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TitleStructural studies of Chikungunya virus maturation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 52, Page 13703-13707, Year 2017
Publish dateDec 26, 2017
AuthorsMoh Lan Yap / Thomas Klose / Akane Urakami / S Saif Hasan / Wataru Akahata / Michael G Rossmann /
PubMed AbstractCleavage of the alphavirus precursor glycoprotein p62 into the E2 and E3 glycoproteins before assembly with the nucleocapsid is the key to producing fusion-competent mature spikes on alphaviruses. ...Cleavage of the alphavirus precursor glycoprotein p62 into the E2 and E3 glycoproteins before assembly with the nucleocapsid is the key to producing fusion-competent mature spikes on alphaviruses. Here we present a cryo-EM, 6.8-Å resolution structure of an "immature" Chikungunya virus in which the cleavage site has been mutated to inhibit proteolysis. The spikes in the immature virus have a larger radius and are less compact than in the mature virus. Furthermore, domains B on the E2 glycoproteins have less freedom of movement in the immature virus, keeping the fusion loops protected under domain B. In addition, the nucleocapsid of the immature virus is more compact than in the mature virus, protecting a conserved ribosome-binding site in the capsid protein from exposure. These differences suggest that the posttranslational processing of the spikes and nucleocapsid is necessary to produce infectious virus.
External linksProc Natl Acad Sci U S A / PubMed:29203665 / PubMed Central
MethodsEM (single particle)
Resolution6.8 Å
Structure data

8734

5vu2

EMDB-8734, PDB-5vu2:
Electron cryo-microscopy of "immature" Chikungunya VLP
Method: EM (single particle) / Resolution: 6.8 Å

Source
  • chikungunya virus strain senegal 37997
  • chikungunya virus (strain 37997)
KeywordsVIRUS LIKE PARTICLE / Chikungunya / virus / immature

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