Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets.
Identifieur interne : 000083 ( PubMed/Corpus ); précédent : 000082; suivant : 000084Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets.
Auteurs : Claudia Pappas ; Hua Yang ; Paul J. Carney ; Melissa B. Pearce ; Jacqueline M. Katz ; James Stevens ; Terrence M. TumpeySource :
- Virology [ 1096-0341 ] ; 2015.
English descriptors
- KwdEn :
- Adaptation, Biological, Animals, Birds, Crystallography, X-Ray, Disease Models, Animal, Ferrets, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Humans, Influenza A virus (genetics), Influenza A virus (isolation & purification), Influenza A virus (pathogenicity), Influenza A virus (physiology), Microarray Analysis, Mutant Proteins (genetics), Mutation, Missense, Orthomyxoviridae Infections (pathology), Orthomyxoviridae Infections (transmission), Orthomyxoviridae Infections (virology), Polysaccharides (analysis), Protein Binding, Swine, Virulence, Virus Attachment.
- MESH :
- chemical , analysis : Polysaccharides.
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus, Mutant Proteins.
- genetics : Influenza A virus.
- isolation & purification : Influenza A virus.
- pathogenicity : Influenza A virus.
- pathology : Orthomyxoviridae Infections.
- physiology : Influenza A virus.
- transmission : Orthomyxoviridae Infections.
- virology : Orthomyxoviridae Infections.
- Adaptation, Biological, Animals, Birds, Crystallography, X-Ray, Disease Models, Animal, Ferrets, Humans, Microarray Analysis, Mutation, Missense, Protein Binding, Swine, Virulence, Virus Attachment.
Abstract
After their disappearance from the human population in 1968, influenza H2 viruses have continued to circulate in the natural avian reservoir. The isolation of this virus subtype from multiple bird species as well as swine highlights the need to better understand the potential of these viruses to spread and cause disease in humans. Here we analyzed the virulence, transmissibility and receptor-binding preference of two avian influenza H2 viruses (H2N2 and H2N3) and compared them to a swine H2N3 (A/swine/Missouri/2124514/2006 [swMO]), and a human H2N2 (A/England/10/1967 [Eng/67]) virus using the ferret model as a mammalian host. Both avian H2 viruses possessed the capacity to spread efficiently between cohoused ferrets, and the swine (swMO) and human (Eng/67) viruses transmitted to naïve ferrets by respiratory droplets. Further characterization of the swMO hemagglutinin (HA) by x-ray crystallography and glycan microarray array identified receptor-specific adaptive mutations. As influenza virus quasispecies dynamics during transmission have not been well characterized, we sequenced nasal washes collected during transmission studies to better understand experimental adaptation of H2 HA. The avian H2 viruses isolated from ferret nasal washes contained mutations in the HA1, including a Gln226Leu substitution, which is a mutation associated with α2,6 sialic acid (human-like) binding preference. These results suggest that the molecular structure of HA in viruses of the H2 subtype continue to have the potential to adapt to a mammalian host and become transmissible, after acquiring additional genetic markers.
DOI: 10.1016/j.virol.2015.01.002
PubMed: 25659818
Links to Exploration step
pubmed:25659818Le document en format XML
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The isolation of this virus subtype from multiple bird species as well as swine highlights the need to better understand the potential of these viruses to spread and cause disease in humans. Here we analyzed the virulence, transmissibility and receptor-binding preference of two avian influenza H2 viruses (H2N2 and H2N3) and compared them to a swine H2N3 (A/swine/Missouri/2124514/2006 [swMO]), and a human H2N2 (A/England/10/1967 [Eng/67]) virus using the ferret model as a mammalian host. Both avian H2 viruses possessed the capacity to spread efficiently between cohoused ferrets, and the swine (swMO) and human (Eng/67) viruses transmitted to naïve ferrets by respiratory droplets. Further characterization of the swMO hemagglutinin (HA) by x-ray crystallography and glycan microarray array identified receptor-specific adaptive mutations. As influenza virus quasispecies dynamics during transmission have not been well characterized, we sequenced nasal washes collected during transmission studies to better understand experimental adaptation of H2 HA. The avian H2 viruses isolated from ferret nasal washes contained mutations in the HA1, including a Gln226Leu substitution, which is a mutation associated with α2,6 sialic acid (human-like) binding preference. These results suggest that the molecular structure of HA in viruses of the H2 subtype continue to have the potential to adapt to a mammalian host and become transmissible, after acquiring additional genetic markers.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25659818</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>14</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN><JournalIssue CitedMedium="Internet"><Volume>477</Volume><PubDate><Year>2015</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets.</ArticleTitle><Pagination><MedlinePgn>61-71</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0042-6822(15)00003-3</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2015.01.002</ELocationID><Abstract><AbstractText>After their disappearance from the human population in 1968, influenza H2 viruses have continued to circulate in the natural avian reservoir. The isolation of this virus subtype from multiple bird species as well as swine highlights the need to better understand the potential of these viruses to spread and cause disease in humans. Here we analyzed the virulence, transmissibility and receptor-binding preference of two avian influenza H2 viruses (H2N2 and H2N3) and compared them to a swine H2N3 (A/swine/Missouri/2124514/2006 [swMO]), and a human H2N2 (A/England/10/1967 [Eng/67]) virus using the ferret model as a mammalian host. Both avian H2 viruses possessed the capacity to spread efficiently between cohoused ferrets, and the swine (swMO) and human (Eng/67) viruses transmitted to naïve ferrets by respiratory droplets. Further characterization of the swMO hemagglutinin (HA) by x-ray crystallography and glycan microarray array identified receptor-specific adaptive mutations. As influenza virus quasispecies dynamics during transmission have not been well characterized, we sequenced nasal washes collected during transmission studies to better understand experimental adaptation of H2 HA. The avian H2 viruses isolated from ferret nasal washes contained mutations in the HA1, including a Gln226Leu substitution, which is a mutation associated with α2,6 sialic acid (human-like) binding preference. These results suggest that the molecular structure of HA in viruses of the H2 subtype continue to have the potential to adapt to a mammalian host and become transmissible, after acquiring additional genetic markers.</AbstractText><CopyrightInformation>Published by Elsevier Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pappas</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Hua</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carney</LastName><ForeName>Paul J</ForeName><Initials>PJ</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pearce</LastName><ForeName>Melissa B</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Katz</LastName><ForeName>Jacqueline M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>James</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tumpey</LastName><ForeName>Terrence M</ForeName><Initials>TM</Initials><AffiliationInfo><Affiliation>Influenza Division, NCIRD, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333, USA. Electronic address: tft9@cdc.gov.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CC999999</GrantID><Agency>Intramural CDC HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 GM062116</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM62116</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH 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="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>02</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000220" MajorTopicYN="Y">Adaptation, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001717" MajorTopicYN="N">Birds</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005289" MajorTopicYN="N">Ferrets</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019267" MajorTopicYN="N">Hemagglutinin Glycoproteins, Influenza Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046228" MajorTopicYN="N">Microarray Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050505" MajorTopicYN="N">Mutant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020125" MajorTopicYN="N">Mutation, Missense</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009976" MajorTopicYN="N">Orthomyxoviridae Infections</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName><QualifierName UI="Q000635" MajorTopicYN="Y">transmission</QualifierName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053585" MajorTopicYN="Y">Virus Attachment</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Ferret</Keyword><Keyword MajorTopicYN="N">Hemagglutinin</Keyword><Keyword MajorTopicYN="N">Influenza</Keyword><Keyword MajorTopicYN="N">Transmission</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>12</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>01</Month><Day>04</Day></PubMedPubDate><PubMedPubDate 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