Inhibition of influenza hemagglutinin with the antiviral inhibitor arbidol using a proteomics based approach and mass spectrometry
Inhibition of influenza hemagglutinin with the antiviral inhibitor arbidol using a proteomics based approach and mass spectrometry
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DOI：
10.1016/j.antiviral.2013.08.021
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发表时间：
2013-11-01
影响因子：
7.6
通讯作者：
Downard, Kevin M.
中科院分区：
文献类型：
--
作者：
Nasser, Zainab H.;Swaminathan, Kavya;Downard, Kevin M.
应用蛋白质组学凝胶电泳方法，通过定量血凝素水平，研究阿比多尔对流感病毒体外增殖的影响。阿比多尔浓度为20 μ g/ml时，可使病毒增殖和血凝素水平降低50%。使用MALDI质谱法研究阿比多尔与流感血凝素的结合，发现它仅与HA2亚基的104-120残基结合，该区域已知含有阿比多尔耐药性突变。平行分子对接结果表明，在HA2残基118-123处，阿比多酚分子以两种可能的方向相互约180度的方向结合。这些综合研究支持阿比多尔作为一种有效的靶向流感病毒抗病毒药物的公认潜力。(C) 2013 Elsevier B.V.版权所有
A proteomics gel electrophoresis based approach has been applied to study the effect of arbidol on the proliferation of influenza virus in vitro through quantitation of hemagglutinin levels. An arbidol concentration of 20 mu g/ml was required to achieve a 50% reduction in virus proliferation and hemagglutinin levels. The use of a MALDI mass spectrometry approach to study the binding of arbidol to influenza hemagglutinin revealed it bound solely to residues 104-120 of the HA2 subunit, a region known to contain an arbidol resistance mutation. Parallel molecular docking results revealed that this binding site was favoured in which the arbidol molecule binds in two possible orientations approximately 180 degrees to one another at HA2 residues 118-123. The combined studies support the recognized potential of arbidol as an effective and targeted antiviral agent against the influenza virus. (C) 2013 Elsevier B.V. All rights reserved.