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Science 28 March 2008:
Vol. 319. no. 5871, pp. 1830 - 1834
DOI: 10.1126/science.1153263
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Reports

The Flavivirus Precursor Membrane-Envelope Protein Complex: Structure and Maturation

Long Li, Shee-Mei Lok, I-Mei Yu, Ying Zhang, Richard J. Kuhn, Jue Chen, Michael G. Rossmann*

Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo–electron microscopy density of immature virus at neutral pH. The pr peptide β-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host.

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

* To whom correspondence should be addressed. E-mail: mr{at}purdue.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation.
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Science 319, 1834-1837
   Abstract »    Full Text »    PDF »


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