Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets
Identifieur interne : 000033 ( 1968/Analysis ); précédent : 000032; suivant : 000034Assessment 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 [ 0042-6822 ] ; 2015.
Descripteurs français
- KwdFr :
- Adaptation biologique, Analyse sur microréseau, Animaux, Attachement viral, Cristallographie aux rayons X, Furets, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Humains, Infections à Orthomyxoviridae (anatomopathologie), Infections à Orthomyxoviridae (transmission), Infections à Orthomyxoviridae (virologie), Liaison aux protéines, Modèles animaux de maladie humaine, Mutation faux-sens, Oiseaux, Polyosides (analyse), Protéines mutantes (génétique), Suidae, Virulence, Virus de la grippe A (génétique), Virus de la grippe A (isolement et purification), Virus de la grippe A (pathogénicité), Virus de la grippe A (physiologie).
- MESH :
- analyse : Polyosides.
- anatomopathologie : Infections à Orthomyxoviridae.
- génétique : Glycoprotéine hémagglutinine du virus influenza, Protéines mutantes, Virus de la grippe A.
- isolement et purification : Virus de la grippe A.
- pathogénicité : Virus de la grippe A.
- physiologie : Virus de la grippe A.
- virologie : Infections à Orthomyxoviridae.
- Adaptation biologique, Analyse sur microréseau, Animaux, Attachement viral, Cristallographie aux rayons X, Furets, Glycoprotéine hémagglutinine du virus influenza, Humains, Infections à Orthomyxoviridae, Liaison aux protéines, Modèles animaux de maladie humaine, Mutation faux-sens, Oiseaux, Suidae, Virulence.
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.
Url:
DOI: 10.1016/j.virol.2015.01.002
PubMed: 25659818
PubMed Central: 5804491
Affiliations:
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PMC:5804491Le document en format XML
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Tumpey</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptation, Biological</term><term>Animals</term><term>Birds</term><term>Crystallography, X-Ray</term><term>Disease Models, Animal</term><term>Ferrets</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term><term>Humans</term><term>Influenza A virus (genetics)</term><term>Influenza A virus (isolation & purification)</term><term>Influenza A virus (pathogenicity)</term><term>Influenza A virus (physiology)</term><term>Microarray Analysis</term><term>Mutant Proteins (genetics)</term><term>Mutation, Missense</term><term>Orthomyxoviridae Infections (pathology)</term><term>Orthomyxoviridae Infections (transmission)</term><term>Orthomyxoviridae Infections (virology)</term><term>Polysaccharides (analysis)</term><term>Protein Binding</term><term>Swine</term><term>Virulence</term><term>Virus Attachment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adaptation biologique</term><term>Analyse sur microréseau</term><term>Animaux</term><term>Attachement viral</term><term>Cristallographie aux rayons X</term><term>Furets</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term><term>Humains</term><term>Infections à Orthomyxoviridae (anatomopathologie)</term><term>Infections à Orthomyxoviridae (transmission)</term><term>Infections à Orthomyxoviridae (virologie)</term><term>Liaison aux protéines</term><term>Modèles animaux de maladie humaine</term><term>Mutation faux-sens</term><term>Oiseaux</term><term>Polyosides (analyse)</term><term>Protéines mutantes (génétique)</term><term>Suidae</term><term>Virulence</term><term>Virus de la grippe A (génétique)</term><term>Virus de la grippe A (isolement et purification)</term><term>Virus de la grippe A (pathogénicité)</term><term>Virus de la grippe A (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Mutant Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Polyosides</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Infections à Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A 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scheme="MESH" qualifier="transmission" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adaptation, Biological</term><term>Animals</term><term>Birds</term><term>Crystallography, X-Ray</term><term>Disease Models, Animal</term><term>Ferrets</term><term>Humans</term><term>Microarray Analysis</term><term>Mutation, Missense</term><term>Protein Binding</term><term>Swine</term><term>Virulence</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adaptation biologique</term><term>Analyse sur microréseau</term><term>Animaux</term><term>Attachement viral</term><term>Cristallographie aux rayons X</term><term>Furets</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Humains</term><term>Infections à Orthomyxoviridae</term><term>Liaison aux protéines</term><term>Modèles animaux de maladie humaine</term><term>Mutation faux-sens</term><term>Oiseaux</term><term>Suidae</term><term>Virulence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">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.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Carney, Paul J" sort="Carney, Paul J" uniqKey="Carney P" first="Paul J." last="Carney">Paul J. Carney</name><name sortKey="Katz, Jacqueline M" sort="Katz, Jacqueline M" uniqKey="Katz J" first="Jacqueline M." last="Katz">Jacqueline M. Katz</name><name sortKey="Pappas, Claudia" sort="Pappas, Claudia" uniqKey="Pappas C" first="Claudia" last="Pappas">Claudia Pappas</name><name sortKey="Pearce, Melissa B" sort="Pearce, Melissa B" uniqKey="Pearce M" first="Melissa B." last="Pearce">Melissa B. Pearce</name><name sortKey="Stevens, James" sort="Stevens, James" uniqKey="Stevens J" first="James" last="Stevens">James Stevens</name><name sortKey="Tumpey, Terrence M" sort="Tumpey, Terrence M" uniqKey="Tumpey T" first="Terrence M." last="Tumpey">Terrence M. Tumpey</name><name sortKey="Yang, Hua" sort="Yang, Hua" uniqKey="Yang H" first="Hua" last="Yang">Hua Yang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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