Hemagglutinin-neuraminidase balance confers respiratory-droplet transmissibility of the pandemic H1N1 influenza virus in ferrets.
Identifieur interne : 000F36 ( PubMed/Curation ); précédent : 000F35; suivant : 000F37Hemagglutinin-neuraminidase balance confers respiratory-droplet transmissibility of the pandemic H1N1 influenza virus in ferrets.
Auteurs : Hui-Ling Yen [République populaire de Chine] ; Chi-Hui Liang ; Chung-Yi Wu ; Heather L. Forrest ; Angela Ferguson ; Ka-Tim Choy ; Jeremy Jones ; Diana Dik-Yan Wong ; Peter Pak-Hang Cheung ; Che-Hsiung Hsu ; Olive T. Li ; Kit M. Yuen ; Renee W Y. Chan ; Leo L M. Poon ; Michael C W. Chan ; John M. Nicholls ; Scott Krauss ; Chi-Huey Wong ; Yi Guan ; Robert G. Webster ; Richard J. Webby ; Malik PeirisSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Appareil respiratoire (anatomopathologie), Appareil respiratoire (virologie), Cinétique, Furets (virologie), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Génome viral (génétique), Infections à Orthomyxoviridae (transmission), Infections à Orthomyxoviridae (virologie), Infections à Orthomyxoviridae (épidémiologie), Liaison aux protéines, Pandémies, Polyosides (métabolisme), Recombinaison génétique (génétique), Récepteurs viraux (métabolisme), Réplication virale (physiologie), Saisons, Sialidase (métabolisme), Sous-type H1N1 du virus de la grippe A (enzymologie), Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H1N1 du virus de la grippe A (physiologie), Spécificité du substrat, Suidae, Tropisme.
- MESH :
- anatomopathologie : Appareil respiratoire.
- enzymologie : Sous-type H1N1 du virus de la grippe A.
- génétique : Génome viral, Recombinaison génétique, Sous-type H1N1 du virus de la grippe A.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Polyosides, Récepteurs viraux, Sialidase.
- physiologie : Réplication virale, Sous-type H1N1 du virus de la grippe A.
- virologie : Appareil respiratoire, Furets, Infections à Orthomyxoviridae.
- épidémiologie : Infections à Orthomyxoviridae.
- Animaux, Cinétique, Liaison aux protéines, Pandémies, Saisons, Spécificité du substrat, Suidae, Tropisme.
English descriptors
- KwdEn :
- Animals, Ferrets (virology), Genome, Viral (genetics), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Influenza A Virus, H1N1 Subtype (enzymology), Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (physiology), Kinetics, Neuraminidase (metabolism), Orthomyxoviridae Infections (epidemiology), Orthomyxoviridae Infections (transmission), Orthomyxoviridae Infections (virology), Pandemics, Polysaccharides (metabolism), Protein Binding, Receptors, Virus (metabolism), Recombination, Genetic (genetics), Respiratory System (pathology), Respiratory System (virology), Seasons, Substrate Specificity, Swine, Tropism, Virus Replication (physiology).
- MESH :
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Neuraminidase, Polysaccharides, Receptors, Virus.
- enzymology : Influenza A Virus, H1N1 Subtype.
- epidemiology : Orthomyxoviridae Infections.
- genetics : Genome, Viral, Influenza A Virus, H1N1 Subtype, Recombination, Genetic.
- pathology : Respiratory System.
- physiology : Influenza A Virus, H1N1 Subtype, Virus Replication.
- transmission : Orthomyxoviridae Infections.
- virology : Ferrets, Orthomyxoviridae Infections, Respiratory System.
- Animals, Kinetics, Pandemics, Protein Binding, Seasons, Substrate Specificity, Swine, Tropism.
