X-ray diffraction analysis of glycoprotein D from herpes simplex virus type 2.
- Author:
Zhujun CHEN
1
;
Guangwen LU
;
Jianxun QI
;
Xiang XU
;
Na ZHANG
;
Jinghua YAN
;
Rongfu WANG
Author Information
1. College of Life Science, Anhui Agricultural University, Hefei 230036, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Baculoviridae;
Crystallization;
Crystallography, X-Ray;
Herpesvirus 2, Human;
chemistry;
Insecta;
genetics;
metabolism;
Recombinant Proteins;
biosynthesis;
chemistry;
genetics;
Viral Fusion Proteins;
biosynthesis;
chemistry;
genetics
- From:
Chinese Journal of Biotechnology
2011;27(10):1499-1506
- CountryChina
- Language:English
-
Abstract:
Glycoprotein D (gD) of Herpes simplex virus type 2 (HSV-2) is a key factor mediating the entry of HSV-2 into host cells. In order to explain the mechanism underlying the gD-mediated receptor-binding and viral entry, we performed a structural study on HSV-2 gD. The ectodomain of the gD protein encompassing residues 1 to 285 was expressed by baculovirus-infected insect cells as a secreted soluble protein with a C-terminal hexa-his tag. The protein was then purified by affinity and size-exclusion chromatography. The purified protein was successfully crystallized using the hanging-drop vapor-diffusion at 18 degrees C in a condition consisting of 0.1 mol/L Hepes pH 7.2, 5% (V/V) 2-methyl-2,4-pentanediol (MPD) and 10% PEG 10 000. The crystals diffracted to 1.8 angstroms resolution and belonged to space group P21, with unit-cell parameters alpha = 63.6, b = 55.4, c = 65.3 angstroms, beta = 96.3 degrees.
