Inhibition of Enterovirus 71 (EV-71) Infections by a Novel Antiviral Peptide Derived from EV-71 Capsid Protein VP1
Identifieur interne : 000957 ( Ncbi/Merge ); précédent : 000956; suivant : 000958Inhibition of Enterovirus 71 (EV-71) Infections by a Novel Antiviral Peptide Derived from EV-71 Capsid Protein VP1
Auteurs : Chee Wah Tan [Malaisie] ; Yoke Fun Chan [Malaisie] ; Kooi Mow Sim [Malaisie] ; Eng Lee Tan [Singapour] ; Chit Laa Poh [Malaisie]Source :
- PLoS ONE [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Alanine (), Alanine (génétique), Animaux, Antiviraux (pharmacologie), Antiviraux (synthèse chimique), Banque de peptides, Cellules HT29, Cellules HeLa, Cellules Vero, Concentration inhibitrice 50, Conformation des protéines, Données de séquences moléculaires, Entérovirus humain A (), Entérovirus humain A (croissance et développement), Entérovirus humain A (génétique), Humains, Infections à entérovirus (), Infections à entérovirus (virologie), Lignée cellulaire tumorale, Modèles moléculaires, Oligopeptides (génétique), Oligopeptides (pharmacologie), Oligopeptides (synthèse chimique), Prolifération cellulaire (), Protéines de capside (), Protéines de capside (génétique), Similitude de séquences d'acides aminés, Structure secondaire des protéines, Substitution d'acide aminé, Survie cellulaire (), Séquence d'acides aminés.
- MESH :
- croissance et développement : Entérovirus humain A.
- génétique : Alanine, Entérovirus humain A, Oligopeptides, Protéines de capside.
- pharmacologie : Antiviraux, Oligopeptides.
- synthèse chimique : Antiviraux, Oligopeptides.
- virologie : Infections à entérovirus.
- Alanine, Animaux, Banque de peptides, Cellules HT29, Cellules HeLa, Cellules Vero, Concentration inhibitrice 50, Conformation des protéines, Données de séquences moléculaires, Entérovirus humain A, Humains, Infections à entérovirus, Lignée cellulaire tumorale, Modèles moléculaires, Prolifération cellulaire, Protéines de capside, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Substitution d'acide aminé, Survie cellulaire, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Alanine (chemistry), Alanine (genetics), Amino Acid Sequence, Amino Acid Substitution, Animals, Antiviral Agents (chemical synthesis), Antiviral Agents (pharmacology), Capsid Proteins (chemistry), Capsid Proteins (genetics), Cell Line, Tumor, Cell Proliferation (drug effects), Cell Survival (drug effects), Chlorocebus aethiops, Enterovirus A, Human (drug effects), Enterovirus A, Human (genetics), Enterovirus A, Human (growth & development), Enterovirus Infections (prevention & control), Enterovirus Infections (virology), HT29 Cells, HeLa Cells, Humans, Inhibitory Concentration 50, Models, Molecular, Molecular Sequence Data, Oligopeptides (chemical synthesis), Oligopeptides (genetics), Oligopeptides (pharmacology), Peptide Library, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Vero Cells.
- MESH :
- chemical , chemical synthesis : Antiviral Agents, Oligopeptides.
- chemical , chemistry : Alanine, Capsid Proteins.
- chemical , genetics : Alanine, Capsid Proteins, Oligopeptides.
- chemical , pharmacology : Antiviral Agents, Oligopeptides.
- drug effects : Cell Proliferation, Cell Survival, Enterovirus A, Human.
- genetics : Enterovirus A, Human.
- growth & development : Enterovirus A, Human.
- prevention & control : Enterovirus Infections.
- virology : Enterovirus Infections.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Tumor, Chlorocebus aethiops, HT29 Cells, HeLa Cells, Humans, Inhibitory Concentration 50, Models, Molecular, Molecular Sequence Data, Peptide Library, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Vero Cells.
