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

• 来源期刊: 中国物理B（英文版）
• 关键词: mutation active sites neuraminidase inhibitor sensitivity
• 年，卷（期）: 2018,（1）
• 页码范围: 145-153
• 页数: 9页
• 语种: 英文
• DOI: 10.1088/1674-1056/27/1/018704

摘要

Neuraminidase (NA), a major surface glycoprotein of infl uenza virus with well-defined active sites, is an ideal plat-form 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.