Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.
Identifieur interne : 000471 ( Ncbi/Curation ); précédent : 000470; suivant : 000472Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.
Auteurs : Eric Bortz [États-Unis] ; Liset Westera ; Jad Maamary ; John Steel ; Randy A. Albrecht ; Balaji Manicassamy ; Geoffrey Chase ; Luis Martínez-Sobrido ; Martin Schwemmle ; Adolfo García-SastreSource :
- mBio [ 2150-7511 ] ; 2011.
Descripteurs français
- KwdFr :
- Humains, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Protéines de liaison à l'ARN (métabolisme), Protéines du core viral (métabolisme), Protéines virales (métabolisme), RNA replicase (métabolisme), Sous-type H1N1 du virus de la grippe A (enzymologie), Sous-type H1N1 du virus de la grippe A (pathogénicité), Sous-type H5N1 du virus de la grippe A (enzymologie), Sous-type H5N1 du virus de la grippe A (pathogénicité).
- MESH :
- enzymologie : Sous-type H1N1 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A.
- métabolisme : Protéines de liaison à l'ARN, Protéines du core viral, Protéines virales, RNA replicase.
- pathogénicité : Sous-type H1N1 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A.
- Humains, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire.
English descriptors
- KwdEn :
- Cell Line, Host-Pathogen Interactions, Humans, Influenza A Virus, H1N1 Subtype (enzymology), Influenza A Virus, H1N1 Subtype (pathogenicity), Influenza A Virus, H5N1 Subtype (enzymology), Influenza A Virus, H5N1 Subtype (pathogenicity), Protein Binding, RNA Replicase (metabolism), RNA-Binding Proteins (metabolism), Viral Core Proteins (metabolism), Viral Proteins (metabolism).
- MESH :
- chemical , metabolism : RNA Replicase, RNA-Binding Proteins, Viral Core Proteins, Viral Proteins.
- enzymology : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype.
- pathogenicity : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype.
- Cell Line, Host-Pathogen Interactions, Humans, Protein Binding.
Abstract
Highly pathogenic avian influenza A (HPAI) viruses of the H5N1 subtype have recently emerged from avian zoonotic reservoirs to cause fatal human disease. Adaptation of HPAI virus RNA-dependent RNA polymerase (PB1, PB2, and PA proteins) and nucleoprotein (NP) to interactions with mammalian host proteins is thought to contribute to the efficiency of viral RNA synthesis and to disease severity. While proteomics experiments have identified a number of human proteins that associate with H1N1 polymerases and/or viral ribonucleoprotein (vRNP), how these host interactions might regulate influenza virus polymerase functions and host adaptation has been largely unexplored. We took a functional genomics (RNA interference [RNAi]) approach to assess the roles of a network of human proteins interacting with influenza virus polymerase proteins in viral polymerase activity from prototype H1N1 and H5N1 viruses. A majority (18 of 31) of the cellular proteins tested, including RNA-binding (DDX17, DDX5, NPM1, and hnRNPM), stress (PARP1, DDB1, and Ku70/86), and intracellular transport proteins, were required for efficient activity of both H1N1 and H5N1 polymerases. NXP2 and NF90 antagonized both polymerases, and six more RNA-associated proteins exhibited strain-specific phenotypes. Remarkably, 12 proteins differentially regulated H5N1 polymerase according to PB2 genotype at mammalian-adaptive residue 627. Among these, DEAD box RNA helicase DDX17/p72 facilitated efficient human-adapted (627K) H5N1 virus mRNA and viral RNA (vRNA) synthesis in human cells. Likewise, the chicken DDX17 homologue was required for efficient avian (627E) H5N1 infection in chicken DF-1 fibroblasts, suggesting that this conserved virus-host interaction contributes to PB2-dependent host species specificity of influenza virus and ultimately to the outcome of human HPAI infections.
DOI: 10.1128/mBio.00151-11
PubMed: 21846828
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pubmed:21846828Le document en format XML
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<term>Influenza A Virus, H1N1 Subtype (pathogenicity)</term>
<term>Influenza A Virus, H5N1 Subtype (enzymology)</term>
<term>Influenza A Virus, H5N1 Subtype (pathogenicity)</term>
<term>Protein Binding</term>
<term>RNA Replicase (metabolism)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Viral Core Proteins (metabolism)</term>
<term>Viral Proteins (metabolism)</term>
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<term>Interactions hôte-pathogène</term>
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<term>Lignée cellulaire</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Protéines du core viral (métabolisme)</term>
<term>Protéines virales (métabolisme)</term>
<term>RNA replicase (métabolisme)</term>
<term>Sous-type H1N1 du virus de la grippe A (enzymologie)</term>
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<term>Sous-type H5N1 du virus de la grippe A (pathogénicité)</term>
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<term>RNA-Binding Proteins</term>
<term>Viral Core Proteins</term>
<term>Viral Proteins</term>
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<term>Protéines du core viral</term>
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<front><div type="abstract" xml:lang="en">Highly pathogenic avian influenza A (HPAI) viruses of the H5N1 subtype have recently emerged from avian zoonotic reservoirs to cause fatal human disease. Adaptation of HPAI virus RNA-dependent RNA polymerase (PB1, PB2, and PA proteins) and nucleoprotein (NP) to interactions with mammalian host proteins is thought to contribute to the efficiency of viral RNA synthesis and to disease severity. While proteomics experiments have identified a number of human proteins that associate with H1N1 polymerases and/or viral ribonucleoprotein (vRNP), how these host interactions might regulate influenza virus polymerase functions and host adaptation has been largely unexplored. We took a functional genomics (RNA interference [RNAi]) approach to assess the roles of a network of human proteins interacting with influenza virus polymerase proteins in viral polymerase activity from prototype H1N1 and H5N1 viruses. A majority (18 of 31) of the cellular proteins tested, including RNA-binding (DDX17, DDX5, NPM1, and hnRNPM), stress (PARP1, DDB1, and Ku70/86), and intracellular transport proteins, were required for efficient activity of both H1N1 and H5N1 polymerases. NXP2 and NF90 antagonized both polymerases, and six more RNA-associated proteins exhibited strain-specific phenotypes. Remarkably, 12 proteins differentially regulated H5N1 polymerase according to PB2 genotype at mammalian-adaptive residue 627. Among these, DEAD box RNA helicase DDX17/p72 facilitated efficient human-adapted (627K) H5N1 virus mRNA and viral RNA (vRNA) synthesis in human cells. Likewise, the chicken DDX17 homologue was required for efficient avian (627E) H5N1 infection in chicken DF-1 fibroblasts, suggesting that this conserved virus-host interaction contributes to PB2-dependent host species specificity of influenza virus and ultimately to the outcome of human HPAI infections.</div>
</front>
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