Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.
Identifieur interne : 002344 ( Ncbi/Merge ); précédent : 002343; suivant : 002345Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.
Auteurs : Qiaoli Li [République populaire de Chine] ; Zhenhuan Zhao ; Dihan Zhou ; Yaoqing Chen ; Wei Hong ; Luyang Cao ; Jingyi Yang ; Yan Zhang ; Wei Shi ; Zhijian Cao ; Yingliang Wu ; Huimin Yan ; Wenxin LiSource :
- Peptides [ 1873-5169 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Antiviraux (pharmacologie), Antiviraux (usage thérapeutique), Chiens, Concentration inhibitrice 50, Conception de médicament, Données de séquences moléculaires, Grippe humaine (anatomopathologie), Grippe humaine (traitement médicamenteux), Grippe humaine (virologie), Humains, Liaison aux protéines, Lignée cellulaire, Morbillivirus (), Morbillivirus (physiologie), Pandémies (), Peptides antimicrobiens cationiques (), Peptides antimicrobiens cationiques (génétique), Peptides antimicrobiens cationiques (pharmacologie), Protéines de l'enveloppe virale (métabolisme), Pénétration virale (), Rougeole (anatomopathologie), Rougeole (traitement médicamenteux), Rougeole (virologie), Réplication virale (), Scorpions (), Scorpions (génétique), Scorpions (métabolisme), Sous-type H5N1 du virus de la grippe A (), Sous-type H5N1 du virus de la grippe A (physiologie), Syndrome respiratoire aigu sévère (anatomopathologie), Syndrome respiratoire aigu sévère (traitement médicamenteux), Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Venins de scorpion (), Venins de scorpion (génétique), Venins de scorpion (métabolisme), Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- anatomopathologie : Grippe humaine, Rougeole, Syndrome respiratoire aigu sévère.
- génétique : Peptides antimicrobiens cationiques, Scorpions, Venins de scorpion.
- métabolisme : Protéines de l'enveloppe virale, Scorpions, Venins de scorpion.
- pharmacologie : Antiviraux, Peptides antimicrobiens cationiques.
- physiologie : Morbillivirus, Sous-type H5N1 du virus de la grippe A, Virus du SRAS.
- traitement médicamenteux : Grippe humaine, Rougeole, Syndrome respiratoire aigu sévère.
- usage thérapeutique : Antiviraux.
- virologie : Grippe humaine, Rougeole, Syndrome respiratoire aigu sévère.
- Animaux, Chiens, Concentration inhibitrice 50, Conception de médicament, Données de séquences moléculaires, Humains, Liaison aux protéines, Lignée cellulaire, Morbillivirus, Pandémies, Peptides antimicrobiens cationiques, Pénétration virale, Réplication virale, Scorpions, Sous-type H5N1 du virus de la grippe A, Séquence d'acides aminés, Venins de scorpion, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antimicrobial Cationic Peptides (chemistry), Antimicrobial Cationic Peptides (genetics), Antimicrobial Cationic Peptides (pharmacology), Antiviral Agents (pharmacology), Antiviral Agents (therapeutic use), Cell Line, Dogs, Drug Design, Humans, Influenza A Virus, H5N1 Subtype (drug effects), Influenza A Virus, H5N1 Subtype (physiology), Influenza, Human (drug therapy), Influenza, Human (pathology), Influenza, Human (virology), Inhibitory Concentration 50, Measles (drug therapy), Measles (pathology), Measles (virology), Molecular Sequence Data, Morbillivirus (drug effects), Morbillivirus (physiology), Pandemics (prevention & control), Protein Binding, SARS Virus (drug effects), SARS Virus (physiology), Scorpion Venoms (chemistry), Scorpion Venoms (genetics), Scorpion Venoms (metabolism), Scorpions (chemistry), Scorpions (genetics), Scorpions (metabolism), Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (virology), Viral Envelope Proteins (metabolism), Virus Internalization (drug effects), Virus Replication (drug effects).
