Journal
ANTIVIRAL RESEARCH
Volume 100, Issue 2, Pages 399-406Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.antiviral.2013.08.021
Keywords
Hemagglutinin; Influenza virus; Antiviral inhibitor; Arbidol; Gel electrophoresis
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Funding
- Australian Research Council [DP110101702]
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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.
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