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Published on: January 5, 2017
X-ray diffraction analysis of glycoprotein D from herpes simplex virus type 2
Zhujun Chen1, Guangwen Lu, Jianxun Qi
1College of Life Science, Anhui Agricultural University, Hefei 230036, China.
Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology
|January 21, 2012
Summary
Structural analysis of Herpes simplex virus type 2 (HSV-2) Glycoprotein D (gD) reveals its role in viral entry. This study elucidates the mechanism of HSV-2 gD-mediated receptor binding and host cell entry.
Area of Science:
- Structural biology
- Virology
- Molecular biology
Background:
- Herpes simplex virus type 2 (HSV-2) Glycoprotein D (gD) is crucial for viral entry into host cells.
- Understanding the gD-mediated mechanism is key to developing antiviral strategies.
Purpose of the Study:
- To elucidate the structural basis of HSV-2 gD-mediated receptor binding and viral entry.
- To provide high-resolution structural data of the HSV-2 gD ectodomain.
Main Methods:
- Expression of HSV-2 gD ectodomain (residues 1-285) using baculovirus system.
- Purification of soluble gD protein via affinity and size-exclusion chromatography.
- Crystallization of purified gD and X-ray diffraction analysis.
Main Results:
- HSV-2 gD ectodomain was successfully expressed, purified, and crystallized.
- Crystals diffracted to 1.8 angstroms resolution.
- Determined crystal space group as P21 with specific unit-cell parameters.
Conclusions:
- The study provides a high-resolution structure of HSV-2 gD.
- This structural information is vital for understanding HSV-2 entry mechanisms.
- The findings lay the groundwork for targeted antiviral drug design.
