H2N2V1, Main, Exploration, bibRecord, 000E09

The PB2 Subunit of the Influenza Virus RNA Polymerase Affects Virulence by Interacting with the Mitochondrial Antiviral Signaling Protein and Inhibiting Expression of Beta Interferon▿

Identifieur interne : 000E09 ( Main/Exploration ); précédent : 000E08; suivant : 000E10

The PB2 Subunit of the Influenza Virus RNA Polymerase Affects Virulence by Interacting with the Mitochondrial Antiviral Signaling Protein and Inhibiting Expression of Beta Interferon▿

Auteurs : Katy M. Graef ; Frank T. Vreede ; Yuk-Fai Lau ; Amber W. Mccall ; Simon M. Carr ; Kanta Subbarao ; Ervin Fodor

Source :

Journal of Virology [ 0022-538X ] ; 2010.

RBID : PMC:2919034

Descripteurs français

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (genetics), Adaptor Proteins, Signal Transducing (metabolism), Amino Acid Sequence, Animals, Down-Regulation, Female, Host-Pathogen Interactions, Humans, Influenza A Virus, H1N1 Subtype (enzymology), Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (pathogenicity), Influenza A Virus, H2N2 Subtype (enzymology), Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (pathogenicity), Influenza A Virus, H5N1 Subtype (enzymology), Influenza A Virus, H5N1 Subtype (genetics), Influenza A Virus, H5N1 Subtype (pathogenicity), Influenza A virus (enzymology), Influenza A virus (genetics), Influenza A virus (pathogenicity), Influenza, Human (genetics), Influenza, Human (metabolism), Influenza, Human (virology), Interferon-beta (genetics), Interferon-beta (metabolism), Mice, Mice, Inbred C57BL, Molecular Sequence Data, Protein Binding, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (metabolism), Sequence Alignment, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism), Virulence.
MESH :
- chemical , chemistry : RNA Replicase, Viral Proteins.
- chemical , genetics : Adaptor Proteins, Signal Transducing, Interferon-beta, RNA Replicase, Viral Proteins.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Interferon-beta, RNA Replicase, Viral Proteins.
- enzymology : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H2N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus.
- genetics : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H2N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus, Influenza, Human.
- metabolism : Influenza, Human.
- pathogenicity : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H2N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus.
- virology : Influenza, Human.
- Amino Acid Sequence, Animals, Down-Regulation, Female, Host-Pathogen Interactions, Humans, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Protein Binding, Sequence Alignment, Virulence.

Abstract

The PB2 subunit of the influenza virus RNA polymerase is a major virulence determinant of influenza viruses. However, the molecular mechanisms involved remain unknown. It was previously shown that the PB2 protein, in addition to its nuclear localization, also accumulates in the mitochondria. Here, we demonstrate that the PB2 protein interacts with the mitochondrial antiviral signaling protein, MAVS (also known as IPS-1, VISA, or Cardif), and inhibits MAVS-mediated beta interferon (IFN-β) expression. In addition, we show that PB2 proteins of influenza viruses differ in their abilities to associate with the mitochondria. In particular, the PB2 proteins of seasonal human influenza viruses localize to the mitochondria while PB2 proteins of avian influenza viruses are nonmitochondrial. This difference in localization is caused by a single amino acid polymorphism in the PB2 mitochondrial targeting signal. In order to address the functional significance of the mitochondrial localization of the PB2 protein in vivo, we have generated two recombinant human influenza viruses encoding either mitochondrial or nonmitochondrial PB2 proteins. We found that the difference in the mitochondrial localization of the PB2 proteins does not affect the growth of these viruses in cell culture. However, the virus encoding the nonmitochondrial PB2 protein induces higher levels of IFN-β and, in an animal model, is attenuated compared to the isogenic virus encoding a mitochondrial PB2. Overall this study implicates the PB2 protein in the regulation of host antiviral innate immune pathways and suggests an important role for the mitochondrial association of the PB2 protein in determining virulence.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919034

DOI: 10.1128/JVI.00879-10
PubMed: 20538852
PubMed Central: 2919034

Affiliations:

