Neuraminidase （NA）, a major surface glycoprotein of influenza 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 ...Neuraminidase （NA）, a major surface glycoprotein of influenza 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 tbr the development of novel inhibitors.展开更多
基金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)Shaanxi Province Postdoctoral Science Foundation,China
文摘Neuraminidase （NA）, a major surface glycoprotein of influenza 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 tbr the development of novel inhibitors.
