SrasV1, Main, Exploration, bibRecord, 000B38

GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.

Identifieur interne : 000B38 ( Main/Exploration ); précédent : 000B37; suivant : 000B39

GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.

Auteurs : Danying Chen [République populaire de Chine] ; Zhifei Hou [République populaire de Chine] ; Dong Jiang [République populaire de Chine] ; Mei Zheng [République populaire de Chine] ; Guoli Li [République populaire de Chine] ; Yue Zhang [République populaire de Chine] ; Rui Li [République populaire de Chine] ; Hanxin Lin [Canada] ; Jinhong Chang [États-Unis] ; Hui Zeng [République populaire de Chine] ; Ju-Tao Guo [États-Unis] ; Xuesen Zhao [République populaire de Chine]

Source :

Emerging microbes & infections [ 2222-1751 ] ; 2019.

RBID : pubmed:31631785

Descripteurs français

English descriptors

KwdEn :
- Cathepsin L (genetics), Cathepsin L (immunology), Cell Line, Ebolavirus (genetics), Ebolavirus (physiology), Hemorrhagic Fever, Ebola (genetics), Hemorrhagic Fever, Ebola (immunology), Hemorrhagic Fever, Ebola (virology), Humans, Lassa Fever (genetics), Lassa Fever (immunology), Lassa Fever (virology), Lassa virus (genetics), Lassa virus (physiology), Lysosomes (genetics), Lysosomes (immunology), Lysosomes (virology), Oxidoreductases Acting on Sulfur Group Donors (genetics), Oxidoreductases Acting on Sulfur Group Donors (immunology), SARS Virus (genetics), SARS Virus (physiology), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (virology), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Internalization, Virus Replication.
MESH :
- chemical , genetics : Cathepsin L, Oxidoreductases Acting on Sulfur Group Donors, Viral Envelope Proteins.
- chemical , immunology : Cathepsin L, Oxidoreductases Acting on Sulfur Group Donors.
- genetics : Ebolavirus, Hemorrhagic Fever, Ebola, Lassa Fever, Lassa virus, Lysosomes, SARS Virus, Severe Acute Respiratory Syndrome.
- immunology : Hemorrhagic Fever, Ebola, Lassa Fever, Lysosomes, Severe Acute Respiratory Syndrome.
- chemical , metabolism : Viral Envelope Proteins.
- physiology : Ebolavirus, Lassa virus, SARS Virus.
- virology : Hemorrhagic Fever, Ebola, Lassa Fever, Lysosomes, Severe Acute Respiratory Syndrome.
- Cell Line, Humans, Virus Internalization, Virus Replication.

Abstract

Interferons (IFNs) control viral infections by inducing expression of IFN-stimulated genes (ISGs) that restrict distinct steps of viral replication. We report herein that gamma-interferon-inducible lysosomal thiol reductase (GILT), a lysosome-associated ISG, restricts the infectious entry of selected enveloped RNA viruses. Specifically, we demonstrated that GILT was constitutively expressed in lung epithelial cells and fibroblasts and its expression could be further induced by type II interferon. While overexpression of GILT inhibited the entry mediated by envelope glycoproteins of SARS coronavirus (SARS-CoV), Ebola virus (EBOV) and Lassa fever virus (LASV), depletion of GILT enhanced the entry mediated by these viral envelope glycoproteins. Furthermore, mutations that impaired the thiol reductase activity or disrupted the N-linked glycosylation, a posttranslational modification essential for its lysosomal localization, largely compromised GILT restriction of viral entry. We also found that the induction of GILT expression reduced the level and activity of cathepsin L, which is required for the entry of these RNA viruses in lysosomes. Our data indicate that GILT is a novel antiviral ISG that specifically inhibits the entry of selected enveloped RNA viruses in lysosomes via disruption of cathepsin L metabolism and function and may play a role in immune control and pathogenesis of these viruses.

