The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design.
Identifieur interne : 000883 ( PubMed/Curation ); précédent : 000882; suivant : 000884The 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.
DOI: 10.1038/s41598-017-04656-y
PubMed: 28674426
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El-Deeb</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222</wicri:regionArea></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:affiliation>Experiments division, Synchrotron SOLEIL, Gif-sur-Yvette, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Experiments division, Synchrotron SOLEIL, 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:affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222</wicri:regionArea></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:affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222, Australia. m.vonitzstein@griffith.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222</wicri:regionArea></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">28674426</PMID><DateCreated><Year>2017</Year><Month>07</Month><Day>04</Day></DateCreated><DateRevised><Year>2017</Year><Month>07</Month><Day>14</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Jul</Month><Day>03</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design.</ArticleTitle><Pagination><MedlinePgn>4507</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-017-04656-y</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dirr</LastName><ForeName>Larissa</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>El-Deeb</LastName><ForeName>Ibrahim M</ForeName><Initials>IM</Initials><AffiliationInfo><Affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland, 4222, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chavas</LastName><ForeName>Leonard M 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DateType="Electronic"><Year>2017</Year><Month>07</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Anal Biochem. 1979 Apr 15;94(2):287-96</RefSource><PMID Version="1">464297</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Antimicrob Agents Chemother. 2004 May;48(5):1495-502</RefSource><PMID Version="1">15105096</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Synchrotron Radiat. 2012 May;19(Pt 3):450-4</RefSource><PMID Version="1">22514184</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2006 Feb 17;281(7):4149-55</RefSource><PMID Version="1">16298994</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proteins. 1992 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