Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription
Identifieur interne : 000E65 ( Main/Exploration ); précédent : 000E64; suivant : 000E66Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription
Auteurs : Rei-Lin Kuo ; Chen Zhao ; Meghana Malur ; Robert M. KrugSource :
- Virology [ 0042-6822 ] ; 2010.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Animaux, Chiens, Données de séquences moléculaires, Facteur-3 de régulation d'interféron (antagonistes et inhibiteurs), Facteur-3 de régulation d'interféron (physiologie), Facteurs de transcription (métabolisme), Humains, Interféron bêta (génétique), Liaison aux protéines, Lignée cellulaire, Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (physiologie), Protéines à motif tripartite, Similitude de séquences d'acides aminés, Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H1N1 du virus de la grippe A (pathogénicité), Sous-type H1N1 du virus de la grippe A (physiologie), Sous-type H3N2 du virus de la grippe A (génétique), Sous-type H3N2 du virus de la grippe A (pathogénicité), Sous-type H3N2 du virus de la grippe A (physiologie), Sous-type H5N1 du virus de la grippe A (génétique), Sous-type H5N1 du virus de la grippe A (pathogénicité), Sous-type H5N1 du virus de la grippe A (physiologie), Spécificité d'espèce, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique, Transcription génétique, Ubiquitin-protein ligases (métabolisme), Virus de la grippe A (génétique), Virus de la grippe A (pathogénicité), Virus de la grippe A (physiologie).
- MESH :
- antagonistes et inhibiteurs : Facteur-3 de régulation d'interféron.
- génétique : ARN messager, Interféron bêta, Protéines virales non structurales, Sous-type H1N1 du virus de la grippe A, Sous-type H3N2 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A, Virus de la grippe A.
- métabolisme : ARN messager, Facteurs de transcription, Ubiquitin-protein ligases.
- pathogénicité : Sous-type H1N1 du virus de la grippe A, Sous-type H3N2 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A, Virus de la grippe A.
- physiologie : Facteur-3 de régulation d'interféron, Protéines virales non structurales, Sous-type H1N1 du virus de la grippe A, Sous-type H3N2 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A, Virus de la grippe A.
- Animaux, Chiens, Données de séquences moléculaires, Humains, Liaison aux protéines, Lignée cellulaire, Protéines virales non structurales, Protéines à motif tripartite, Similitude de séquences d'acides aminés, Spécificité d'espèce, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique, Transcription génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Dogs, Humans, Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (pathogenicity), Influenza A Virus, H1N1 Subtype (physiology), Influenza A Virus, H3N2 Subtype (genetics), Influenza A Virus, H3N2 Subtype (pathogenicity), Influenza A Virus, H3N2 Subtype (physiology), Influenza A Virus, H5N1 Subtype (genetics), Influenza A Virus, H5N1 Subtype (pathogenicity), Influenza A Virus, H5N1 Subtype (physiology), Influenza A virus (genetics), Influenza A virus (pathogenicity), Influenza A virus (physiology), Interferon Regulatory Factor-3 (antagonists & inhibitors), Interferon Regulatory Factor-3 (physiology), Interferon-beta (genetics), Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, RNA, Messenger (genetics), RNA, Messenger (metabolism), Sequence Homology, Amino Acid, Species Specificity, Transcription Factors (metabolism), Transcription, Genetic, Tripartite Motif Proteins, Ubiquitin-Protein Ligases (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (physiology).
- MESH :
- chemical , antagonists & inhibitors : Interferon Regulatory Factor-3.
- chemical , chemistry : Viral Nonstructural Proteins.
- genetics : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H3N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus, Interferon-beta, RNA, Messenger, Viral Nonstructural Proteins.
- chemical , metabolism : RNA, Messenger, Transcription Factors, Ubiquitin-Protein Ligases.
- pathogenicity : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H3N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus.
- physiology : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H3N2 Subtype, Influenza A Virus, H5N1 Subtype, Influenza A virus, Interferon Regulatory Factor-3, Viral Nonstructural Proteins.
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Dogs, Humans, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Species Specificity, Transcription, Genetic, Tripartite Motif Proteins.
Abstract
We demonstrate that influenza A virus strains that circulate in humans differ markedly in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription. Strong activation occurs in cells infected with viruses expressing NS1 proteins of seasonal H3N2 and H2N2 viruses, whereas activation is blocked in cells infected with viruses expressing NS1 proteins of some, but not all seasonal H1N1 viruses. The NS1 proteins of the 2009 H1N1 and H5N1 viruses also block these activations. The difference in this NS1 function is mediated largely by the C-terminal region of the effector domain, which contains the only amino acid (K or E at position 196) that covaries with the functional difference. Further, we show that TRIM25 binds the NS1 protein whether or not IRF3 activation is blocked, demonstrating that binding of TRIM25 by the NS1 protein does not necessarily lead to the blocking of IRF3 activation.