Abstract
Enterovirus 71 (EV-71) is the main causative agent of hand, foot and mouth disease (HFMD). In recent years, EV-71 infections were reported to cause high fatalities and severe neurological complications in Asia. Currently, no effective antiviral or vaccine is available to treat or prevent EV-71 infection. In this study, we have discovered a synthetic peptide which could be developed as a potential antiviral for inhibition of EV-71. Ninety five synthetic peptides (15-mers) overlapping the entire EV-71 capsid protein, VP1, were chemically synthesized and tested for antiviral properties against EV-71 in human Rhabdomyosarcoma (RD) cells. One peptide, SP40, was found to significantly reduce cytopathic effects of all representative EV-71 strains from genotypes A, B and C tested, with IC50 values ranging from 6–9.3 µM in RD cells. The
Url:
DOI: 10.1371/journal.pone.0034589
PubMed: 22563456
PubMed Central: 3341398
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PMC:3341398Le document en format XML
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Fun" uniqKey="Chan Y" first="Yoke Fun" last="Chan">Yoke Fun Chan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Sim, Kooi Mow" sort="Sim, Kooi Mow" uniqKey="Sim K" first="Kooi Mow" last="Sim">Kooi Mow Sim</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar</wicri:regionArea><wicri:noRegion>Kampar</wicri:noRegion></affiliation></author><author><name sortKey="Tan, Eng Lee" sort="Tan, Eng Lee" uniqKey="Tan E" first="Eng Lee" last="Tan">Eng Lee Tan</name><affiliation wicri:level="1"><nlm:aff id="aff3"><addr-line>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore, Singapore</addr-line></nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore</wicri:regionArea><wicri:noRegion>Singapore</wicri:noRegion></affiliation></author><author><name sortKey="Poh, Chit Laa" sort="Poh, Chit Laa" uniqKey="Poh C" first="Chit Laa" last="Poh">Chit Laa Poh</name><affiliation wicri:level="1"><nlm:aff id="aff4"><addr-line>School of Health and Natural Sciences, Sunway University, Petaling Jaya, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>School of Health and Natural Sciences, Sunway University, Petaling Jaya</wicri:regionArea><wicri:noRegion>Petaling Jaya</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine (chemistry)</term><term>Alanine (genetics)</term><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Antiviral Agents (chemical synthesis)</term><term>Antiviral Agents (pharmacology)</term><term>Capsid Proteins (chemistry)</term><term>Capsid Proteins (genetics)</term><term>Cell Line, Tumor</term><term>Cell Proliferation (drug effects)</term><term>Cell Survival (drug effects)</term><term>Chlorocebus aethiops</term><term>Enterovirus A, Human (drug effects)</term><term>Enterovirus A, Human (genetics)</term><term>Enterovirus A, Human (growth & development)</term><term>Enterovirus Infections (prevention & control)</term><term>Enterovirus Infections (virology)</term><term>HT29 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (genetics)</term><term>Oligopeptides (pharmacology)</term><term>Peptide Library</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alanine ()</term><term>Alanine (génétique)</term><term>Animaux</term><term>Antiviraux (pharmacologie)</term><term>Antiviraux (synthèse chimique)</term><term>Banque de peptides</term><term>Cellules HT29</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Concentration inhibitrice 50</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Entérovirus humain A ()</term><term>Entérovirus humain A (croissance et développement)</term><term>Entérovirus humain A (génétique)</term><term>Humains</term><term>Infections à entérovirus ()</term><term>Infections à entérovirus (virologie)</term><term>Lignée cellulaire tumorale</term><term>Modèles moléculaires</term><term>Oligopeptides (génétique)</term><term>Oligopeptides (pharmacologie)</term><term>Oligopeptides (synthèse chimique)</term><term>Prolifération cellulaire ()</term><term>Protéines de capside ()</term><term>Protéines de capside (génétique)</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé</term><term>Survie cellulaire ()</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Antiviral Agents</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alanine</term><term>Capsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alanine</term><term>Capsid