Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.
Identifieur interne : 001507 ( PubMed/Corpus ); précédent : 001506; suivant : 001508Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.
Auteurs : Qiaoli Li ; 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.
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 to Exploration step
pubmed:21620914Le document en format XML
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first="Zhenhuan" last="Zhao">Zhenhuan Zhao</name></author><author><name sortKey="Zhou, Dihan" sort="Zhou, Dihan" uniqKey="Zhou D" first="Dihan" last="Zhou">Dihan Zhou</name></author><author><name sortKey="Chen, Yaoqing" sort="Chen, Yaoqing" uniqKey="Chen Y" first="Yaoqing" last="Chen">Yaoqing Chen</name></author><author><name sortKey="Hong, Wei" sort="Hong, Wei" uniqKey="Hong W" first="Wei" last="Hong">Wei Hong</name></author><author><name sortKey="Cao, Luyang" sort="Cao, Luyang" uniqKey="Cao L" first="Luyang" last="Cao">Luyang Cao</name></author><author><name sortKey="Yang, Jingyi" sort="Yang, Jingyi" uniqKey="Yang J" first="Jingyi" last="Yang">Jingyi Yang</name></author><author><name sortKey="Zhang, Yan" sort="Zhang, Yan" uniqKey="Zhang Y" first="Yan" last="Zhang">Yan Zhang</name></author><author><name sortKey="Shi, Wei" sort="Shi, Wei" uniqKey="Shi W" first="Wei" last="Shi">Wei Shi</name></author><author><name sortKey="Cao, Zhijian" sort="Cao, Zhijian" uniqKey="Cao Z" first="Zhijian" last="Cao">Zhijian Cao</name></author><author><name sortKey="Wu, Yingliang" sort="Wu, Yingliang" uniqKey="Wu Y" first="Yingliang" last="Wu">Yingliang Wu</name></author><author><name sortKey="Yan, Huimin" sort="Yan, Huimin" uniqKey="Yan H" first="Huimin" last="Yan">Huimin Yan</name></author><author><name sortKey="Li, Wenxin" sort="Li, Wenxin" uniqKey="Li W" first="Wenxin" last="Li">Wenxin Li</name></author></analytic><series><title level="j">Peptides</title><idno type="eISSN">1873-5169</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><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><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization (drug effects)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antimicrobial Cationic Peptides</term><term>Scorpion Venoms</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antimicrobial Cationic Peptides</term><term>Scorpion Venoms</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Scorpion Venoms</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antimicrobial Cationic Peptides</term><term>Antiviral Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Scorpions</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Influenza A Virus, H5N1 Subtype</term><term>Morbillivirus</term><term>SARS Virus</term><term>Virus Internalization</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Influenza, Human</term><term>Measles</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Scorpions</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Scorpions</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Influenza, Human</term><term>Measles</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H5N1 Subtype</term><term>Morbillivirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Pandemics</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></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21620914</PMID><DateCompleted><Year>2011</Year><Month>11</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-5169</ISSN><JournalIssue CitedMedium="Internet"><Volume>32</Volume><Issue>7</Issue><PubDate><Year>2011</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Peptides</Title><ISOAbbreviation>Peptides</ISOAbbreviation></Journal><ArticleTitle>Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses.</ArticleTitle><Pagination><MedlinePgn>1518-25</MedlinePgn></Pagination><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></Author><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></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D023181">Antimicrobial Cationic Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012604">Scorpion Venoms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D023181" MajorTopicYN="N">Antimicrobial Cationic Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004285" MajorTopicYN="N">Dogs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015195" MajorTopicYN="N">Drug Design</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053124" MajorTopicYN="N">Influenza A Virus, H5N1 Subtype</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008457" MajorTopicYN="N">Measles</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018103" MajorTopicYN="N">Morbillivirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058873" MajorTopicYN="N">Pandemics</DescriptorName><QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012604" MajorTopicYN="N">Scorpion Venoms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012605" MajorTopicYN="N">Scorpions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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