DOI: 10.1080/22221751.2019.1677446
PubMed: 31631785

Affiliations:

Le document en format XML

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<author><name sortKey="Chang, Jinhong" sort="Chang, Jinhong" uniqKey="Chang J" first="Jinhong" last="Chang">Jinhong Chang</name>
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<author><name sortKey="Chang, Jinhong" sort="Chang, Jinhong" uniqKey="Chang J" first="Jinhong" last="Chang">Jinhong Chang</name>
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<author><name sortKey="Zeng, Hui" sort="Zeng, Hui" uniqKey="Zeng H" first="Hui" last="Zeng">Hui Zeng</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Guo, Ju Tao" sort="Guo, Ju Tao" uniqKey="Guo J" first="Ju-Tao" last="Guo">Ju-Tao Guo</name>
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<author><name sortKey="Zhao, Xuesen" sort="Zhao, Xuesen" uniqKey="Zhao X" first="Xuesen" last="Zhao">Xuesen Zhao</name>
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<term>Syndrome respiratoire aigu sévère</term>
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<term>Virus Replication</term>
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<term>Pénétration virale</term>
<term>Réplication virale</term>
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<front><div type="abstract" xml:lang="en">Interferons (IFNs) control viral infections by inducing expression of IFN-stimulated genes (ISGs) that restrict distinct steps of viral replication. We report herein that gamma-interferon-inducible lysosomal thiol reductase (GILT), a lysosome-associated ISG, restricts the infectious entry of selected enveloped RNA viruses. Specifically, we demonstrated that GILT was constitutively expressed in lung epithelial cells and fibroblasts and its expression could be further induced by type II interferon. While overexpression of GILT inhibited the entry mediated by envelope glycoproteins of SARS coronavirus (SARS-CoV), Ebola virus (EBOV) and Lassa fever virus (LASV), depletion of GILT enhanced the entry mediated by these viral envelope glycoproteins. Furthermore, mutations that impaired the thiol reductase activity or disrupted the N-linked glycosylation, a posttranslational modification essential for its lysosomal localization, largely compromised GILT restriction of viral entry. We also found that the induction of GILT expression reduced the level and activity of cathepsin L, which is required for the entry of these RNA viruses in lysosomes. Our data indicate that GILT is a novel antiviral ISG that specifically inhibits the entry of selected enveloped RNA viruses in lysosomes <i>via</i>
 disruption of cathepsin L metabolism and function and may play a role in immune control and pathogenesis of these viruses.</div>
</front>
</TEI>
<affiliations><list><country><li>Canada</li>
<li>République populaire de Chine</li>
<li>États-Unis</li>
</country>
<region><li>Pennsylvanie</li>
</region>
</list>
<tree><country name="République populaire de Chine"><noRegion><name sortKey="Chen, Danying" sort="Chen, Danying" uniqKey="Chen D" first="Danying" last="Chen">Danying Chen</name>
</noRegion>
<name sortKey="Hou, Zhifei" sort="Hou, Zhifei" uniqKey="Hou Z" first="Zhifei" last="Hou">Zhifei Hou</name>
<name sortKey="Jiang, Dong" sort="Jiang, Dong" uniqKey="Jiang D" first="Dong" last="Jiang">Dong Jiang</name>
<name sortKey="Li, Guoli" sort="Li, Guoli" uniqKey="Li G" first="Guoli" last="Li">Guoli Li</name>
<name sortKey="Li, Rui" sort="Li, Rui" uniqKey="Li R" first="Rui" last="Li">Rui Li</name>
<name sortKey="Zeng, Hui" sort="Zeng, Hui" uniqKey="Zeng H" first="Hui" last="Zeng">Hui Zeng</name>
<name sortKey="Zhang, Yue" sort="Zhang, Yue" uniqKey="Zhang Y" first="Yue" last="Zhang">Yue Zhang</name>
<name sortKey="Zhao, Xuesen" sort="Zhao, Xuesen" uniqKey="Zhao X" first="Xuesen" last="Zhao">Xuesen Zhao</name>
<name sortKey="Zheng, Mei" sort="Zheng, Mei" uniqKey="Zheng M" first="Mei" last="Zheng">Mei Zheng</name>
</country>
<country name="Canada"><noRegion><name sortKey="Lin, Hanxin" sort="Lin, Hanxin" uniqKey="Lin H" first="Hanxin" last="Lin">Hanxin Lin</name>
</noRegion>
</country>
<country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Chang, Jinhong" sort="Chang, Jinhong" uniqKey="Chang J" first="Jinhong" last="Chang">Jinhong Chang</name>
</region>
<name sortKey="Guo, Ju Tao" sort="Guo, Ju Tao" uniqKey="Guo J" first="Ju-Tao" last="Guo">Ju-Tao Guo</name>
</country>
</tree>
</affiliations>
</record>

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GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.

GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.

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