Format

Send to

Choose Destination
See comment in PubMed Commons below
J Virol. 2009 Dec;83(23):12101-7. doi: 10.1128/JVI.01637-09. Epub 2009 Sep 16.

Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion.

Author information

1
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.

Abstract

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.

PMID:
19759134
PMCID:
PMC2786737
DOI:
10.1128/JVI.01637-09
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center