The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design
Identifieur interne : 000041 ( Pmc/Checkpoint ); précédent : 000040; suivant : 000042The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design
Auteurs : Larissa Dirr [Australie] ; Ibrahim M. El-Deeb [Australie] ; Leonard M. G. Chavas [France] ; Patrice Guillon [Australie] ; Mark Von Itzstein [Australie]Source :
- Scientific Reports [ 2045-2322 ] ; 2017.
Abstract
Human parainfluenza viruses represent a leading cause of lower respiratory tract disease in children, with currently no available approved drug or vaccine. The viral surface glycoprotein haemagglutinin-neuraminidase (HN) represents an ideal antiviral target. Herein, we describe the first structure-based study on the rearrangement of key active site amino acid residues by an induced opening of the 216-loop, through the accommodation of appropriately functionalised neuraminic acid-based inhibitors. We discovered that the rearrangement is influenced by the degree of loop opening and is controlled by the neuraminic acid’s C-4 substituent’s size (large or small). In this study, we found that these rearrangements induce a butterfly effect of paramount importance in HN inhibitor design and define criteria for the ideal substituent size in two different categories of HN inhibitors and provide novel structural insight into the druggable viral HN protein.
Url:
DOI: 10.1038/s41598-017-04656-y
PubMed: 28674426
PubMed Central: 5495814
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El-Deeb</name><affiliation wicri:level="1"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0437 5432</institution-id><institution-id institution-id-type="GRID">grid.1022.1</institution-id><institution>Institute for Glycomics,</institution><institution>Griffith University,</institution></institution-wrap>Gold Coast Campus, Queensland, 4222 Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Gold Coast Campus, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Chavas, Leonard M G" sort="Chavas, Leonard M G" uniqKey="Chavas L" first="Leonard M. G." last="Chavas">Leonard M. G. Chavas</name><affiliation wicri:level="1"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.426328.9</institution-id><institution>Experiments division,</institution><institution>Synchrotron SOLEIL,</institution></institution-wrap>Gif-sur-Yvette, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Guillon, Patrice" sort="Guillon, Patrice" uniqKey="Guillon P" first="Patrice" last="Guillon">Patrice Guillon</name><affiliation wicri:level="1"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0437 5432</institution-id><institution-id institution-id-type="GRID">grid.1022.1</institution-id><institution>Institute for Glycomics,</institution><institution>Griffith University,</institution></institution-wrap>Gold Coast Campus, Queensland, 4222 Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Gold Coast Campus, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Itzstein, Mark Von" sort="Itzstein, Mark Von" uniqKey="Itzstein M" first="Mark Von" last="Itzstein">Mark Von Itzstein</name><affiliation wicri:level="1"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0437 5432</institution-id><institution-id institution-id-type="GRID">grid.1022.1</institution-id><institution>Institute for Glycomics,</institution><institution>Griffith University,</institution></institution-wrap>Gold Coast Campus, Queensland, 4222 Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Gold Coast Campus, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author></analytic><series><title level="j">Scientific Reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="Par1">Human parainfluenza viruses represent a leading cause of lower respiratory tract disease in children, with currently no available approved drug or vaccine. The viral surface glycoprotein haemagglutinin-neuraminidase (HN) represents an ideal antiviral target. Herein, we describe the first structure-based study on the rearrangement of key active site amino acid residues by an induced opening of the 216-loop, through the accommodation of appropriately functionalised neuraminic acid-based inhibitors. We discovered that the rearrangement is influenced by the degree of loop opening and is controlled by the neuraminic acid’s C-4 substituent’s size (large or small). In this study, we found that these rearrangements induce a butterfly effect of paramount importance in HN inhibitor design and define criteria for the ideal substituent size in two different categories of HN inhibitors and provide novel structural insight into the druggable viral HN protein.