Receptor specificity and transmission of H2N2 subtype viruses isolated from the pandemic of 1957.
Identifieur interne : 000195 ( PubMed/Corpus ); précédent : 000194; suivant : 000196Receptor specificity and transmission of H2N2 subtype viruses isolated from the pandemic of 1957.
Auteurs : Claudia Pappas ; Karthik Viswanathan ; Aarthi Chandrasekaran ; Rahul Raman ; Jacqueline M. Katz ; Ram Sasisekharan ; Terrence M. TumpeySource :
- PloS one [ 1932-6203 ] ; 2010.
English descriptors
- KwdEn :
- Animals, Birds, Disease Outbreaks, Erythrocytes (immunology), Ferrets, Hemagglutination, Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (isolation & purification), Influenza A Virus, H2N2 Subtype (metabolism), Influenza in Birds (transmission), Influenza in Birds (virology), Influenza, Human (epidemiology), Influenza, Human (transmission), Influenza, Human (virology), Male, Microarray Analysis, Models, Molecular, Mutation, Polysaccharides (metabolism), Protein Conformation, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Respiration, Seasons, Substrate Specificity.
- MESH :
- chemical , chemistry : Receptors, Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- epidemiology : Influenza, Human.
- genetics : Influenza A Virus, H2N2 Subtype.
- immunology : Erythrocytes.
- isolation & purification : Influenza A Virus, H2N2 Subtype.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H2N2 Subtype, Polysaccharides, Receptors, Virus.
- transmission : Influenza in Birds, Influenza, Human.
- virology : Influenza in Birds, Influenza, Human.
- Animals, Birds, Disease Outbreaks, Ferrets, Hemagglutination, Humans, Male, Microarray Analysis, Models, Molecular, Mutation, Protein Conformation, Respiration, Seasons, Substrate Specificity.
Abstract
Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.
DOI: 10.1371/journal.pone.0011158
PubMed: 20574518
Links to Exploration step
pubmed:20574518Le document en format XML
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The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20574518</PMID><DateCompleted><Year>2010</Year><Month>11</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Jun</Month><Day>21</Day></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Receptor specificity and transmission of H2N2 subtype viruses isolated from the pandemic of 1957.</ArticleTitle><Pagination><MedlinePgn>e11158</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0011158</ELocationID><Abstract><AbstractText>Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pappas</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Influenza Division, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Viswanathan</LastName><ForeName>Karthik</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Chandrasekaran</LastName><ForeName>Aarthi</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Raman</LastName><ForeName>Rahul</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Katz</LastName><ForeName>Jacqueline M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Sasisekharan</LastName><ForeName>Ram</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Tumpey</LastName><ForeName>Terrence M</ForeName><Initials>TM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>U54 GM062116</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 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="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate 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