Abstract
A novel reassortant derived from North American triple-reassortant (TRsw) and Eurasian swine (EAsw) influenza viruses acquired sustained human-to-human transmissibility and caused the 2009 influenza pandemic. To identify molecular determinants that allowed efficient transmission of the pandemic H1N1 virus among humans, we evaluated the direct-contact and respiratory-droplet transmissibility in ferrets of representative swine influenza viruses of different lineages obtained through a 13-y surveillance program in southern China. Whereas all viruses studied were transmitted by direct contact with varying efficiency, respiratory-droplet transmissibility (albeit inefficient) was observed only in the TRsw-like A/swine/Hong Kong/915/04 (sw915) (H1N2) virus. The sw915 virus had acquired the M gene derived from EAsw and differed from the gene constellation of the pandemic H1N1 virus by the neuraminidase (NA) gene alone. Glycan array analysis showed that pandemic H1N1 virus A/HK/415742/09 (HK415742) and sw915 possess similar receptor-binding specificity and affinity for α2,6-linked sialosides. Sw915 titers in differentiated normal human bronchial epithelial cells and in ferret nasal washes were lower than those of HK415742. Introducing the NA from pandemic HK415742 into sw915 did not increase viral replication efficiency but increased respiratory-droplet transmissibility, despite a substantial amino acid difference between the two viruses. The NA of the pandemic HK415742 virus possessed significantly higher enzyme activity than that of sw915 or other swine influenza viruses. Our results suggest that a unique gene constellation and hemagglutinin-neuraminidase balance play a critical role in acquisition of efficient and sustained human-to-human transmissibility.
DOI: 10.1073/pnas.1111000108
PubMed: 21825167
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(transmission)</term><term>Orthomyxoviridae Infections (virology)</term><term>Pandemics</term><term>Polysaccharides (metabolism)</term><term>Protein Binding</term><term>Receptors, Virus (metabolism)</term><term>Recombination, Genetic (genetics)</term><term>Respiratory System (pathology)</term><term>Respiratory System (virology)</term><term>Seasons</term><term>Substrate Specificity</term><term>Swine</term><term>Tropism</term><term>Virus Replication (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Appareil respiratoire (anatomopathologie)</term><term>Appareil respiratoire (virologie)</term><term>Cinétique</term><term>Furets (virologie)</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Génome viral (génétique)</term><term>Infections à Orthomyxoviridae (transmission)</term><term>Infections à Orthomyxoviridae (virologie)</term><term>Infections à Orthomyxoviridae (épidémiologie)</term><term>Liaison aux protéines</term><term>Pandémies</term><term>Polyosides (métabolisme)</term><term>Recombinaison génétique (génétique)</term><term>Récepteurs viraux (métabolisme)</term><term>Réplication virale (physiologie)</term><term>Saisons</term><term>Sialidase (métabolisme)</term><term>Sous-type H1N1 du virus de la grippe A (enzymologie)</term><term>Sous-type H1N1 du virus de la grippe A (génétique)</term><term>Sous-type H1N1 du virus de la grippe A (physiologie)</term><term>Spécificité du substrat</term><term>Suidae</term><term>Tropisme</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Neuraminidase</term><term>Polysaccharides</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Appareil respiratoire</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Genome, Viral</term><term>Influenza A Virus, H1N1 Subtype</term><term>Recombination, Genetic</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Génome viral</term><term>Recombinaison génétique</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Polyosides</term><term>Récepteurs viraux</term><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Respiratory System</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Réplication virale</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="transmission" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Appareil respiratoire</term><term>Furets</term><term>Infections à Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Ferrets</term><term>Orthomyxoviridae Infections</term><term>Respiratory System</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Infections à Orthomyxoviridae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Kinetics</term><term>Pandemics</term><term>Protein Binding</term><term>Seasons</term><term>Substrate Specificity</term><term>Swine</term><term>Tropism</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cinétique</term><term>Liaison aux protéines</term><term>Pandémies</term><term>Saisons</term><term>Spécificité du substrat</term><term>Suidae</term><term>Tropisme</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A novel reassortant derived from North American triple-reassortant (TRsw) and Eurasian swine (EAsw) influenza viruses acquired sustained human-to-human transmissibility and caused the 2009 influenza pandemic. To identify molecular determinants that allowed efficient transmission of the pandemic H1N1 virus among humans, we evaluated the direct-contact and respiratory-droplet transmissibility in ferrets of representative swine influenza viruses of different lineages obtained through a 13-y surveillance program in southern China. Whereas all viruses studied were transmitted by direct contact with varying efficiency, respiratory-droplet transmissibility (albeit inefficient) was observed only in the TRsw-like A/swine/Hong Kong/915/04 (sw915) (H1N2) virus. The sw915 virus had acquired the M gene derived from EAsw and differed from the gene