Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors

doi:10.1088/1674-1056/27/1/018704

中国物理B ›› 2018, Vol. 27 ›› Issue (1): 18704-018704.doi: 10.1088/1674-1056/27/1/018704

所属专题： TOPICAL REVIEW — Soft matter and biological physics

• SPECIAL TOPIC—Non-equilibrium phenomena in soft matters • 上一篇下一篇

Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors

Zhi-wei Yang(杨志伟), Dong-xiao Hao(郝东晓), Yi-zhuo Che(车一卓), Jia-hui Yang(杨嘉辉), Lei Zhang(张磊), Sheng-li Zhang(张胜利)

1 Department of Applied Physics, School of Science, Xi'an Jiaotong University, Xi'an 710049, China;
2 Department of Applied Chemistry, School of Science, Xi'an Jiaotong University, Xi'an 710049, China;
3 School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710049, China

收稿日期:2017-09-01 修回日期:2017-10-24 出版日期:2018-01-05 发布日期:2018-01-05
通讯作者: Lei Zhang, Sheng-li Zhang E-mail:zhangleio@mail.xjtu.edu.cn;zhangsl@mail.xjtu.edu.cn
基金资助:
Project supported by the National Natural Science Foundation of China (Grant Nos. 11374237 and 11504287), Fundamental Research Funds for the Central Universities, China, China Postdoctoral Science Foundation (Grant No. 2017M613147), and Shaanxi Province Postdoctoral Science Foundation, China.

Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors

Zhi-wei Yang(杨志伟)^1,2,3, Dong-xiao Hao(郝东晓)¹, Yi-zhuo Che(车一卓)¹, Jia-hui Yang(杨嘉辉)¹, Lei Zhang(张磊)¹, Sheng-li Zhang(张胜利)¹

1 Department of Applied Physics, School of Science, Xi'an Jiaotong University, Xi'an 710049, China;
2 Department of Applied Chemistry, School of Science, Xi'an Jiaotong University, Xi'an 710049, China;
3 School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710049, China

Received:2017-09-01 Revised:2017-10-24 Online:2018-01-05 Published:2018-01-05
Contact: Lei Zhang, Sheng-li Zhang E-mail:zhangleio@mail.xjtu.edu.cn;zhangsl@mail.xjtu.edu.cn
Supported by:
Project supported by the National Natural Science Foundation of China (Grant Nos. 11374237 and 11504287), Fundamental Research Funds for the Central Universities, China, China Postdoctoral Science Foundation (Grant No. 2017M613147), and Shaanxi Province Postdoctoral Science Foundation, China.

摘要/Abstract

摘要：

Neuraminidase (NA), a major surface glycoprotein of influenza virus with well-defined active sites, is an ideal platform for the development of antiviral drugs. However, a growing number of NA mutations have drug resistance to today's inhibitors. Numerous efforts are made to explore the resistance mechanisms through understanding the structural changes in mutated NA proteins and the associated different binding profiles of inhibitors, via x-ray, nuclear magnetic resonance, electron microscopy, and molecular dynamics methods. This review presents the architectural features of mutated NA proteins, as well as the respective inhibitor sensitivities arising from these spatial differences. Finally, we summarize the resistance mechanisms of today's neuraminidase inhibitors and the outlook for the development of novel inhibitors.

关键词: mutation, active sites, neuraminidase, inhibitor sensitivity

Abstract:

Key words: mutation, active sites, neuraminidase, inhibitor sensitivity

中图分类号: (Enzymes)

87.14.ej

87.15.-v (Biomolecules: structure and physical properties) 87.15.A- (Theory, modeling, and computer simulation) 87.15.B- (Structure of biomolecules)

杨志伟, 郝东晓, 车一卓, 杨嘉辉, 张磊, 张胜利. Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors[J]. 中国物理B, 2018, 27(1): 18704-018704.

Zhi-wei Yang(杨志伟), Dong-xiao Hao(郝东晓), Yi-zhuo Che(车一卓), Jia-hui Yang(杨嘉辉), Lei Zhang(张磊), Sheng-li Zhang(张胜利). Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors[J]. Chin. Phys. B, 2018, 27(1): 18704-018704.

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Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors

Mutation-induced spatial differences in neuraminidase structure and sensitivity to neuraminidase inhibitors

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