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. 2012 Sep 1;68(Pt 9):1094-7.
doi: 10.1107/S1744309112030151. Epub 2012 Aug 31.

Crystallization and preliminary X-ray analysis of Chandipura virus glycoprotein G

Eduard Baquero  1 , Linda Buonocore, John K Rose, Stéphane Bressanelli, Yves Gaudin, Aurélie A Albertini
Affiliations

Crystallization and preliminary X-ray analysis of Chandipura virus glycoprotein G

Eduard Baquero et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Fusion in members of the Rhabdoviridae virus family is mediated by the G glycoprotein. At low pH, the G glycoprotein catalyzes fusion between viral and endosomal membranes by undergoing a major conformational change from a pre-fusion trimer to a post-fusion trimer. The structure of the G glycoprotein from vesicular stomatitis virus (VSV G), the prototype of Vesiculovirus, has recently been solved in its trimeric pre-fusion and post-fusion conformations; however, little is known about the structural details of the transition. In this work, a soluble form of the ectodomain of Chandipura virus G glycoprotein (CHAV G(th)) was purified using limited proteolysis of purified virus; this soluble ectodomain was also crystallized. This protein shares 41% amino-acid identity with VSV G and thus its structure could provide further clues about the structural transition of rhabdoviral glycoproteins induced by low pH. Crystals of CHAV G(th) obtained at pH 7.5 diffracted X-rays to 3.1 Å resolution. These crystals belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 150.3, b = 228.2, c = 78.8 Å. Preliminary analysis of the data based on the space group and the self-rotation function indicated that there was no trimeric association of the protomers. This unusual oligomeric status could result from the presence of fusion intermediates in the crystal.

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Figures

Figure 1
Figure 1
SDS–PAGE analysis of CHAV Gth purification. Lane M, molecular-mass marker (labelled in kDa); lane V, recombinant VSV encoding CHAV G; lane D, virus digested with thermolysin; lane Gth, CHAV Gth after purification. Viral proteins are also indicated (L, large protein, G, glycoprotein; N, nucleoprotein; P, phospho­protein; M, matrix protein).
Figure 2
Figure 2
Crystal of Gth obtained using 14% PEG 3350, 0.3 M Na2SO4, 0.1 M HEPES pH 7.6.
Figure 3
Figure 3
X-ray diffraction image from Gth crystals obtained at intermediate pH. The black circle indicates the diffraction limit at 3.0 Å resolution.
Figure 4
Figure 4
Self-rotation functions of a Gth data set obtained from crystals grown at pH 7.5: (a) χ = 180.0°, (b) χ = 120.0°.
See this image and copyright information in PMC

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