Dengue structure differs at the temperatures of its human and mosquito hosts

被引:173
作者
Zhang, Xinzheng [1 ]
Sheng, Ju [1 ]
Plevka, Pavel [1 ]
Kuhn, Richard J. [1 ]
Diamond, Michael S. [2 ,3 ,4 ]
Rossmann, Michael G. [1 ]
机构
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[2] Washington Univ, Sch Med, Dept Med, St Louis, MO 63110 USA
[3] Washington Univ, Sch Med, Dept Mol Microbiol, St Louis, MO 63110 USA
[4] Washington Univ, Sch Med, Dept Pathol & Immunol, St Louis, MO 63110 USA
基金
美国国家卫生研究院;
关键词
host temperature; irreversible and conformational change; temperature dependence; cryo-EM; WEST-NILE-VIRUS; ENVELOPE PROTEIN; DOMAIN-III; GLYCOPROTEIN; COMPLEX; VACCINE; BINDING; ORGANIZATION; RECOGNITION; RECOMBINANT;
D O I
10.1073/pnas.1304300110
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
We report on a conformational transition of dengue virus when changing the temperature from that present in its mosquito vectors to that of its human host. Using cryoelectron microscopy, we show that although the virus has a smooth surface, a diameter of similar to 500 angstrom, and little exposed membrane at room temperature, the virions have a bumpy appearance with a diameter of similar to 550 angstrom and some exposed membrane at 37 degrees C. The bumpy structure at 37 degrees C was found to be similar to the previously predicted structure of an intermediate between the smooth mature and fusogenic forms. As humans have a body temperature of 37 degrees C, the bumpy form of the virus would be the form present in humans. Thus, optimal dengue virus vaccines should induce antibodies that preferentially recognize epitopes exposed on the bumpy form of the virus.
引用
收藏
页码:6795 / 6799
页数:5
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