On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus.
Identifieur interne : 001460 ( PubMed/Checkpoint ); précédent : 001459; suivant : 001461On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus.
Auteurs : Zai Wang [République populaire de Chine] ; 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.
Descripteurs français
- KwdFr :
- Adamantane (), Adamantane (analogues et dérivés), Adamantane (métabolisme), Adamantane (pharmacologie), Adamantane (usage thérapeutique), Biologie informatique, Eau (), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Helicase (), Helicase (génétique), Helicase (métabolisme), Interactions hydrophobes et hydrophiles, Liaison aux protéines (génétique), Liaison hydrogène, Modèles moléculaires, Mutation faux-sens (génétique), Protéines de l'enveloppe virale (génétique), Protéines de la matrice virale (génétique), Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Pyridines (), Pyridines (métabolisme), Pyridines (pharmacologie), Pyridines (usage thérapeutique), RNA helicases (), RNA helicases (génétique), RNA helicases (métabolisme), Résistance virale aux médicaments (génétique), Sites de fixation (génétique), Structure quaternaire des protéines, Syndrome respiratoire aigu sévère (traitement médicamenteux), Virus du SRAS (), Virus du SRAS (génétique), Électricité statique.
- MESH :
- analogues et dérivés : Adamantane.
- génétique : Glycoprotéines membranaires, Helicase, Liaison aux protéines, Mutation faux-sens, Protéines de l'enveloppe virale, Protéines de la matrice virale, Protéines virales, RNA helicases, Résistance virale aux médicaments, Sites de fixation, Virus du SRAS.
- métabolisme : Adamantane, Helicase, Protéines virales, Pyridines, RNA helicases.
- pharmacologie : Adamantane, Pyridines.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- usage thérapeutique : Adamantane, Pyridines.
- Adamantane, Biologie informatique, Eau, Glycoprotéine de spicule des coronavirus, Helicase, Interactions hydrophobes et hydrophiles, Liaison hydrogène, Modèles moléculaires, Protéines virales, Pyridines, RNA helicases, Structure quaternaire des protéines, Virus du SRAS, Électricité statique.
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
Affiliations:
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pubmed:21134131Le document en format XML
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<term>Adamantane (metabolism)</term>
<term>Adamantane (pharmacology)</term>
<term>Adamantane (therapeutic use)</term>
<term>Binding Sites (genetics)</term>
<term>Computational Biology</term>
<term>DNA Helicases (chemistry)</term>
<term>DNA Helicases (genetics)</term>
<term>DNA Helicases (metabolism)</term>
<term>Drug Resistance, Viral (genetics)</term>
<term>Hydrogen Bonding</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Models, Molecular</term>
<term>Mutation, Missense (genetics)</term>
<term>Protein Binding (genetics)</term>
<term>Protein Structure, Quaternary</term>
<term>Pyridines (chemistry)</term>
<term>Pyridines (metabolism)</term>
<term>Pyridines (pharmacology)</term>
<term>Pyridines (therapeutic use)</term>
<term>RNA Helicases (chemistry)</term>
<term>RNA Helicases (genetics)</term>
<term>RNA Helicases (metabolism)</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (genetics)</term>
<term>Severe Acute Respiratory Syndrome (drug therapy)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Static Electricity</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Matrix Proteins (genetics)</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
<term>Water (chemistry)</term>
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<term>Adamantane (analogues et dérivés)</term>
<term>Adamantane (métabolisme)</term>
<term>Adamantane (pharmacologie)</term>
<term>Adamantane (usage thérapeutique)</term>
<term>Biologie informatique</term>
<term>Eau ()</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Helicase ()</term>
<term>Helicase (génétique)</term>
<term>Helicase (métabolisme)</term>
<term>Interactions hydrophobes et hydrophiles</term>
<term>Liaison aux protéines (génétique)</term>
<term>Liaison hydrogène</term>
<term>Modèles moléculaires</term>
<term>Mutation faux-sens (génétique)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de la matrice virale (génétique)</term>
<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>Pyridines ()</term>
<term>Pyridines (métabolisme)</term>
<term>Pyridines (pharmacologie)</term>
<term>Pyridines (usage thérapeutique)</term>
<term>RNA helicases ()</term>
<term>RNA helicases (génétique)</term>
<term>RNA helicases (métabolisme)</term>
<term>Résistance virale aux médicaments (génétique)</term>
<term>Sites de fixation (génétique)</term>
<term>Structure quaternaire des protéines</term>
<term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (génétique)</term>
<term>Électricité statique</term>
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</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adamantane</term>
<term>DNA Helicases</term>
<term>Pyridines</term>
<term>RNA Helicases</term>
<term>Viral Proteins</term>
<term>Water</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Helicases</term>
<term>Membrane Glycoproteins</term>
<term>RNA Helicases</term>
<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adamantane</term>
<term>DNA Helicases</term>
<term>Pyridines</term>
<term>RNA Helicases</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Adamantane</term>
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<term>Pyridines</term>
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<term>Drug Resistance, Viral</term>
<term>Mutation, Missense</term>
<term>Protein Binding</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term>
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<term>Liaison aux protéines</term>
<term>Mutation faux-sens</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
<term>Protéines virales</term>
<term>RNA helicases</term>
<term>Résistance virale aux médicaments</term>
<term>Sites de fixation</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adamantane</term>
<term>Helicase</term>
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<keywords scheme="MESH" qualifier="usage thérapeutique" xml:lang="fr"><term>Adamantane</term>
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<term>Hydrogen Bonding</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Models, Molecular</term>
<term>Protein Structure, Quaternary</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Static Electricity</term>
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<term>Biologie informatique</term>
<term>Eau</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Helicase</term>
<term>Interactions hydrophobes et hydrophiles</term>
<term>Liaison hydrogène</term>
<term>Modèles moléculaires</term>
<term>Protéines virales</term>
<term>Pyridines</term>
<term>RNA helicases</term>
<term>Structure quaternaire des protéines</term>
<term>Virus du SRAS</term>
<term>Électricité statique</term>
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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>
</front>
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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>
<CopyrightInformation>© 2010 The Authors Journal compilation © 2010 FEBS.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Zai</ForeName>
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<ForeName>Hao-Jie</ForeName>
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<Author ValidYN="Y"><LastName>Tanner</LastName>
<ForeName>Julian A</ForeName>
<Initials>JA</Initials>
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<Initials>A</Initials>
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<ForeName>Bo-Jian</ForeName>
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