Proteins</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Entérovirus humain A</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Proliferation</term><term>Cell Survival</term><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alanine</term><term>Entérovirus humain A</term><term>Oligopeptides</term><term>Protéines de capside</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Enterovirus Infections</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Antiviraux</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à entérovirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Enterovirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line, Tumor</term><term>Chlorocebus aethiops</term><term>HT29 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptide Library</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alanine</term><term>Animaux</term><term>Banque de peptides</term><term>Cellules HT29</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Concentration inhibitrice 50</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Entérovirus humain A</term><term>Humains</term><term>Infections à entérovirus</term><term>Lignée cellulaire tumorale</term><term>Modèles moléculaires</term><term>Prolifération cellulaire</term><term>Protéines de capside</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé</term><term>Survie cellulaire</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Enterovirus 71 (EV-71) is the main causative agent of hand, foot and mouth disease (HFMD). In recent years, EV-71 infections were reported to cause high fatalities and severe neurological complications in Asia. Currently, no effective antiviral or vaccine is available to treat or prevent EV-71 infection. In this study, we have discovered a synthetic peptide which could be developed as a potential antiviral for inhibition of EV-71. Ninety five synthetic peptides (15-mers) overlapping the entire EV-71 capsid protein, VP1, were chemically synthesized and tested for antiviral properties against EV-71 in human Rhabdomyosarcoma (RD) cells. One peptide, SP40, was found to significantly reduce cytopathic effects of all representative EV-71 strains from genotypes A, B and C tested, with IC<sub>50</sub> values ranging from 6–9.3 µM in RD cells. The <italic>in vitro</italic> inhibitory effect of SP40 exhibited a dose dependent concentration corresponding to a decrease in infectious viral particles, total viral RNA and the levels of VP1 protein. The antiviral activity of SP40 peptide was not restricted to a specific cell line as inhibition of EV-71 was observed in RD, HeLa, HT-29 and Vero cells. Besides inhibition of EV-71, it also had antiviral activities against CV-A16 and poliovirus type 1 in cell culture. Mechanism of action studies suggested that the SP40 peptide was not virucidal but was able to block viral attachment to the RD cells. Substitutions of arginine and lysine residues with alanine in the SP40 peptide at positions R3A, R4A, K5A and R13A were found to significantly decrease antiviral activities, implying the importance of positively charged amino acids for the antiviral activities. The data demonstrated the potential and feasibility of SP40 as a broad spectrum antiviral agent against EV-71.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Stanway, G" uniqKey="Stanway G">G Stanway</name></author><author><name sortKey="Brown, F" uniqKey="Brown F">F Brown</name></author><author><name sortKey="Christian, P" uniqKey="Christian P">P Christian</name></author><author><name sortKey="Hovi, T" uniqKey="Hovi T">T Hovi</name></author><author><name sortKey="Tyypia, T" uniqKey="Tyypia T">T Tyypia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brown, Ba" uniqKey="Brown B">BA Brown</name></author><author><name sortKey="Pallansch, Ma" uniqKey="Pallansch M">MA Pallansch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shindarov, Lm" uniqKey="Shindarov L">LM Shindarov</name></author><author><name sortKey="Chumakov, Mp" uniqKey="Chumakov M">MP 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uniqKey="Belaid A">A Belaid</name></author><author><name sortKey="Aouni, M" uniqKey="Aouni M">M Aouni</name></author><author><name sortKey="Khelifa, R" uniqKey="Khelifa R">R Khelifa</name></author><author><name sortKey="Trabelsi, A" uniqKey="Trabelsi A">A Trabelsi</name></author><author><name sortKey="Jemmali, M" uniqKey="Jemmali M">M Jemmali</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Andersen, Jh" uniqKey="Andersen