Antiviral activity of stachyflin on influenza A viruses of different hemagglutinin subtypes
Identifieur interne : 000914 ( Main/Exploration ); précédent : 000913; suivant : 000915Antiviral activity of stachyflin on influenza A viruses of different hemagglutinin subtypes
Auteurs : Yurie Motohashi [Japon] ; Manabu Igarashi [Japon] ; Masatoshi Okamatsu [Japon] ; Takeshi Noshi [Japon] ; Yoshihiro Sakoda [Japon] ; Naoki Yamamoto [Japon] ; Kimihito Ito [Japon] ; Ryu Yoshida [Japon] ; Hiroshi Kida [Japon]Source :
- Virology Journal [ 1743-422X ] ; 2013.
Abstract
The hemagglutinin (HA) of influenza viruses is a possible target for antiviral drugs because of its key roles in the initiation of infection. Although it was found that a natural compound, Stachyflin, inhibited the growth of H1 and H2 but not H3 influenza viruses in MDCK cells, inhibitory activity of the compound has not been assessed against H4-H16 influenza viruses and the precise mechanism of inhibition has not been clarified.
Inhibitory activity of Stachyflin against H4-H16 influenza viruses, as well as H1-H3 viruses was examined in MDCK cells. To identify factors responsible for the susceptibility of the viruses to this compound, Stachyflin-resistant viruses were selected in MDCK cells and used for computer docking simulation.
It was found that in addition to antiviral activity of Stachyflin against influenza viruses of H1 and H2 subtypes, it inhibited replication of viruses of H5 and H6 subtypes, as well as A(H1N1)pdm09 virus in MDCK cells. Stachyflin also inhibited the virus growth in the lungs of mice infected with A/WSN/1933 (H1N1) and A/chicken/Ibaraki/1/2005 (H5N2). Substitution of amino acid residues was found on the HA2 subunit of Stachyflin-resistant viruses. Docking simulation indicated that D37, K51, T107, and K121 are responsible for construction of the cavity for the binding of the compound. In addition, 3-dimensional structure of the cavity of the HA of Stachyflin-susceptible virus strains was different from that of insusceptible virus strains.
Antiviral activity of Stachyflin was found against A(H1N1)pdm09, H5, and H6 viruses, and identified a potential binding pocket for Stachyflin on the HA. The present results should provide us with useful information for the development of HA inhibitors with more effective and broader spectrum.
Url:
DOI: 10.1186/1743-422X-10-118
PubMed: 23587221
PubMed Central: 3648499
Affiliations:
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Kida</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I2">Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020</wicri:regionArea><wicri:noRegion>Sapporo 001-0020</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno 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type="wicri:Area/Main/Exploration">000914</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Antiviral activity of stachyflin on influenza A viruses of different hemagglutinin subtypes</title><author><name sortKey="Motohashi, Yurie" sort="Motohashi, Yurie" uniqKey="Motohashi Y" first="Yurie" last="Motohashi">Yurie Motohashi</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation></author><author><name sortKey="Igarashi, Manabu" sort="Igarashi, Manabu" uniqKey="Igarashi M" first="Manabu" last="Igarashi">Manabu Igarashi</name><affiliation wicri:level="1"><nlm:aff id="I2">Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020</wicri:regionArea><wicri:noRegion>Sapporo 001-0020</wicri:noRegion></affiliation></author><author><name sortKey="Okamatsu, Masatoshi" sort="Okamatsu, Masatoshi" uniqKey="Okamatsu M" first="Masatoshi" last="Okamatsu">Masatoshi Okamatsu</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation></author><author><name sortKey="Noshi, Takeshi" sort="Noshi, Takeshi" uniqKey="Noshi T" first="Takeshi" last="Noshi">Takeshi Noshi</name><affiliation wicri:level="1"><nlm:aff id="I3">Discovery Research Laboratories, Shionogi & Co., Ltd., Settsu, Osaka 566-0022, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Discovery Research Laboratories, Shionogi & Co., Ltd., Settsu, Osaka 566-0022</wicri:regionArea><wicri:noRegion>Osaka 566-0022</wicri:noRegion></affiliation></author><author><name sortKey="Sakoda, Yoshihiro" sort="Sakoda, Yoshihiro" uniqKey="Sakoda Y" first="Yoshihiro" last="Sakoda">Yoshihiro Sakoda</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation></author><author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation></author><author><name sortKey="Ito, Kimihito" sort="Ito, Kimihito" uniqKey="Ito K" first="Kimihito" last="Ito">Kimihito Ito</name><affiliation wicri:level="1"><nlm:aff id="I2">Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020</wicri:regionArea><wicri:noRegion>Sapporo 001-0020</wicri:noRegion></affiliation></author><author><name sortKey="Yoshida, Ryu" sort="Yoshida, Ryu" uniqKey="Yoshida R" first="Ryu" last="Yoshida">Ryu Yoshida</name><affiliation wicri:level="1"><nlm:aff id="I3">Discovery Research Laboratories, Shionogi & Co., Ltd., Settsu, Osaka 566-0022, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Discovery Research Laboratories, Shionogi & Co., Ltd., Settsu, Osaka 566-0022</wicri:regionArea><wicri:noRegion>Osaka 566-0022</wicri:noRegion></affiliation></author><author><name sortKey="Kida, Hiroshi" sort="Kida, Hiroshi" uniqKey="Kida H" first="Hiroshi" last="Kida">Hiroshi Kida</name><affiliation wicri:level="1"><nlm:aff id="I1">Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Disease Control, Laboratory of Microbiology, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18 Nishi-9, Sapporo 060-0818</wicri:regionArea><wicri:noRegion>Sapporo 060-0818</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I2">Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Bioinformatics, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020</wicri:regionArea><wicri:noRegion>Sapporo 001-0020</wicri:noRegion></affiliation></author></analytic><series><title level="j">Virology Journal</title><idno type="eISSN">1743-422X</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>The hemagglutinin (HA) of influenza viruses is a possible target for antiviral drugs because of its key roles in the initiation of infection. Although it was found that a natural compound, Stachyflin, inhibited the growth of H1 and H2 but not H3 influenza viruses in MDCK cells, inhibitory activity of the compound has not been assessed against H4-H16 influenza viruses and the precise mechanism of inhibition has not been clarified.</p></sec><sec><title>Methods</title><p>Inhibitory activity of Stachyflin against H4-H16 influenza viruses, as well as H1-H3 viruses was examined in MDCK cells. To identify factors responsible for the susceptibility of the viruses to this compound, Stachyflin-resistant viruses were selected in MDCK cells and used for computer docking simulation.</p></sec><sec><title>Results</title><p>It was found that in addition to antiviral activity of Stachyflin against influenza viruses of H1 and H2 subtypes, it inhibited replication of viruses of H5 and H6 subtypes, as well as A(H1N1)pdm09 virus in MDCK cells. Stachyflin also inhibited the virus growth in the lungs of mice infected with A/WSN/1933 (H1N1) and A/chicken/Ibaraki/1/2005 (H5N2). Substitution of amino acid residues was found on the HA2 subunit of Stachyflin-resistant viruses. Docking simulation indicated that D37, K51, T107, and K121 are responsible for construction of the cavity for the binding of the compound. In addition, 3-dimensional structure of the cavity of the HA of Stachyflin-susceptible virus strains was different from that of insusceptible virus strains.</p></sec><sec><title>Conclusion</title><p>Antiviral activity of Stachyflin was found against A(H1N1)pdm09, H5, and H6 viruses, and identified a potential binding pocket for Stachyflin on the HA. The present results should provide us with useful information for the development of HA inhibitors with more effective and broader spectrum.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Hay, Aj" uniqKey="Hay A">AJ Hay</name></author><author><name sortKey="Wolstenholme, Aj" uniqKey="Wolstenholme A">AJ Wolstenholme</name></author><author><name sortKey="Skehel, Jj" uniqKey="Skehel J">JJ Skehel</name></author><author><name sortKey="Smith, Mh" uniqKey="Smith M">MH Smith</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Moscona, A" uniqKey="Moscona A">A Moscona</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pinto, Lh" uniqKey="Pinto L">LH Pinto</name></author><author><name sortKey="Holsinger, Lj" uniqKey="Holsinger L">LJ Holsinger</name></author><author><name sortKey="Lamb, Ra" uniqKey="Lamb R">RA 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uniqKey="Bowie J">JU Bowie</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Thomsen, R" uniqKey="Thomsen R">R Thomsen</name></author><author><name sortKey="Christensen, Mh" uniqKey="Christensen M">MH Christensen</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Motohashi, Yurie" sort="Motohashi, Yurie" uniqKey="Motohashi Y" first="Yurie" last="Motohashi">Yurie Motohashi</name></noRegion><name sortKey="Igarashi, Manabu" sort="Igarashi, Manabu" uniqKey="Igarashi M" first="Manabu" last="Igarashi">Manabu Igarashi</name><name sortKey="Ito, Kimihito" sort="Ito, Kimihito" uniqKey="Ito K" first="Kimihito" last="Ito">Kimihito Ito</name><name sortKey="Kida, Hiroshi" sort="Kida, Hiroshi" uniqKey="Kida H" first="Hiroshi" last="Kida">Hiroshi Kida</name><name sortKey="Kida, Hiroshi" sort="Kida, Hiroshi" uniqKey="Kida H" first="Hiroshi" last="Kida">Hiroshi Kida</name><name sortKey="Noshi, Takeshi" sort="Noshi, Takeshi" uniqKey="Noshi T" first="Takeshi" last="Noshi">Takeshi Noshi</name><name sortKey="Okamatsu, Masatoshi" sort="Okamatsu, Masatoshi" uniqKey="Okamatsu M" first="Masatoshi" last="Okamatsu">Masatoshi Okamatsu</name><name sortKey="Sakoda, Yoshihiro" sort="Sakoda, Yoshihiro" uniqKey="Sakoda Y" first="Yoshihiro" last="Sakoda">Yoshihiro Sakoda</name><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name><name sortKey="Yoshida, Ryu" sort="Yoshida, Ryu" uniqKey="Yoshida R" first="Ryu" last="Yoshida">Ryu Yoshida</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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