On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus.
Identifieur interne : 001580 ( PubMed/Corpus ); précédent : 001579; suivant : 001581On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus.
Auteurs : Zai Wang ; Jian-Dong Huang ; Kin-Ling Wong ; Pei-Gang Wang ; Hao-Jie Zhang ; Julian A. Tanner ; Ottavia Spiga ; Andrea Bernini ; Bo-Jian Zheng ; Neri NiccolaiSource :
- The FEBS journal [ 1742-4658 ] ; 2011.
English descriptors
- KwdEn :
- Adamantane (analogs & derivatives), Adamantane (chemistry), Adamantane (metabolism), Adamantane (pharmacology), Adamantane (therapeutic use), Binding Sites (genetics), Computational Biology, DNA Helicases (chemistry), DNA Helicases (genetics), DNA Helicases (metabolism), Drug Resistance, Viral (genetics), Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Membrane Glycoproteins (genetics), Models, Molecular, Mutation, Missense (genetics), Protein Binding (genetics), Protein Structure, Quaternary, Pyridines (chemistry), Pyridines (metabolism), Pyridines (pharmacology), Pyridines (therapeutic use), RNA Helicases (chemistry), RNA Helicases (genetics), RNA Helicases (metabolism), SARS Virus (drug effects), SARS Virus (genetics), Severe Acute Respiratory Syndrome (drug therapy), Spike Glycoprotein, Coronavirus, Static Electricity, Viral Envelope Proteins (genetics), Viral Matrix Proteins (genetics), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism), Water (chemistry).
- MESH :
- chemical , analogs & derivatives : Adamantane.
- chemical , chemistry : Adamantane, DNA Helicases, Pyridines, RNA Helicases, Viral Proteins, Water.
- chemical , genetics : DNA Helicases, Membrane Glycoproteins, RNA Helicases, Viral Envelope Proteins, Viral Matrix Proteins, Viral Proteins.
- chemical , metabolism : Adamantane, DNA Helicases, Pyridines, RNA Helicases, Viral Proteins.
- chemical , pharmacology : Adamantane, Pyridines.
- chemical , therapeutic use : Adamantane, Pyridines.
- drug effects : SARS Virus.
- drug therapy : Severe Acute Respiratory Syndrome.
- genetics : Binding Sites, Drug Resistance, Viral, Mutation, Missense, Protein Binding, SARS Virus.
- Computational Biology, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Structure, Quaternary, Spike Glycoprotein, Coronavirus, Static Electricity.
Abstract
In a previous study, severe acute respiratory syndrome coronavirus (SARS-CoV) was cultured in the presence of bananin, an effective adamantane-related molecule with antiviral activity. In the present study, we show that all bananin-resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS-CoV bananin-resistant variants was performed. The S259/L mutation of SARS-CoV helicase is always found in all the identified bananin-resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS-CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS-CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.
DOI: 10.1111/j.1742-4658.2010.07961.x
PubMed: 21134131
Links to Exploration step
pubmed:21134131Le document en format XML
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<front><div type="abstract" xml:lang="en">In a previous study, severe acute respiratory syndrome coronavirus (SARS-CoV) was cultured in the presence of bananin, an effective adamantane-related molecule with antiviral activity. In the present study, we show that all bananin-resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS-CoV bananin-resistant variants was performed. The S259/L mutation of SARS-CoV helicase is always found in all the identified bananin-resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS-CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS-CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.</div>
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<Abstract><AbstractText>In a previous study, severe acute respiratory syndrome coronavirus (SARS-CoV) was cultured in the presence of bananin, an effective adamantane-related molecule with antiviral activity. In the present study, we show that all bananin-resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS-CoV bananin-resistant variants was performed. The S259/L mutation of SARS-CoV helicase is always found in all the identified bananin-resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS-CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS-CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.</AbstractText>
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