Url:
DOI: 10.1016/j.virol.2010.09.012
PubMed: 20934196
PubMed Central: 2975781
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: 000524
- to stream Pmc, to step Curation: 000524
- to stream Pmc, to step Checkpoint: 000935
- to stream PubMed, to step Corpus: 000189
- to stream PubMed, to step Curation: 000189
- to stream PubMed, to step Checkpoint: 000181
- to stream Ncbi, to step Merge: 000570
- to stream Ncbi, to step Curation: 000570
- to stream Ncbi, to step Checkpoint: 000570
- to stream Main, to step Merge: 000E71
- to stream Main, to step Curation: 000E65
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription</title><author><name sortKey="Kuo, Rei Lin" sort="Kuo, Rei Lin" uniqKey="Kuo R" first="Rei-Lin" last="Kuo">Rei-Lin Kuo</name></author><author><name sortKey="Zhao, Chen" sort="Zhao, Chen" uniqKey="Zhao C" first="Chen" last="Zhao">Chen Zhao</name></author><author><name sortKey="Malur, Meghana" sort="Malur, Meghana" uniqKey="Malur M" first="Meghana" last="Malur">Meghana Malur</name></author><author><name sortKey="Krug, Robert M" sort="Krug, Robert M" uniqKey="Krug R" first="Robert M." last="Krug">Robert M. Krug</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20934196</idno><idno type="pmc">2975781</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2975781</idno><idno type="RBID">PMC:2975781</idno><idno type="doi">10.1016/j.virol.2010.09.012</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">000524</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000524</idno><idno type="wicri:Area/Pmc/Curation">000524</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000524</idno><idno type="wicri:Area/Pmc/Checkpoint">000935</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000935</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:20934196</idno><idno type="wicri:Area/PubMed/Corpus">000189</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000189</idno><idno type="wicri:Area/PubMed/Curation">000189</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000189</idno><idno type="wicri:Area/PubMed/Checkpoint">000181</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000181</idno><idno type="wicri:Area/Ncbi/Merge">000570</idno><idno type="wicri:Area/Ncbi/Curation">000570</idno><idno type="wicri:Area/Ncbi/Checkpoint">000570</idno><idno type="wicri:doubleKey">0042-6822:2010:Kuo R:influenza:a:virus</idno><idno type="wicri:Area/Main/Merge">000E71</idno><idno type="wicri:Area/Main/Curation">000E65</idno><idno type="wicri:Area/Main/Exploration">000E65</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription</title><author><name sortKey="Kuo, Rei Lin" sort="Kuo, Rei Lin" uniqKey="Kuo R" first="Rei-Lin" last="Kuo">Rei-Lin Kuo</name></author><author><name sortKey="Zhao, Chen" sort="Zhao, Chen" uniqKey="Zhao C" first="Chen" last="Zhao">Chen Zhao</name></author><author><name sortKey="Malur, Meghana" sort="Malur, Meghana" uniqKey="Malur M" first="Meghana" last="Malur">Meghana Malur</name></author><author><name sortKey="Krug, Robert M" sort="Krug, Robert M" uniqKey="Krug R" first="Robert M." last="Krug">Robert M. Krug</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Dogs</term><term>Humans</term><term>Influenza A Virus, H1N1 Subtype (genetics)</term><term>Influenza A Virus, H1N1 Subtype (pathogenicity)</term><term>Influenza A Virus, H1N1 Subtype (physiology)</term><term>Influenza A Virus, H3N2 Subtype (genetics)</term><term>Influenza A Virus, H3N2 Subtype (pathogenicity)</term><term>Influenza A Virus, H3N2 Subtype (physiology)</term><term>Influenza A Virus, H5N1 Subtype (genetics)</term><term>Influenza A Virus, H5N1 Subtype (pathogenicity)</term><term>Influenza A Virus, H5N1 Subtype (physiology)</term><term>Influenza A virus (genetics)</term><term>Influenza A virus (pathogenicity)</term><term>Influenza A virus (physiology)</term><term>Interferon Regulatory Factor-3 (antagonists & inhibitors)</term><term>Interferon Regulatory Factor-3 (physiology)</term><term>Interferon-beta (genetics)</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Sequence Homology, Amino Acid</term><term>Species Specificity</term><term>Transcription Factors (metabolism)</term><term>Transcription, Genetic</term><term>Tripartite Motif Proteins</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>ARN messager (métabolisme)</term><term>Animaux</term><term>Chiens</term><term>Données de séquences moléculaires</term><term>Facteur-3 de régulation d'interféron (antagonistes et inhibiteurs)</term><term>Facteur-3 de régulation d'interféron (physiologie)</term><term>Facteurs de transcription (métabolisme)</term><term>Humains</term><term>Interféron bêta (génétique)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (physiologie)</term><term>Protéines à motif tripartite</term><term>Similitude de séquences d'acides aminés</term><term>Sous-type