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Steffens, A" uniqKey="Steffens A">A Steffens</name></author><author><name sortKey="Finelli, L" uniqKey="Finelli L">L Finelli</name></author><author><name sortKey="Whitaker, B" uniqKey="Whitaker B">B Whitaker</name></author><author><name sortKey="Fowlkes, A" uniqKey="Fowlkes A">A Fowlkes</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Abedi, Gr" uniqKey="Abedi G">GR Abedi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Henrickson, Kj" uniqKey="Henrickson K">KJ 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Sci Rep</journal-id><journal-id journal-id-type="iso-abbrev">Sci Rep</journal-id><journal-title-group><journal-title>Scientific Reports</journal-title></journal-title-group><issn pub-type="epub">2045-2322</issn><publisher><publisher-name>Nature Publishing Group UK</publisher-name><publisher-loc>London</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">28674426</article-id><article-id pub-id-type="pmc">5495814</article-id><article-id pub-id-type="publisher-id">4656</article-id><article-id pub-id-type="doi">10.1038/s41598-017-04656-y</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Dirr</surname><given-names>Larissa</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>El-Deeb</surname><given-names>Ibrahim M.</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Chavas</surname><given-names>Leonard M. G.</given-names></name><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author"><name><surname>Guillon</surname><given-names>Patrice</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">http://orcid.org/0000-0001-6302-7524</contrib-id><name><surname>Itzstein</surname><given-names>Mark von</given-names></name><address><email>m.vonitzstein@griffith.edu.au</email></address><xref ref-type="aff" rid="Aff1">1</xref></contrib><aff id="Aff1"><label>1</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0437 5432</institution-id><institution-id institution-id-type="GRID">grid.1022.1</institution-id><institution>Institute for Glycomics,</institution><institution>Griffith University,</institution></institution-wrap>Gold Coast Campus, Queensland, 4222 Australia</aff><aff id="Aff2"><label>2</label><institution-wrap><institution-id institution-id-type="GRID">grid.426328.9</institution-id><institution>Experiments division,</institution><institution>Synchrotron SOLEIL,</institution></institution-wrap>Gif-sur-Yvette, France</aff></contrib-group><pub-date pub-type="epub"><day>3</day><month>7</month><year>2017</year></pub-date><pub-date pub-type="pmc-release"><day>3</day><month>7</month><year>2017</year></pub-date><pub-date pub-type="collection"><year>2017</year></pub-date><volume>7</volume><elocation-id>4507</elocation-id><history><date date-type="received"><day>16</day><month>12</month><year>2016</year></date><date date-type="accepted"><day>23</day><month>5</month><year>2017</year></date></history><permissions><copyright-statement>© The Author(s) 2017</copyright-statement><license license-type="OpenAccess"><license-p><bold>Open Access</bold> This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>.</license-p></license></permissions><abstract id="Abs1"><p id="Par1">Human parainfluenza viruses represent a leading cause of lower respiratory tract disease in children, with currently no available approved drug or vaccine. The viral surface glycoprotein haemagglutinin-neuraminidase (HN) represents an ideal antiviral target. Herein, we describe the first structure-based study on the rearrangement of key active site amino acid residues by an induced opening of the 216-loop, through the accommodation of appropriately functionalised neuraminic acid-based inhibitors. We discovered that the rearrangement is influenced by the degree of loop opening and is controlled by the neuraminic acid’s C-4 substituent’s size (large or small). In this study, we found that these rearrangements induce a butterfly effect of paramount importance in HN inhibitor design and define criteria for the ideal substituent size in two different categories of HN inhibitors and provide novel structural insight into the druggable viral HN protein.</p></abstract><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© The Author(s) 2017</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc><affiliations><list><country><li>Australie</li><li>France</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Dirr, Larissa" sort="Dirr, Larissa" uniqKey="Dirr L" first="Larissa" last="Dirr">Larissa Dirr</name></noRegion><name sortKey="El Deeb, Ibrahim M" sort="El Deeb, Ibrahim M" uniqKey="El Deeb I" first="Ibrahim M." last="El-Deeb">Ibrahim M. El-Deeb</name><name sortKey="Guillon, Patrice" sort="Guillon, Patrice" uniqKey="Guillon P" first="Patrice" last="Guillon">Patrice Guillon</name><name sortKey="Itzstein, Mark Von" sort="Itzstein, Mark Von" uniqKey="Itzstein M" first="Mark Von" last="Itzstein">Mark Von Itzstein</name></country><country name="France"><noRegion><name sortKey="Chavas, Leonard M G" sort="Chavas, Leonard M G" uniqKey="Chavas L" first="Leonard M. G." last="Chavas">Leonard M. G. Chavas</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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