J">JH Andersen</name></author><author><name sortKey="Jenssen, H" uniqKey="Jenssen H">H Jenssen</name></author><author><name sortKey="Gutteberg, Tj" uniqKey="Gutteberg T">TJ Gutteberg</name></author></analytic></biblStruct></listBibl></div1></back></TEI><double pmid="22563456"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibition of Enterovirus 71 (EV-71) Infections by a Novel Antiviral Peptide Derived from EV-71 Capsid Protein VP1</title><author><name sortKey="Tan, Chee Wah" sort="Tan, Chee Wah" uniqKey="Tan C" first="Chee Wah" last="Tan">Chee Wah Tan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Chan, Yoke Fun" sort="Chan, Yoke Fun" uniqKey="Chan Y" first="Yoke Fun" last="Chan">Yoke Fun Chan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Sim, Kooi Mow" sort="Sim, Kooi Mow" uniqKey="Sim K" first="Kooi Mow" last="Sim">Kooi Mow Sim</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar</wicri:regionArea><wicri:noRegion>Kampar</wicri:noRegion></affiliation></author><author><name sortKey="Tan, Eng Lee" sort="Tan, Eng Lee" uniqKey="Tan E" first="Eng Lee" last="Tan">Eng Lee Tan</name><affiliation wicri:level="1"><nlm:aff id="aff3"><addr-line>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore, Singapore</addr-line></nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore</wicri:regionArea><wicri:noRegion>Singapore</wicri:noRegion></affiliation></author><author><name sortKey="Poh, Chit Laa" sort="Poh, Chit Laa" uniqKey="Poh C" first="Chit Laa" last="Poh">Chit Laa Poh</name><affiliation wicri:level="1"><nlm:aff id="aff4"><addr-line>School of Health and Natural Sciences, Sunway University, Petaling Jaya, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>School of Health and Natural Sciences, Sunway University, Petaling Jaya</wicri:regionArea><wicri:noRegion>Petaling Jaya</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22563456</idno><idno type="pmc">3341398</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3341398</idno><idno type="RBID">PMC:3341398</idno><idno type="doi">10.1371/journal.pone.0034589</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">001066</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001066</idno><idno type="wicri:Area/Pmc/Curation">001066</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001066</idno><idno type="wicri:Area/Pmc/Checkpoint">001298</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">001298</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Inhibition of Enterovirus 71 (EV-71) Infections by a Novel Antiviral Peptide Derived from EV-71 Capsid Protein VP1</title><author><name sortKey="Tan, Chee Wah" sort="Tan, Chee Wah" uniqKey="Tan C" first="Chee Wah" last="Tan">Chee Wah Tan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Chan, Yoke Fun" sort="Chan, Yoke Fun" uniqKey="Chan Y" first="Yoke Fun" last="Chan">Yoke Fun Chan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Sim, Kooi Mow" sort="Sim, Kooi Mow" uniqKey="Sim K" first="Kooi Mow" last="Sim">Kooi Mow Sim</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar</wicri:regionArea><wicri:noRegion>Kampar</wicri:noRegion></affiliation></author><author><name sortKey="Tan, Eng Lee" sort="Tan, Eng Lee" uniqKey="Tan E" first="Eng Lee" last="Tan">Eng Lee Tan</name><affiliation wicri:level="1"><nlm:aff id="aff3"><addr-line>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore, Singapore</addr-line></nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>Centre for Biomedical and Life Sciences, Singapore Polytechnic, Singapore</wicri:regionArea><wicri:noRegion>Singapore</wicri:noRegion></affiliation></author><author><name sortKey="Poh, Chit Laa" sort="Poh, Chit Laa" uniqKey="Poh C" first="Chit Laa" last="Poh">Chit Laa Poh</name><affiliation wicri:level="1"><nlm:aff id="aff4"><addr-line>School of Health and Natural Sciences, Sunway University, Petaling Jaya, Malaysia</addr-line></nlm:aff><country xml:lang="fr">Malaisie</country><wicri:regionArea>School of Health and Natural Sciences, Sunway University, Petaling Jaya</wicri:regionArea><wicri:noRegion>Petaling Jaya</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Enterovirus 71 (EV-71) is the main causative agent of hand, foot and mouth disease (HFMD). In recent years, EV-71 infections were reported to cause high fatalities and severe neurological complications in Asia. Currently, no effective antiviral or vaccine is