The flavivirus precursor membrane-envelope protein complex: Structure and maturation

被引：390

作者：

Li, Long ^{[1
]}

Lok, Shee-Mei ^{[1
]}

Yu, I-Mei ^{[1
]}

Zhang, Ying ^{[1
]}

Kuhn, Richard J. ^{[1
]}

Chen, Jue ^{[1
]}

Rossmann, Michael G. ^{[1
]}

机构：

[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

来源：

SCIENCE | 2008年 / 319卷 / 5871期

关键词：

D O I：

10.1126/science.1153263

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 beta-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.

引用

页码：1830 / 1834

页数：5

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