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

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 hel...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2010-02, Vol.327 (5966), p.689-693
Main Authors: Ge, Peng, Tsao, Jun, Schein, Stan, Green, Todd J, Luo, Ming, Zhou, Z. Hong
Format: Article
Language:English
Subjects:
Amino acids
Biological and medical sciences
Bullets
Cryoelectron Microscopy
Crystal structure
Crystallography, X-Ray
Fundamental and applied biological sciences. Psychology
Image Processing, Computer-Assisted
Lipid Bilayers
Microbiology
Microscopy
Models, Molecular
Morphology, structure, chemical composition, physicochemical properties
Mutagenesis
Nucleocapsid
Nucleocapsid Proteins - chemistry
Nucleocapsid Proteins - genetics
Nucleocapsid Proteins - ultrastructure
Nucleoproteins
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits - chemistry
Proteins
Rhabdovirus
Ribonucleic acid
RNA
RNA, Viral - chemistry
RNA, Viral - ultrastructure
Tree trunks
Vesicular stomatitis virus
Vesiculovirus - chemistry
Vesiculovirus - physiology
Vesiculovirus - ultrastructure
Viral Matrix Proteins - chemistry
Viral Matrix Proteins - ultrastructure
Virion - chemistry
Virion - ultrastructure
Virions
Virology
Virus Assembly
Viruses
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1181766