- MESH :
- chemical , chemistry : Antimicrobial Cationic Peptides, Scorpion Venoms.
- chemical , genetics : Antimicrobial Cationic Peptides, Scorpion Venoms.
- chemical , metabolism : Scorpion Venoms, Viral Envelope Proteins.
- chemical , pharmacology : Antimicrobial Cationic Peptides, Antiviral Agents.
- chemical , therapeutic use : Antiviral Agents.
- chemistry : Scorpions.
- drug effects : Influenza A Virus, H5N1 Subtype, Morbillivirus, SARS Virus, Virus Internalization, Virus Replication.
- drug therapy : Influenza, Human, Measles, Severe Acute Respiratory Syndrome.
- genetics : Scorpions.
- metabolism : Scorpions.
- pathology : Influenza, Human, Measles, Severe Acute Respiratory Syndrome.
- physiology : Influenza A Virus, H5N1 Subtype, Morbillivirus, SARS Virus.
- prevention & control : Pandemics.
- virology : Influenza, Human, Measles, Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Cell Line, Dogs, Drug Design, Humans, Inhibitory Concentration 50, Molecular Sequence Data, Protein Binding.
Abstract
Outbreaks of SARS-CoV, influenza A (H5N1, H1N1) and measles viruses in recent years have raised serious concerns about the measures available to control emerging and re-emerging infectious viral diseases. Effective antiviral agents are lacking that specifically target RNA viruses such as measles, SARS-CoV and influenza H5N1 viruses, and available vaccinations have demonstrated variable efficacy. Therefore, the development of novel antiviral agents is needed to close the vaccination gap and silence outbreaks. We previously identified mucroporin, a cationic host defense peptide from scorpion venom, which can effectively inhibit standard bacteria. The optimized mucroporin-M1 can inhibit gram-positive bacteria at low concentrations and antibiotic-resistant pathogens. In this investigation, we further tested mucroporin and the optimized mucroporin-M1 for their antiviral activity. Surprisingly, we found that the antiviral activities of mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses were notably increased with an EC₅₀ of 7.15 μg/ml (3.52 μM) and a CC₅₀ of 70.46 μg/ml (34.70 μM) against measles virus, an EC₅₀ of 14.46 μg/ml (7.12 μM) against SARS-CoV and an EC₅₀ of 2.10 μg/ml (1.03 μM) against H5N1, while the original peptide mucroporin showed no antiviral activity against any of these three viruses. The inhibition model could be via a direct interaction with the virus envelope, thereby decreasing the infectivity of virus. This report provides evidence that host defense peptides from scorpion venom can be modified for antiviral activity by rational design and represents a practical approach for developing broad-spectrum antiviral agents, especially against RNA viruses.
