tetano
Editor, Senior Moderator
Antiviral Res. 2013 Sep 3. pii: S0166-3542(13)00241-6. doi: 10.1016/j.antiviral.2013.08.021. [Epub ahead of print]
Inhibition of influenza hemagglutinin with the antiviral inhibitor arbidol using a proteomics based approach and mass spectrometry.
Nasser ZH, Swaminathan K, M?ller P, Downard KM.
Source
School of Molecular Bioscience, University of Sydney, Sydney, Australia.
Abstract
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 20ug/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? 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.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
Antiviral inhibitor, Arbidol, Gel electrophoresis, Hemagglutinin, Influenza virus
PMID:
24012882
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24012882
Inhibition of influenza hemagglutinin with the antiviral inhibitor arbidol using a proteomics based approach and mass spectrometry.
Nasser ZH, Swaminathan K, M?ller P, Downard KM.
Source
School of Molecular Bioscience, University of Sydney, Sydney, Australia.
Abstract
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 20ug/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? 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.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
Antiviral inhibitor, Arbidol, Gel electrophoresis, Hemagglutinin, Influenza virus
PMID:
24012882
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24012882