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Title3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.
Journal, issue, pagesCell, Vol. 141, Issue 3, Page 472-482, Year 2010
Publish dateApr 30, 2010
AuthorsXing Zhang / Lei Jin / Qin Fang / Wong H Hui / Z Hong Zhou /
PubMed AbstractTo achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this ...To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. Here, using single-particle cryo-electron microscopy, we report a 3.3 A structure of the primed, infectious subvirion particle of aquareovirus. The density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. Our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that Lys84 and Glu76 may facilitate this autocleavage in a nucleophilic attack. We observe a myristoyl group, covalently linked to the N terminus of the penetration protein and embedded in a hydrophobic pocket. These results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger.
External linksCell / PubMed:20398923 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

5160

3iyl

EMDB-5160: Atomic CryoEM Structure of a Non-Enveloped Virus Reveals How its Membrane Protein is Primed for Cell Entry
PDB-3iyl: Atomic CryoEM Structure of a Nonenveloped Virus Suggests How Membrane Penetration Protein is Primed for Cell Entry
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MYR:
MYRISTIC ACID

Source
  • grass carp reovirus
KeywordsVIRUS / Non-enveloped virus / Membrane penetration protein / Autocleavage / Myristol Group / Icosahedral virus

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