H1N1 du virus de la grippe A (génétique)</term><term>Sous-type H1N1 du virus de la grippe A (pathogénicité)</term><term>Sous-type H1N1 du virus de la grippe A (physiologie)</term><term>Sous-type H3N2 du virus de la grippe A (génétique)</term><term>Sous-type H3N2 du virus de la grippe A (pathogénicité)</term><term>Sous-type H3N2 du virus de la grippe A (physiologie)</term><term>Sous-type H5N1 du virus de la grippe A (génétique)</term><term>Sous-type H5N1 du virus de la grippe A (pathogénicité)</term><term>Sous-type H5N1 du virus de la grippe A (physiologie)</term><term>Spécificité d'espèce</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transcription génétique</term><term>Ubiquitin-protein ligases (métabolisme)</term><term>Virus de la grippe A (génétique)</term><term>Virus de la grippe A (pathogénicité)</term><term>Virus de la grippe A (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Interferon Regulatory Factor-3</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Facteur-3 de régulation d'interféron</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza A Virus, H3N2 Subtype</term><term>Influenza A Virus, H5N1 Subtype</term><term>Influenza A virus</term><term>Interferon-beta</term><term>RNA, Messenger</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term><term>Interféron bêta</term><term>Protéines virales non structurales</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Sous-type H3N2 du virus de la grippe A</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA, Messenger</term><term>Transcription Factors</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Facteurs de transcription</term><term>Ubiquitin-protein ligases</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza A Virus, H3N2 Subtype</term><term>Influenza A Virus, H5N1 Subtype</term><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Sous-type H1N1 du virus de la grippe A</term><term>Sous-type H3N2 du virus de la grippe A</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Facteur-3 de régulation d'interféron</term><term>Protéines virales non structurales</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Sous-type H3N2 du virus de la grippe A</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza A Virus, H3N2 Subtype</term><term>Influenza A Virus, H5N1 Subtype</term><term>Influenza A virus</term><term>Interferon Regulatory Factor-3</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Dogs</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term><term>Species Specificity</term><term>Transcription, Genetic</term><term>Tripartite Motif Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chiens</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines virales non structurales</term><term>Protéines à motif tripartite</term><term>Similitude de séquences d'acides aminés</term><term>Spécificité d'espèce</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transcription génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">We demonstrate that influenza A virus strains that circulate in humans differ markedly in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription. Strong activation occurs in cells infected with viruses expressing NS1 proteins of seasonal H3N2 and H2N2 viruses, whereas activation is blocked in cells infected with viruses expressing NS1 proteins of some, but not all seasonal H1N1 viruses. The NS1 proteins of the 2009 H1N1 and H5N1 viruses also block these activations. The difference in this NS1 function is mediated largely by the C-terminal region of the effector domain, which contains the only amino acid (K or E at position 196) that covaries with the functional difference. Further, we show that TRIM25 binds the NS1 protein whether or not IRF3 activation is blocked, demonstrating that binding of TRIM25 by the NS1 protein does not necessarily lead to the blocking of IRF3 activation.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Krug, Robert M" sort="Krug, Robert M" uniqKey="Krug R" first="Robert M." last="Krug">Robert M. Krug</name><name sortKey="Kuo, Rei Lin" sort="Kuo, Rei Lin" uniqKey="Kuo R" first="Rei-Lin" last="Kuo">Rei-Lin Kuo</name><name sortKey="Malur, Meghana" sort="Malur, Meghana" uniqKey="Malur M" first="Meghana" last="Malur">Meghana Malur</name><name sortKey="Zhao, Chen" sort="Zhao, Chen" uniqKey="Zhao C" first="Chen" last="Zhao">Chen Zhao</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000E65 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000E65 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= PMC:2975781
|texte= Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-β transcription
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:20934196" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a H2N2V1
| This area was generated with Dilib version V0.6.33. |  |