DOI: 10.1016/j.peptides.2011.05.015
PubMed: 21620914
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001507
- to stream PubMed, to step Curation: 001507
- to stream PubMed, to step Checkpoint: 001403
Links to Exploration step
pubmed:21620914Le document en format XML
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<term>Animals</term>
<term>Antimicrobial Cationic Peptides (chemistry)</term>
<term>Antimicrobial Cationic Peptides (genetics)</term>
<term>Antimicrobial Cationic Peptides (pharmacology)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Antiviral Agents (therapeutic use)</term>
<term>Cell Line</term>
<term>Dogs</term>
<term>Drug Design</term>
<term>Humans</term>
<term>Influenza A Virus, H5N1 Subtype (drug effects)</term>
<term>Influenza A Virus, H5N1 Subtype (physiology)</term>
<term>Influenza, Human (drug therapy)</term>
<term>Influenza, Human (pathology)</term>
<term>Influenza, Human (virology)</term>
<term>Inhibitory Concentration 50</term>
<term>Measles (drug therapy)</term>
<term>Measles (pathology)</term>
<term>Measles (virology)</term>
<term>Molecular Sequence Data</term>
<term>Morbillivirus (drug effects)</term>
<term>Morbillivirus (physiology)</term>
<term>Pandemics (prevention & control)</term>
<term>Protein Binding</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (physiology)</term>
<term>Scorpion Venoms (chemistry)</term>
<term>Scorpion Venoms (genetics)</term>
<term>Scorpion Venoms (metabolism)</term>
<term>Scorpions (chemistry)</term>
<term>Scorpions (genetics)</term>
<term>Scorpions (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (drug therapy)</term>
<term>Severe Acute Respiratory Syndrome (pathology)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
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<term>Virus Replication (drug effects)</term>
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<term>Antiviraux (pharmacologie)</term>
<term>Antiviraux (usage thérapeutique)</term>
<term>Chiens</term>
<term>Concentration inhibitrice 50</term>
<term>Conception de médicament</term>
<term>Données de séquences moléculaires</term>
<term>Grippe humaine (anatomopathologie)</term>
<term>Grippe humaine (traitement médicamenteux)</term>
<term>Grippe humaine (virologie)</term>
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<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Morbillivirus ()</term>
<term>Morbillivirus (physiologie)</term>
<term>Pandémies ()</term>
<term>Peptides antimicrobiens cationiques ()</term>
<term>Peptides antimicrobiens cationiques (génétique)</term>
<term>Peptides antimicrobiens cationiques (pharmacologie)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Pénétration virale ()</term>
<term>Rougeole (anatomopathologie)</term>
<term>Rougeole (traitement médicamenteux)</term>
<term>Rougeole (virologie)</term>
<term>Réplication virale ()</term>
<term>Scorpions ()</term>
<term>Scorpions (génétique)</term>
<term>Scorpions (métabolisme)</term>
<term>Sous-type H5N1 du virus de la grippe A ()</term>
<term>Sous-type H5N1 du virus de la grippe A (physiologie)</term>
<term>Syndrome respiratoire aigu sévère (anatomopathologie)</term>
<term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Séquence d'acides aminés</term>
<term>Venins de scorpion ()</term>
<term>Venins de scorpion (génétique)</term>
<term>Venins de scorpion (métabolisme)</term>
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<term>Virus du SRAS (physiologie)</term>
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<term>Scorpion Venoms</term>
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<term>Antiviral Agents</term>
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<term>Scorpions</term>
<term>Venins de scorpion</term>
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<term>Scorpions</term>
<term>Venins de scorpion</term>
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<term>Severe Acute Respiratory Syndrome</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term>
<term>Peptides antimicrobiens cationiques</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Morbillivirus</term>
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<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H5N1 Subtype</term>
<term>Morbillivirus</term>
<term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Pandemics</term>
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<keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Grippe humaine</term>
<term>Rougeole</term>
<term>Syndrome respiratoire aigu sévère</term>
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<keywords scheme="MESH" qualifier="usage thérapeutique" xml:lang="fr"><term>Antiviraux</term>
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<term>Rougeole</term>
<term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term>
<term>Measles</term>
<term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cell Line</term>
<term>Dogs</term>
<term>Drug Design</term>
<term>Humans</term>
<term>Inhibitory Concentration 50</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Chiens</term>
<term>Concentration inhibitrice 50</term>
<term>Conception de médicament</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
