Co‐degradation of interferon signaling factor DDX3 by PB1‐F2 as a basis for high virulence of 1918 pandemic influenza
Identifieur interne : 000357 ( Main/Curation ); précédent : 000356; suivant : 000358Co‐degradation of interferon signaling factor DDX3 by PB1‐F2 as a basis for high virulence of 1918 pandemic influenza
Auteurs : Eun-Sook Park ; Young Ho Byun ; Soree Park ; Yo Han Jang ; Woo-Ry Han ; Juhee Won ; Kyung Cho Cho ; Doo Hyun Kim ; Ah Ram Lee ; Gu-Choul Shin ; Yong Kwang Park ; Hong Seok Kang ; Heewoo Sim ; Yea Na Ha ; Byeongjune Jae ; Ahyun Son ; Paul Kim ; Jieun Yu ; Hye-Min Lee ; Sun-Bin Kwon ; Kwang Pyo Kim ; Seung-Hyun Lee ; Yeong-Min Park ; Baik L. Seong ; Kyun-Hwan KimSource :
- The EMBO Journal [ 0261-4189 ] ; 2019.
Descripteurs français
- KwdFr :
- Animaux, Cellules A549, Cellules HEK293, Cellules U937, Cellules rénales canines Madin-Darby, Chiens, DEAD-box RNA helicases (métabolisme), Femelle, Grippe humaine (histoire), Grippe humaine (virologie), Grippe humaine (épidémiologie), Histoire du 20ème siècle, Humains, Interférons (métabolisme), Orthomyxoviridae (métabolisme), Orthomyxoviridae (pathogénicité), Pandémies, Protéines virales (métabolisme), Protéines virales (physiologie), Protéolyse, Souris, Souris de lignée BALB C, Transduction du signal, Virulence (physiologie).
- MESH :
- histoire : Grippe humaine.
- métabolisme : DEAD-box RNA helicases, Interférons, Orthomyxoviridae, Protéines virales.
- pathogénicité : Orthomyxoviridae.
- physiologie : Protéines virales, Virulence.
- virologie : Grippe humaine.
- épidémiologie : Grippe humaine.
- Animaux, Cellules A549, Cellules HEK293, Cellules U937, Cellules rénales canines Madin-Darby, Chiens, Femelle, Histoire du 20ème siècle, Humains, Pandémies, Protéolyse, Souris, Souris de lignée BALB C, Transduction du signal.
English descriptors
- KwdEn :
- A549 Cells, Animals, DEAD-box RNA Helicases (metabolism), Dogs, Female, HEK293 Cells, History, 20th Century, Humans, Influenza, Human (epidemiology), Influenza, Human (history), Influenza, Human (virology), Interferons (metabolism), Madin Darby Canine Kidney Cells, Mice, Mice, Inbred BALB C, Orthomyxoviridae (metabolism), Orthomyxoviridae (pathogenicity), Pandemics, Proteolysis, Signal Transduction, U937 Cells, Viral Proteins (metabolism), Viral Proteins (physiology), Virulence (physiology).
- MESH :
- chemical , metabolism : DEAD-box RNA Helicases, Interferons, Viral Proteins.
- epidemiology : Influenza, Human.
- history : Influenza, Human.
- metabolism : Orthomyxoviridae.
- pathogenicity : Orthomyxoviridae.
- chemical , physiology : Viral Proteins, Virulence.
- virology : Influenza, Human.
- A549 Cells, Animals, Dogs, Female, HEK293 Cells, History, 20th Century, Humans, Madin Darby Canine Kidney Cells, Mice, Mice, Inbred BALB C, Pandemics, Proteolysis, Signal Transduction, U937 Cells.
Abstract
The multifunctional influenza virus protein
Url:
DOI: 10.15252/embj.201899475
PubMed: 30979777
PubMed Central: 6518015
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PMC:6518015Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Co‐degradation of interferon signaling factor DDX3 by PB1‐F2 as a basis for high virulence of 1918 pandemic influenza</title>
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<author><name sortKey="Won, Juhee" sort="Won, Juhee" uniqKey="Won J" first="Juhee" last="Won">Juhee Won</name>
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<author><name sortKey="Cho, Kyung Cho" sort="Cho, Kyung Cho" uniqKey="Cho K" first="Kyung Cho" last="Cho">Kyung Cho Cho</name>
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<author><name sortKey="Kim, Doo Hyun" sort="Kim, Doo Hyun" uniqKey="Kim D" first="Doo Hyun" last="Kim">Doo Hyun Kim</name>
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<author><name sortKey="Shin, Gu Houl" sort="Shin, Gu Houl" uniqKey="Shin G" first="Gu-Choul" last="Shin">Gu-Choul Shin</name>
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<author><name sortKey="Kang, Hong Seok" sort="Kang, Hong Seok" uniqKey="Kang H" first="Hong Seok" last="Kang">Hong Seok Kang</name>
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<author><name sortKey="Sim, Heewoo" sort="Sim, Heewoo" uniqKey="Sim H" first="Heewoo" last="Sim">Heewoo Sim</name>
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</affiliation>
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<author><name sortKey="Ha, Yea Na" sort="Ha, Yea Na" uniqKey="Ha Y" first="Yea Na" last="Ha">Yea Na Ha</name>
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</affiliation>
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<author><name sortKey="Jae, Byeongjune" sort="Jae, Byeongjune" uniqKey="Jae B" first="Byeongjune" last="Jae">Byeongjune Jae</name>
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<author><name sortKey="Son, Ahyun" sort="Son, Ahyun" uniqKey="Son A" first="Ahyun" last="Son">Ahyun Son</name>
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<author><name sortKey="Kim, Paul" sort="Kim, Paul" uniqKey="Kim P" first="Paul" last="Kim">Paul Kim</name>
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<author><name sortKey="Yu, Jieun" sort="Yu, Jieun" uniqKey="Yu J" first="Jieun" last="Yu">Jieun Yu</name>