constellation of the pandemic H1N1 virus by the neuraminidase (NA) gene alone. Glycan array analysis showed that pandemic H1N1 virus A/HK/415742/09 (HK415742) and sw915 possess similar receptor-binding specificity and affinity for α2,6-linked sialosides. Sw915 titers in differentiated normal human bronchial epithelial cells and in ferret nasal washes were lower than those of HK415742. Introducing the NA from pandemic HK415742 into sw915 did not increase viral replication efficiency but increased respiratory-droplet transmissibility, despite a substantial amino acid difference between the two viruses. The NA of the pandemic HK415742 virus possessed significantly higher enzyme activity than that of sw915 or other swine influenza viruses. Our results suggest that a unique gene constellation and hemagglutinin-neuraminidase balance play a critical role in acquisition of efficient and sustained human-to-human transmissibility.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21825167</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>108</Volume><Issue>34</Issue><PubDate><Year>2011</Year><Month>Aug</Month><Day>23</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Hemagglutinin-neuraminidase balance confers respiratory-droplet transmissibility of the pandemic H1N1 influenza virus in ferrets.</ArticleTitle><Pagination><MedlinePgn>14264-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1111000108</ELocationID><Abstract><AbstractText>A novel reassortant derived from North American triple-reassortant (TRsw) and Eurasian swine (EAsw) influenza viruses acquired sustained human-to-human transmissibility and caused the 2009 influenza pandemic. To identify molecular determinants that allowed efficient transmission of the pandemic H1N1 virus among humans, we evaluated the direct-contact and respiratory-droplet transmissibility in ferrets of representative swine influenza viruses of different lineages obtained through a 13-y surveillance program in southern China. Whereas all viruses studied were transmitted by direct contact with varying efficiency, respiratory-droplet transmissibility (albeit inefficient) was observed only in the TRsw-like A/swine/Hong Kong/915/04 (sw915) (H1N2) virus. The sw915 virus had acquired the M gene derived from EAsw and differed from the gene constellation of the pandemic H1N1 virus by the neuraminidase (NA) gene alone. Glycan array analysis showed that pandemic H1N1 virus A/HK/415742/09 (HK415742) and sw915 possess similar receptor-binding specificity and affinity for α2,6-linked sialosides. Sw915 titers in differentiated normal human bronchial epithelial cells and in ferret nasal washes were lower than those of HK415742. Introducing the NA from pandemic HK415742 into sw915 did not increase viral replication efficiency but increased respiratory-droplet transmissibility, despite a substantial amino acid difference between the two viruses. The NA of the pandemic HK415742 virus possessed significantly higher enzyme activity than that of sw915 or other swine influenza viruses. Our results suggest that a unique gene constellation and hemagglutinin-neuraminidase balance play a critical role in acquisition of efficient and sustained human-to-human transmissibility.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yen</LastName><ForeName>Hui-Ling</ForeName><Initials>HL</Initials><AffiliationInfo><Affiliation>Department of Microbiology, HKU-Pasteur Research Centre, University of Hong Kong, Pokfulam, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liang</LastName><ForeName>Chi-Hui</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Chung-Yi</ForeName><Initials>CY</Initials></Author><Author ValidYN="Y"><LastName>Forrest</LastName><ForeName>Heather L</ForeName><Initials>HL</Initials></Author><Author ValidYN="Y"><LastName>Ferguson</LastName><ForeName>Angela</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Choy</LastName><ForeName>Ka-Tim</ForeName><Initials>KT</Initials></Author><Author ValidYN="Y"><LastName>Jones</LastName><ForeName>Jeremy</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Diana Dik-Yan</ForeName><Initials>DD</Initials></Author><Author ValidYN="Y"><LastName>Cheung</LastName><ForeName>Peter Pak-Hang</ForeName><Initials>PP</Initials></Author><Author ValidYN="Y"><LastName>Hsu</LastName><ForeName>Che-Hsiung</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Olive T</ForeName><Initials>OT</Initials></Author><Author ValidYN="Y"><LastName>Yuen</LastName><ForeName>Kit M</ForeName><Initials>KM</Initials></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>Renee W Y</ForeName><Initials>RW</Initials></Author><Author ValidYN="Y"><LastName>Poon</LastName><ForeName>Leo L M</ForeName><Initials>LL</Initials></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>Michael C W</ForeName><Initials>MC</Initials></Author><Author ValidYN="Y"><LastName>Nicholls</LastName><ForeName>John M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Krauss</LastName><ForeName>Scott</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Chi-Huey</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Guan</LastName><ForeName>Yi</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Webster</LastName><ForeName>Robert G</ForeName><Initials>RG</Initials></Author><Author ValidYN="Y"><LastName>Webby</LastName><ForeName>Richard J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Peiris</LastName><ForeName>Malik</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>HHSN266200700005C</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HHSN266200700005C</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>08</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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