available to treat or prevent EV-71 infection. In this study, we have discovered a synthetic peptide which could be developed as a potential antiviral for inhibition of EV-71. Ninety five synthetic peptides (15-mers) overlapping the entire EV-71 capsid protein, VP1, were chemically synthesized and tested for antiviral properties against EV-71 in human Rhabdomyosarcoma (RD) cells. One peptide, SP40, was found to significantly reduce cytopathic effects of all representative EV-71 strains from genotypes A, B and C tested, with IC<sub>50</sub> values ranging from 6–9.3 µM in RD cells. The <italic>in vitro</italic> inhibitory effect of SP40 exhibited a dose dependent concentration corresponding to a decrease in infectious viral particles, total viral RNA and the levels of VP1 protein. The antiviral activity of SP40 peptide was not restricted to a specific cell line as inhibition of EV-71 was observed in RD, HeLa, HT-29 and Vero cells. Besides inhibition of EV-71, it also had antiviral activities against CV-A16 and poliovirus type 1 in cell culture. Mechanism of action studies suggested that the SP40 peptide was not virucidal but was able to block viral attachment to the RD cells. Substitutions of arginine and lysine residues with alanine in the SP40 peptide at positions R3A, R4A, K5A and R13A were found to significantly decrease antiviral activities, implying the importance of positively charged amino acids for the antiviral activities. The data demonstrated the potential and feasibility of SP40 as a broad spectrum antiviral agent against EV-71.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Stanway, G" uniqKey="Stanway G">G Stanway</name></author><author><name sortKey="Brown, F" uniqKey="Brown F">F Brown</name></author><author><name sortKey="Christian, P" uniqKey="Christian P">P Christian</name></author><author><name sortKey="Hovi, T" uniqKey="Hovi T">T Hovi</name></author><author><name sortKey="Tyypia, T" uniqKey="Tyypia T">T Tyypia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brown, Ba" uniqKey="Brown B">BA Brown</name></author><author><name sortKey="Pallansch, Ma" uniqKey="Pallansch M">MA Pallansch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shindarov, Lm" uniqKey="Shindarov L">LM Shindarov</name></author><author><name sortKey="Chumakov, Mp" uniqKey="Chumakov M">MP 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last="Tan">Chee Wah Tan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Chan, Yoke Fun" sort="Chan, Yoke Fun" uniqKey="Chan Y" first="Yoke Fun" last="Chan">Yoke Fun Chan</name></author><author><name sortKey="Sim, Kooi Mow" sort="Sim, Kooi Mow" uniqKey="Sim K" first="Kooi Mow" last="Sim">Kooi Mow Sim</name></author><author><name sortKey="Tan, Eng Lee" sort="Tan, Eng Lee" uniqKey="Tan E" first="Eng Lee" last="Tan">Eng Lee Tan</name></author><author><name sortKey="Poh, Chit Laa" sort="Poh, Chit Laa" uniqKey="Poh C" first="Chit Laa" last="Poh">Chit Laa Poh</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22563456</idno><idno type="pmid">22563456</idno><idno type="doi">10.1371/journal.pone.0034589</idno><idno type="wicri:Area/PubMed/Corpus">001D82</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001D82</idno><idno type="wicri:Area/PubMed/Curation">001D82</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001D82</idno><idno type="wicri:Area/PubMed/Checkpoint">001C72</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001C72</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of enterovirus 71 (EV-71) infections by a novel antiviral peptide derived from EV-71 capsid protein VP1.</title><author><name sortKey="Tan, Chee Wah" sort="Tan, Chee Wah" uniqKey="Tan C" first="Chee Wah" last="Tan">Chee Wah Tan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>Department of Medical Microbiology, Faculty of Medicine, University of Malaya, Kuala Lumpur</wicri:regionArea><wicri:noRegion>Kuala Lumpur</wicri:noRegion></affiliation></author><author><name sortKey="Chan, Yoke Fun" sort="Chan, Yoke Fun" uniqKey="Chan Y" first="Yoke Fun" last="Chan">Yoke Fun Chan</name></author><author><name sortKey="Sim, Kooi Mow" sort="Sim, Kooi Mow" uniqKey="Sim K" first="Kooi Mow" last="Sim">Kooi Mow Sim</name></author><author><name sortKey="Tan, Eng Lee" sort="Tan, Eng Lee" uniqKey="Tan E" first="Eng Lee" last="Tan">Eng Lee Tan</name></author><author><name sortKey="Poh, Chit Laa" sort="Poh, Chit Laa" uniqKey="Poh C" first="Chit