A 27-amino-acid deletion in the neuraminidase stalk supports replication of an avian H2N2 influenza A virus in the respiratory tract of chickens.
Identifieur interne : 000191 ( PubMed/Curation ); précédent : 000190; suivant : 000192A 27-amino-acid deletion in the neuraminidase stalk supports replication of an avian H2N2 influenza A virus in the respiratory tract of chickens.
Auteurs : Erin M. Sorrell [Pays-Bas] ; Haichen Song ; Lindomar Pena ; Daniel R. PerezSource :
- Journal of virology [ 1098-5514 ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Appareil respiratoire (virologie), Caille, Coturnix, Données de séquences moléculaires, Délétion de séquence, Grippe chez les oiseaux (virologie), Lignée cellulaire, Maladies de la volaille (virologie), Poulets, Protéines virales (génétique), Protéines virales (métabolisme), Réplication virale, Sialidase (génétique), Sialidase (métabolisme), Sous-type H2N2 du virus de la grippe A (enzymologie), Sous-type H2N2 du virus de la grippe A (génétique), Sous-type H2N2 du virus de la grippe A (physiologie).
- MESH :
- enzymologie : Sous-type H2N2 du virus de la grippe A.
- génétique : Protéines virales, Sialidase, Sous-type H2N2 du virus de la grippe A.
- métabolisme : Protéines virales, Sialidase.
- physiologie : Sous-type H2N2 du virus de la grippe A.
- virologie : Appareil respiratoire, Grippe chez les oiseaux, Maladies de la volaille.
- Animaux, Caille, Coturnix, Données de séquences moléculaires, Délétion de séquence, Lignée cellulaire, Poulets, Réplication virale.
English descriptors
- KwdEn :
- Animals, Cell Line, Chickens, Coturnix, Influenza A Virus, H2N2 Subtype (enzymology), Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (physiology), Influenza in Birds (virology), Molecular Sequence Data, Neuraminidase (genetics), Neuraminidase (metabolism), Poultry Diseases (virology), Quail, Respiratory System (virology), Sequence Deletion, Viral Proteins (genetics), Viral Proteins (metabolism), Virus Replication.
- MESH :
- chemical , genetics : Neuraminidase, Viral Proteins.
- enzymology : Influenza A Virus, H2N2 Subtype.
- genetics : Influenza A Virus, H2N2 Subtype.
- chemical , metabolism : Neuraminidase, Viral Proteins.
- physiology : Influenza A Virus, H2N2 Subtype.
- virology : Influenza in Birds, Poultry Diseases, Respiratory System.
- Animals, Cell Line, Chickens, Coturnix, Molecular Sequence Data, Quail, Sequence Deletion, Virus Replication.
Abstract
The events and mechanisms that lead to interspecies transmission of, and host adaptation to, influenza A virus are unknown; however, both surface and internal proteins have been implicated. Our previous report highlighted the role that Japanese quail play as an intermediate host, expanding the host range of a mallard H2N2 virus, A/mallard/Potsdam/178-4/83 (H2N2), through viral adaptation. This quail-adapted virus supported transmission in quail and increased its host range to replicate and be transmitted efficiently in chickens. Here we report that of the six amino acid changes in the quail-adapted virus, a single change in the hemagglutinin (HA) was crucial for transmission in quail, while the changes in the polymerase genes favored replication at lower temperatures than those for the wild-type mallard virus. Reverse genetic analysis indicated that all adaptive mutations were necessary for transmission in chickens, further implicating quail in extending this virus to terrestrial poultry. Adaptation of the quail-adapted virus in chickens resulted in the alteration of viral tropism from intestinal shedding to shedding and transmission via the respiratory tract. Sequence analysis indicated that this chicken-adapted virus maintained all quail-adaptive mutations, as well as an additional change in the HA and, most notably, a 27-amino-acid deletion in the stalk region of neuraminidase (NA), a genotypic marker of influenza virus adaptation to chickens. This stalk deletion was shown to be responsible for the change in virus tropism from the intestine to the respiratory tract.
DOI: 10.1128/JVI.01460-10
PubMed: 20826691
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Our previous report highlighted the role that Japanese quail play as an intermediate host, expanding the host range of a mallard H2N2 virus, A/mallard/Potsdam/178-4/83 (H2N2), through viral adaptation. This quail-adapted virus supported transmission in quail and increased its host range to replicate and be transmitted efficiently in chickens. Here we report that of the six amino acid changes in the quail-adapted virus, a single change in the hemagglutinin (HA) was crucial for transmission in quail, while the changes in the polymerase genes favored replication at lower temperatures than those for the wild-type mallard virus. Reverse genetic analysis indicated that all adaptive mutations were necessary for transmission in chickens, further implicating quail in extending this virus to terrestrial poultry. Adaptation of the quail-adapted virus in chickens resulted in the alteration of viral tropism from intestinal shedding to shedding and transmission via the respiratory tract. Sequence analysis indicated that this chicken-adapted virus maintained all quail-adaptive mutations, as well as an additional change in the HA and, most notably, a 27-amino-acid deletion in the stalk region of neuraminidase (NA), a genotypic marker of influenza virus adaptation to chickens. This stalk deletion was shown to be responsible for the change in virus tropism from the intestine to the respiratory tract.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20826691</PMID><DateCompleted><Year>2010</Year><Month>11</Month><Day>22</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>84</Volume><Issue>22</Issue><PubDate><Year>2010</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>A 27-amino-acid deletion in the neuraminidase stalk supports replication of an avian H2N2 influenza A virus in the respiratory tract of chickens.</ArticleTitle><Pagination><MedlinePgn>11831-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01460-10</ELocationID><Abstract><AbstractText>The events and mechanisms that lead to interspecies transmission of, and host adaptation to, influenza A virus are unknown; however, both surface and internal proteins have been implicated. Our previous report highlighted the role that Japanese quail play as an intermediate host, expanding the host range of a mallard H2N2 virus, A/mallard/Potsdam/178-4/83 (H2N2), through viral adaptation. This quail-adapted virus supported transmission in quail and increased its host range to replicate and be transmitted efficiently in chickens. Here we report that of the six amino acid changes in the quail-adapted virus, a single change in the hemagglutinin (HA) was crucial for transmission in quail, while the changes in the polymerase genes favored replication at lower temperatures than those for the wild-type mallard virus. Reverse genetic analysis indicated that all adaptive mutations were necessary for transmission in chickens, further implicating quail in extending this virus to terrestrial poultry. Adaptation of the quail-adapted virus in chickens resulted in the alteration of viral tropism from intestinal shedding to shedding and transmission via the respiratory tract. Sequence analysis indicated that this chicken-adapted virus maintained all quail-adaptive mutations, as well as an additional change in the HA and, most notably, a 27-amino-acid deletion in the stalk region of neuraminidase (NA), a genotypic marker of influenza virus adaptation to chickens. This stalk deletion was shown to be responsible for the change in virus tropism from the intestine to the respiratory tract.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sorrell</LastName><ForeName>Erin M</ForeName><Initials>EM</Initials><AffiliationInfo><Affiliation>Department of Virology, Erasmus Medical Center, Rotterdam, Netherlands. esorrell@umd.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Haichen</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Pena</LastName><ForeName>Lindomar</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Perez</LastName><ForeName>Daniel R</ForeName><Initials>DR</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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