Cryo-EM Model of the Bullet-Shaped Vesicular Stomatitis Virus

被引:195
作者
Ge, Peng [1 ,2 ,3 ,4 ]
Tsao, Jun [5 ]
Schein, Stan [2 ,6 ]
Green, Todd J. [5 ]
Luo, Ming [5 ]
Zhou, Z. Hong [1 ,2 ,3 ,4 ]
机构
[1] Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, Calif NanoSyst Inst, Los Angeles, CA 90095 USA
[3] Baylor Coll Med, Struct Computat Biol & Mol Biophys Program, Houston, TX 77030 USA
[4] Univ Texas Med Sch Houston, Dept Pathol & Lab Med, Houston, TX 77030 USA
[5] Univ Alabama, Dept Microbiol, Birmingham, AL 35294 USA
[6] Univ Calif Los Angeles, Dept Psychol, Los Angeles, CA 90095 USA
关键词
MATRIX PROTEIN; CRYSTAL-STRUCTURE; GLYCOPROTEIN-G; DOMAIN; NUCLEOPROTEIN; COMPLEX; CELLS; FORM;
D O I
10.1126/science.1181766
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
Vesicular stomatitis virus (VSV) is a bullet-shaped rhabdovirus and a model system of negative-strand RNA viruses. Through direct visualization by means of cryo-electron microscopy, we show that each virion contains two nested, left-handed helices: an outer helix of matrix protein M and an inner helix of nucleoprotein N and RNA. M has a hub domain with four contact sites that link to neighboring M and N subunits, providing rigidity by clamping adjacent turns of the nucleocapsid. Side-by-side interactions between neighboring N subunits are critical for the nucleocapsid to form a bullet shape, and structure-based mutagenesis results support this description. Together, our data suggest a mechanism of VSV assembly in which the nucleocapsid spirals from the tip to become the helical trunk, both subsequently framed and rigidified by the M layer.
引用
收藏
页码:689 / 693
页数:5
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