Laa" last="Poh">Chit Laa Poh</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012" 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Molecular</term><term>Molecular Sequence Data</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (genetics)</term><term>Oligopeptides (pharmacology)</term><term>Peptide Library</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alanine ()</term><term>Alanine (génétique)</term><term>Animaux</term><term>Antiviraux (pharmacologie)</term><term>Antiviraux (synthèse chimique)</term><term>Banque de peptides</term><term>Cellules HT29</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Concentration inhibitrice 50</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Entérovirus humain A ()</term><term>Entérovirus humain A (croissance et développement)</term><term>Entérovirus humain A (génétique)</term><term>Humains</term><term>Infections à entérovirus 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Proteins</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Entérovirus humain A</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Proliferation</term><term>Cell Survival</term><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Enterovirus A, Human</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alanine</term><term>Entérovirus humain A</term><term>Oligopeptides</term><term>Protéines de capside</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Enterovirus Infections</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Antiviraux</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à entérovirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Enterovirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line, Tumor</term><term>Chlorocebus aethiops</term><term>HT29 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptide Library</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alanine</term><term>Animaux</term><term>Banque de peptides</term><term>Cellules HT29</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Concentration inhibitrice 50</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Entérovirus humain A</term><term>Humains</term><term>Infections à entérovirus</term><term>Lignée cellulaire tumorale</term><term>Modèles moléculaires</term><term>Prolifération cellulaire</term><term>Protéines de capside</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Substitution d'acide aminé</term><term>Survie cellulaire</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Enterovirus 71 (EV-71) is the main causative agent of hand, foot and mouth disease (HFMD). In recent years, EV-71 infections were reported to cause high fatalities and severe neurological complications in Asia. Currently, no effective antiviral or vaccine is available to treat or prevent EV-71 infection. In this study, we have discovered a synthetic peptide which could be developed as a potential antiviral for inhibition of EV-71. Ninety five synthetic peptides (15-mers) overlapping the entire EV-71 capsid protein, VP1, were chemically synthesized and tested for antiviral properties against EV-71 in human Rhabdomyosarcoma (RD) cells. One peptide, SP40, was found to significantly reduce cytopathic effects of all representative EV-71 strains from genotypes A, B and C tested, with IC(50) values ranging from 6-9.3 µM in RD cells. The in vitro inhibitory effect of SP40 exhibited a dose dependent concentration corresponding to a decrease in infectious viral particles, total viral RNA and the levels of VP1 protein. The antiviral activity of SP40 peptide was not restricted to a specific cell line as inhibition of EV-71 was observed in RD, HeLa, HT-29 and Vero cells. Besides inhibition of EV-71, it also had antiviral activities against CV-A16 and poliovirus type 1 in cell culture. Mechanism of action studies suggested that the SP40 peptide was not virucidal but was able to block viral attachment to the RD cells. Substitutions of arginine and lysine residues with alanine in the SP40 peptide at positions R3A, R4A, K5A and R13A were found to significantly decrease antiviral activities, implying the importance of positively charged amino acids for the antiviral activities. The data demonstrated the potential and feasibility of SP40 as a broad spectrum antiviral agent against EV-71.</div></front></TEI></pubmed></double></record>Pour manipuler ce document sous Unix (Dilib)
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