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<front><div type="abstract" xml:lang="en">Outbreaks of SARS-CoV, influenza A (H5N1, H1N1) and measles viruses in recent years have raised serious concerns about the measures available to control emerging and re-emerging infectious viral diseases. Effective antiviral agents are lacking that specifically target RNA viruses such as measles, SARS-CoV and influenza H5N1 viruses, and available vaccinations have demonstrated variable efficacy. Therefore, the development of novel antiviral agents is needed to close the vaccination gap and silence outbreaks. We previously identified mucroporin, a cationic host defense peptide from scorpion venom, which can effectively inhibit standard bacteria. The optimized mucroporin-M1 can inhibit gram-positive bacteria at low concentrations and antibiotic-resistant pathogens. In this investigation, we further tested mucroporin and the optimized mucroporin-M1 for their antiviral activity. Surprisingly, we found that the antiviral activities of mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses were notably increased with an EC₅₀ of 7.15 μg/ml (3.52 μM) and a CC₅₀ of 70.46 μg/ml (34.70 μM) against measles virus, an EC₅₀ of 14.46 μg/ml (7.12 μM) against SARS-CoV and an EC₅₀ of 2.10 μg/ml (1.03 μM) against H5N1, while the original peptide mucroporin showed no antiviral activity against any of these three viruses. The inhibition model could be via a direct interaction with the virus envelope, thereby decreasing the infectivity of virus. This report provides evidence that host defense peptides from scorpion venom can be modified for antiviral activity by rational design and represents a practical approach for developing broad-spectrum antiviral agents, especially against RNA viruses.</div>
</front>
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<Title>Peptides</Title>
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<ArticleTitle>Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.</ArticleTitle>
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<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.peptides.2011.05.015</ELocationID>
<Abstract><AbstractText>Outbreaks of SARS-CoV, influenza A (H5N1, H1N1) and measles viruses in recent years have raised serious concerns about the measures available to control emerging and re-emerging infectious viral diseases. Effective antiviral agents are lacking that specifically target RNA viruses such as measles, SARS-CoV and influenza H5N1 viruses, and available vaccinations have demonstrated variable efficacy. Therefore, the development of novel antiviral agents is needed to close the vaccination gap and silence outbreaks. We previously identified mucroporin, a cationic host defense peptide from scorpion venom, which can effectively inhibit standard bacteria. The optimized mucroporin-M1 can inhibit gram-positive bacteria at low concentrations and antibiotic-resistant pathogens. In this investigation, we further tested mucroporin and the optimized mucroporin-M1 for their antiviral activity. Surprisingly, we found that the antiviral activities of mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses were notably increased with an EC₅₀ of 7.15 μg/ml (3.52 μM) and a CC₅₀ of 70.46 μg/ml (34.70 μM) against measles virus, an EC₅₀ of 14.46 μg/ml (7.12 μM) against SARS-CoV and an EC₅₀ of 2.10 μg/ml (1.03 μM) against H5N1, while the original peptide mucroporin showed no antiviral activity against any of these three viruses. The inhibition model could be via a direct interaction with the virus envelope, thereby decreasing the infectivity of virus. This report provides evidence that host defense peptides from scorpion venom can be modified for antiviral activity by rational design and represents a practical approach for developing broad-spectrum antiviral agents, especially against RNA viruses.</AbstractText>
<CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Qiaoli</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhao</LastName>
<ForeName>Zhenhuan</ForeName>
<Initials>Z</Initials>
</Author>
<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Dihan</ForeName>
<Initials>D</Initials>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Yaoqing</ForeName>
<Initials>Y</Initials>
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<Author ValidYN="Y"><LastName>Hong</LastName>
<ForeName>Wei</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Luyang</ForeName>
<Initials>L</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Jingyi</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Yan</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Wei</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Zhijian</ForeName>
<Initials>Z</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Yingliang</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yan</LastName>
<ForeName>Huimin</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Wenxin</ForeName>
<Initials>W</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2011</Year>
<Month>05</Month>
<Day>19</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Peptides</MedlineTA>
<NlmUniqueID>8008690</NlmUniqueID>
<ISSNLinking>0196-9781</ISSNLinking>
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<NameOfSubstance UI="D012604">Scorpion Venoms</NameOfSubstance>
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<NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance>
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</ChemicalList>
<CitationSubset>IM</CitationSubset>
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</MeshHeading>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
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<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
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<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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</MeshHeading>
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</MeshHeading>
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<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
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<affiliations><list><country><li>République populaire de Chine</li>
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