Influenza A virus uncoating.
Identifieur interne : 000421 ( Main/Exploration ); précédent : 000420; suivant : 000422Influenza A virus uncoating.
Auteurs : Yohei Yamauchi [Royaume-Uni]Source :
- Advances in virus research [ 1557-8399 ] ; 2020.
Abstract
Influenza A virus (IAV) is an enveloped virus of the Orthomyxoviridae with a negative-sense single-stranded RNA genome. During virus cell entry, viral and cellular cues are delivered in a stepwise manner within two distinct cellular compartments-the endosomes and the cytosol. Endosome maturation primes the viral core for uncoating by cytosolic host proteins and host-mediated virus disaggregation is essential for genome import and replication in the nucleus. Recent evidence shows that two well-known cellular proteins-histone deacetylase 6 (HDAC6) and karyopherin-β2 (kapβ2)-uncoat influenza virus. HDAC6 is 1 of 11 HDACs and an X-linked, cytosolic lysine deacetylase. Under normal cellular conditions HDAC6 is the tubulin deacetylase. Under proteasomal stress HDAC6 binds unanchored ubiquitin, dynein and myosin II to sequester misfolded protein aggregates for autophagy. Kapβ2 is a member of the importin β family that transports RNA-binding proteins into the nucleus by binding to disordered nuclear localization signals (NLSs) known as PY-NLS. Kapβ2 is emerging as a universal uncoating factor for IAV and human immunodeficiency virus type 1 (HIV-1). Kapβ2 can also reverse liquid-liquid phase separation (LLPS) of RNA-binding proteins by promoting their disaggregation. Thus, it is becoming evident that key players in the management of cellular condensates and membraneless organelles are potent virus uncoating factors. This emerging concept reveals implications in viral pathogenesis, as well as, the promise for cell-targeted therapeutic strategies to block universal virus uncoating pathways hijacked by enveloped RNA viruses.
DOI: 10.1016/bs.aivir.2020.01.001
PubMed: 32327145
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000036
- to stream PubMed, to step Curation: 000036
- to stream PubMed, to step Checkpoint: 000091
- to stream Ncbi, to step Merge: 000F87
- to stream Ncbi, to step Curation: 000F87
- to stream Ncbi, to step Checkpoint: 000F87
- to stream Main, to step Merge: 000421
- to stream Main, to step Curation: 000421
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Influenza A virus uncoating.</title>
<author><name sortKey="Yamauchi, Yohei" sort="Yamauchi, Yohei" uniqKey="Yamauchi Y" first="Yohei" last="Yamauchi">Yohei Yamauchi</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Cellular & Molecular Medicine, University of Bristol, Bristol, United Kingdom. Electronic address: yohei.yamauchi@bristol.ac.uk.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>School of Cellular & Molecular Medicine, University of Bristol, Bristol</wicri:regionArea>
<wicri:noRegion>Bristol</wicri:noRegion>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2020">2020</date>
<idno type="RBID">pubmed:32327145</idno>
<idno type="pmid">32327145</idno>
<idno type="doi">10.1016/bs.aivir.2020.01.001</idno>
<idno type="wicri:Area/PubMed/Corpus">000036</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000036</idno>
<idno type="wicri:Area/PubMed/Curation">000036</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000036</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000091</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000091</idno>
<idno type="wicri:Area/Ncbi/Merge">000F87</idno>
<idno type="wicri:Area/Ncbi/Curation">000F87</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000F87</idno>
<idno type="wicri:Area/Main/Merge">000421</idno>
<idno type="wicri:Area/Main/Curation">000421</idno>
<idno type="wicri:Area/Main/Exploration">000421</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Influenza A virus uncoating.</title>
<author><name sortKey="Yamauchi, Yohei" sort="Yamauchi, Yohei" uniqKey="Yamauchi Y" first="Yohei" last="Yamauchi">Yohei Yamauchi</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Cellular & Molecular Medicine, University of Bristol, Bristol, United Kingdom. Electronic address: yohei.yamauchi@bristol.ac.uk.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>School of Cellular & Molecular Medicine, University of Bristol, Bristol</wicri:regionArea>
<wicri:noRegion>Bristol</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j">Advances in virus research</title>
<idno type="eISSN">1557-8399</idno>
<imprint><date when="2020" type="published">2020</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Influenza A virus (IAV) is an enveloped virus of the Orthomyxoviridae with a negative-sense single-stranded RNA genome. During virus cell entry, viral and cellular cues are delivered in a stepwise manner within two distinct cellular compartments-the endosomes and the cytosol. Endosome maturation primes the viral core for uncoating by cytosolic host proteins and host-mediated virus disaggregation is essential for genome import and replication in the nucleus. Recent evidence shows that two well-known cellular proteins-histone deacetylase 6 (HDAC6) and karyopherin-β2 (kapβ2)-uncoat influenza virus. HDAC6 is 1 of 11 HDACs and an X-linked, cytosolic lysine deacetylase. Under normal cellular conditions HDAC6 is the tubulin deacetylase. Under proteasomal stress HDAC6 binds unanchored ubiquitin, dynein and myosin II to sequester misfolded protein aggregates for autophagy. Kapβ2 is a member of the importin β family that transports RNA-binding proteins into the nucleus by binding to disordered nuclear localization signals (NLSs) known as PY-NLS. Kapβ2 is emerging as a universal uncoating factor for IAV and human immunodeficiency virus type 1 (HIV-1). Kapβ2 can also reverse liquid-liquid phase separation (LLPS) of RNA-binding proteins by promoting their disaggregation. Thus, it is becoming evident that key players in the management of cellular condensates and membraneless organelles are potent virus uncoating factors. This emerging concept reveals implications in viral pathogenesis, as well as, the promise for cell-targeted therapeutic strategies to block universal virus uncoating pathways hijacked by enveloped RNA viruses.</div>
</front>
</TEI>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
</list>
<tree><country name="Royaume-Uni"><noRegion><name sortKey="Yamauchi, Yohei" sort="Yamauchi, Yohei" uniqKey="Yamauchi Y" first="Yohei" last="Yamauchi">Yohei Yamauchi</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/StressCovidV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000421 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000421 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= StressCovidV1 |flux= Main |étape= Exploration |type= RBID |clé= pubmed:32327145 |texte= Influenza A virus uncoating. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:32327145" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \ | NlmPubMed2Wicri -a StressCovidV1
This area was generated with Dilib version V0.6.33. |