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<author><name sortKey="Lee, Hye In" sort="Lee, Hye In" uniqKey="Lee H" first="Hye-Min" last="Lee">Hye-Min Lee</name>
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</affiliation>
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<author><name sortKey="Kwon, Sun In" sort="Kwon, Sun In" uniqKey="Kwon S" first="Sun-Bin" last="Kwon">Sun-Bin Kwon</name>
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</affiliation>
</author>
<author><name sortKey="Kim, Kwang Pyo" sort="Kim, Kwang Pyo" uniqKey="Kim K" first="Kwang Pyo" last="Kim">Kwang Pyo Kim</name>
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<term>Animals</term>
<term>DEAD-box RNA Helicases (metabolism)</term>
<term>Dogs</term>
<term>Female</term>
<term>HEK293 Cells</term>
<term>History, 20th Century</term>
<term>Humans</term>
<term>Influenza, Human (epidemiology)</term>
<term>Influenza, Human (history)</term>
<term>Influenza, Human (virology)</term>
<term>Interferons (metabolism)</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Orthomyxoviridae (metabolism)</term>
<term>Orthomyxoviridae (pathogenicity)</term>
<term>Pandemics</term>
<term>Proteolysis</term>
<term>Signal Transduction</term>
<term>U937 Cells</term>
<term>Viral Proteins (metabolism)</term>
<term>Viral Proteins (physiology)</term>
<term>Virulence (physiology)</term>
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<term>Cellules A549</term>
<term>Cellules HEK293</term>
<term>Cellules U937</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chiens</term>
<term>DEAD-box RNA helicases (métabolisme)</term>
<term>Femelle</term>
<term>Grippe humaine (histoire)</term>
<term>Grippe humaine (virologie)</term>
<term>Grippe humaine (épidémiologie)</term>
<term>Histoire du 20ème siècle</term>
<term>Humains</term>
<term>Interférons (métabolisme)</term>
<term>Orthomyxoviridae (métabolisme)</term>
<term>Orthomyxoviridae (pathogénicité)</term>
<term>Pandémies</term>
<term>Protéines virales (métabolisme)</term>
<term>Protéines virales (physiologie)</term>
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</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Viral Proteins</term>
<term>Virulence</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term>
</keywords>
<keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Grippe humaine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>A549 Cells</term>
<term>Animals</term>
<term>Dogs</term>
<term>Female</term>
<term>HEK293 Cells</term>
<term>History, 20th Century</term>
<term>Humans</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Pandemics</term>
<term>Proteolysis</term>
<term>Signal Transduction</term>
<term>U937 Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules A549</term>
<term>Cellules HEK293</term>
<term>Cellules U937</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chiens</term>
<term>Femelle</term>
<term>Histoire du 20ème siècle</term>
<term>Humains</term>
<term>Pandémies</term>
<term>Protéolyse</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Transduction du signal</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p>The multifunctional influenza virus protein <styled-content style="fixed-case">PB</styled-content>
1‐F2 plays several roles in deregulation of host innate immune responses and is a known immunopathology enhancer of the 1918 influenza pandemic. Here, we show that the 1918 <styled-content style="fixed-case">PB</styled-content>
1‐F2 protein not only interferes with the mitochondria‐dependent pathway of type I interferon (<styled-content style="fixed-case">IFN</styled-content>
) signaling, but also acquired a novel <styled-content style="fixed-case">IFN</styled-content>
antagonist function by targeting the <styled-content style="fixed-case">DEAD</styled-content>
‐box helicase <styled-content style="fixed-case">DDX</styled-content>
3, a key downstream mediator in antiviral interferon signaling, toward proteasome‐dependent degradation. Interactome analysis revealed that 1918 <styled-content style="fixed-case">PB</styled-content>
1‐F2, but not <styled-content style="fixed-case">PR</styled-content>
8 <styled-content style="fixed-case">PB</styled-content>
1‐F2, binds to <styled-content style="fixed-case">DDX</styled-content>
3 and causes its co‐degradation. Consistent with intrinsic protein instability as basis for this gain‐of‐function, internal structural disorder is associated with the unique cytotoxic sequences of the 1918 <styled-content style="fixed-case">PB</styled-content>
1‐F2 protein. Infusing mice with recombinant <styled-content style="fixed-case">DDX</styled-content>
3 protein completely rescued them from lethal infection with the 1918 <styled-content style="fixed-case">PB</styled-content>
1‐F2‐producing virus. Alongside <styled-content style="fixed-case">NS</styled-content>
1 protein, 1918 <styled-content style="fixed-case">PB</styled-content>
1‐F2 therefore constitutes a potent <styled-content style="fixed-case">IFN</styled-content>
antagonist causative for the severe pathogenicity of the 1918 influenza strain. Our identification of molecular determinants of pathogenesis should be useful for the future design of new antiviral strategies against influenza pandemics.</p>
</div>
</front>
</TEI>
</record>
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