J Struct Biol. 1992 Jul-Aug;109(1):61-9.

Structure of bluetongue virus particles by cryoelectron microscopy.

Source

Laboratoire de Biologie Structurale, CEA and CNRS URA 1333, Grenoble, France.

Abstract

The structure of the bluetongue virus (BTV) particle, determined by cryoelectron microscopy and image analysis, reveals a well-ordered outer shell which differs markedly from other known Reoviridae. The inner shell is known to have an icosahedral structure with 260 triangular spikes of VP7 trimers arranged on a T = 13,l lattice. The outer shell is seen to consist of 120 globular regions (possibly VP5), which sit neatly on each of the six-membered rings of VP7 trimers. "Sail"-shaped spikes located above 180 of the VP7 trimers form 60 triskelion-type motifs which cover all but 20 of the VP7 trimers. These spikes are possibly the hemagglutinating protein VP2 which contains a virus neutralization epitope. Thus, VP2 and VP5 together form a continuous layer around the inner shell except for holes on the 5-fold axis.

PMID:: 1337461; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

MeSH Terms

Substances

Viral Structural Proteins

Grant Support

A126879/PHS HHS/United States

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