Le document en format XML

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<term>Adaptor Proteins, Signal Transducing (metabolism)</term>
<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Down-Regulation</term>
<term>Female</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Influenza A Virus, H1N1 Subtype (enzymology)</term>
<term>Influenza A Virus, H1N1 Subtype (genetics)</term>
<term>Influenza A Virus, H1N1 Subtype (pathogenicity)</term>
<term>Influenza A Virus, H2N2 Subtype (enzymology)</term>
<term>Influenza A Virus, H2N2 Subtype (genetics)</term>
<term>Influenza A Virus, H2N2 Subtype (pathogenicity)</term>
<term>Influenza A Virus, H5N1 Subtype (enzymology)</term>
<term>Influenza A Virus, H5N1 Subtype (genetics)</term>
<term>Influenza A Virus, H5N1 Subtype (pathogenicity)</term>
<term>Influenza A virus (enzymology)</term>
<term>Influenza A virus (genetics)</term>
<term>Influenza A virus (pathogenicity)</term>
<term>Influenza, Human (genetics)</term>
<term>Influenza, Human (metabolism)</term>
<term>Influenza, Human (virology)</term>
<term>Interferon-beta (genetics)</term>
<term>Interferon-beta (metabolism)</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>RNA Replicase (chemistry)</term>
<term>RNA Replicase (genetics)</term>
<term>RNA Replicase (metabolism)</term>
<term>Sequence Alignment</term>
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<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term>
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<term>Données de séquences moléculaires</term>
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<term>Grippe humaine (métabolisme)</term>
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<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
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<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>RNA replicase ()</term>
<term>RNA replicase (génétique)</term>
<term>RNA replicase (métabolisme)</term>
<term>Régulation négative</term>
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<term>Souris de lignée C57BL</term>
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<term>Sous-type H1N1 du virus de la grippe A (génétique)</term>
<term>Sous-type H1N1 du virus de la grippe A (pathogénicité)</term>
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<term>Sous-type H2N2 du virus de la grippe A (génétique)</term>
<term>Sous-type H2N2 du virus de la grippe A (pathogénicité)</term>
<term>Sous-type H5N1 du virus de la grippe A (enzymologie)</term>
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<term>Virus de la grippe A</term>
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<term>Influenza A Virus, H5N1 Subtype</term>
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<term>Protéines virales</term>
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<term>Sous-type H5N1 du virus de la grippe A</term>
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<term>Influenza A Virus, H2N2 Subtype</term>
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<term>Sous-type H5N1 du virus de la grippe A</term>
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<term>Down-Regulation</term>
<term>Female</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Mice</term>
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<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Sequence Alignment</term>
<term>Virulence</term>
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<term>Données de séquences moléculaires</term>
<term>Femelle</term>
<term>Humains</term>
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<term>Régulation négative</term>
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<front><div type="abstract" xml:lang="en"><p>The PB2 subunit of the influenza virus RNA polymerase is a major virulence determinant of influenza viruses. However, the molecular mechanisms involved remain unknown. It was previously shown that the PB2 protein, in addition to its nuclear localization, also accumulates in the mitochondria. Here, we demonstrate that the PB2 protein interacts with the mitochondrial antiviral signaling protein, MAVS (also known as IPS-1, VISA, or Cardif), and inhibits MAVS-mediated beta interferon (IFN-β) expression. In addition, we show that PB2 proteins of influenza viruses differ in their abilities to associate with the mitochondria. In particular, the PB2 proteins of seasonal human influenza viruses localize to the mitochondria while PB2 proteins of avian influenza viruses are nonmitochondrial. This difference in localization is caused by a single amino acid polymorphism in the PB2 mitochondrial targeting signal. In order to address the functional significance of the mitochondrial localization of the PB2 protein <italic>in vivo</italic>
, we have generated two recombinant human influenza viruses encoding either mitochondrial or nonmitochondrial PB2 proteins. We found that the difference in the mitochondrial localization of the PB2 proteins does not affect the growth of these viruses in cell culture. However, the virus encoding the nonmitochondrial PB2 protein induces higher levels of IFN-β and, in an animal model, is attenuated compared to the isogenic virus encoding a mitochondrial PB2. Overall this study implicates the PB2 protein in the regulation of host antiviral innate immune pathways and suggests an important role for the mitochondrial association of the PB2 protein in determining virulence.</p>
</div>
</front>
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<affiliations><list></list>
<tree><noCountry><name sortKey="Carr, Simon M" sort="Carr, Simon M" uniqKey="Carr S" first="Simon M." last="Carr">Simon M. Carr</name>
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<name sortKey="Graef, Katy M" sort="Graef, Katy M" uniqKey="Graef K" first="Katy M." last="Graef">Katy M. Graef</name>
<name sortKey="Lau, Yuk Fai" sort="Lau, Yuk Fai" uniqKey="Lau Y" first="Yuk-Fai" last="Lau">Yuk-Fai Lau</name>
<name sortKey="Mccall, Amber W" sort="Mccall, Amber W" uniqKey="Mccall A" first="Amber W." last="Mccall">Amber W. Mccall</name>
<name sortKey="Subbarao, Kanta" sort="Subbarao, Kanta" uniqKey="Subbarao K" first="Kanta" last="Subbarao">Kanta Subbarao</name>
<name sortKey="Vreede, Frank T" sort="Vreede, Frank T" uniqKey="Vreede F" first="Frank T." last="Vreede">Frank T. Vreede</name>
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The PB2 Subunit of the Influenza Virus RNA Polymerase Affects Virulence by Interacting with the Mitochondrial Antiviral Signaling Protein and Inhibiting Expression of Beta Interferon▿

The PB2 Subunit of the Influenza Virus RNA Polymerase Affects Virulence by Interacting with the Mitochondrial Antiviral Signaling Protein and Inhibiting Expression of Beta Interferon▿

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