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TitleAssociation of the pr peptides with dengue virus at acidic pH blocks membrane fusion.
Journal, issue, pagesJ Virol, Vol. 83, Issue 23, Page 12101-12107, Year 2009
Publish dateSep 16, 2009
AuthorsI-M Yu / H A Holdaway / P R Chipman / R J Kuhn / M G Rossmann / J Chen /
PubMed AbstractFlavivirus assembles into an inert particle that requires proteolytic activation by furin to enable transmission to other hosts. We previously showed that immature virus undergoes a conformational ...Flavivirus assembles into an inert particle that requires proteolytic activation by furin to enable transmission to other hosts. We previously showed that immature virus undergoes a conformational change at low pH that renders it accessible to furin (I. M. Yu, W. Zhang, H. A. Holdaway, L. Li, V. A. Kostyuchenko, P. R. Chipman, R. J. Kuhn, M. G. Rossmann, and J. Chen, Science 319:1834-1837, 2008). Here we show, using cryoelectron microscopy, that the structure of immature dengue virus at pH 6.0 is essentially the same before and after the cleavage of prM. The structure shows that after cleavage, the proteolytic product pr remains associated with the virion at acidic pH, and that furin cleavage by itself does not induce any major conformational changes. We also show by liposome cofloatation experiments that pr retention prevents membrane insertion, suggesting that pr is present on the virion in the trans-Golgi network to protect the progeny virus from fusion within the host cell.
External linksJ Virol / PubMed:19759134 / PubMed Central
MethodsEM (single particle)
Resolution22.0 Å
Structure data

5117

3iya

EMDB-5117: Structure of furin-cleaved immature dengue virus at low pH
PDB-3iya: Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH
Method: EM (single particle) / Resolution: 22.0 Å

Source
  • dengue virus 2
KeywordsVIRUS / prM / E / Icosahedral virus

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