Journal
CHINESE PHYSICS B
Volume 27, Issue 1, Pages -Publisher
IOP Publishing Ltd
DOI: 10.1088/1674-1056/27/1/018704
Keywords
mutation; active sites; neuraminidase; inhibitor sensitivity
Categories
Funding
- National Natural Science Foundation of China [11374237, 11504287]
- Fundamental Research Funds for the Central Universities, China
- China Postdoctoral Science Foundation [2017M613147]
- Shaanxi Province Postdoctoral Science Foundation, China
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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.
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