogenic electron tomography and subtomogram averaging in isolated DMVs. The structures uncover an unexpected stoichiometry and topology of the nsp3-nsp4 pore complex comprising 12 copies each of nsp3 and nsp4, organized in 4 concentric stacking hexamer rings, mimicking a miniature nuclear pore complex. The transmembrane domains are interdigitated to create a high local curvature at the double-membrane junction, coupling double-membrane reorganization with pore formation. The ectodomains form extensive contacts in a pseudo-12-fold symmetry, belting the pore complex from the intermembrane space. A central positively charged ring of arginine residues coordinates the putative RNA translocation, essential for virus replication. Our work establishes a framework for understanding DMV pore formation and RNA translocation, providing a structural basis for the development of new antiviral strategies to combat coronavirus infection.
External linksNature / PubMed:39143215 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution4.2 - 6.2 Å
Structure data

39107

8yax

EMDB-39107, PDB-8yax:
SARS-CoV-2 DMV nsp3-4 pore complex (full-pore)
Method: EM (subtomogram averaging) / Resolution: 4.9 Å

39109

8yb5

EMDB-39109, PDB-8yb5:
SARS-CoV-2 DMV nsp3-4 pore complex (consensus-pore, C6 symmetry)
Method: EM (subtomogram averaging) / Resolution: 4.2 Å

EMDB-39111: SARS-CoV-2 DMV nsp3-4 pore complex (extended-pore)
Method: EM (subtomogram averaging) / Resolution: 4.7 Å

39112

8yb7

EMDB-39112, PDB-8yb7:
SARS-CoV-2 DMV nsp3-4 pore complex (consensus-pore, C3 symmetry)
Method: EM (subtomogram averaging) / Resolution: 4.6 Å

EMDB-39113: SARS-CoV-2 DMV nsp3-4 pore complex (mini-pore)
Method: EM (subtomogram averaging) / Resolution: 4.6 Å

EMDB-39159: SARS-CoV-2 DMV nsp3-4 pore complex (full-length-pore)
Method: EM (subtomogram averaging) / Resolution: 6.2 Å

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / Double membrane vesicle / pore complex / nsp3 / nsp4 / RNA transport

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