GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.
Identifieur interne : 000865 ( PubMed/Corpus ); précédent : 000864; suivant : 000866GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.
Auteurs : Danying Chen ; Zhifei Hou ; Dong Jiang ; Mei Zheng ; Guoli Li ; Yue Zhang ; Rui Li ; Hanxin Lin ; Jinhong Chang ; Hui Zeng ; Ju-Tao Guo ; Xuesen ZhaoSource :
- Emerging microbes & infections [ 2222-1751 ] ; 2019.
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
Links to Exploration step
pubmed:31631785Le document en format XML
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<term>Ebolavirus (physiology)</term>
<term>Hemorrhagic Fever, Ebola (genetics)</term>
<term>Hemorrhagic Fever, Ebola (immunology)</term>
<term>Hemorrhagic Fever, Ebola (virology)</term>
<term>Humans</term>
<term>Lassa Fever (genetics)</term>
<term>Lassa Fever (immunology)</term>
<term>Lassa Fever (virology)</term>
<term>Lassa virus (genetics)</term>
<term>Lassa virus (physiology)</term>
<term>Lysosomes (genetics)</term>
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<term>Oxidoreductases Acting on Sulfur Group Donors (genetics)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (immunology)</term>
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<term>SARS Virus (physiology)</term>
<term>Severe Acute Respiratory Syndrome (genetics)</term>
<term>Severe Acute Respiratory Syndrome (immunology)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Virus Internalization</term>
<term>Virus Replication</term>
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<term>Viral Envelope Proteins</term>
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<term>Hemorrhagic Fever, Ebola</term>
<term>Lassa Fever</term>
<term>Lassa virus</term>
<term>Lysosomes</term>
<term>SARS Virus</term>
<term>Severe Acute Respiratory Syndrome</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>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31631785</PMID>
<DateCompleted><Year>2020</Year>
<Month>01</Month>
<Day>15</Day>
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<DateRevised><Year>2020</Year>
<Month>01</Month>
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<Issue>1</Issue>
<PubDate><Year>2019</Year>
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<Title>Emerging microbes & infections</Title>
<ISOAbbreviation>Emerg Microbes Infect</ISOAbbreviation>
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<ArticleTitle>GILT restricts the cellular entry mediated by the envelope glycoproteins of SARS-CoV, Ebola virus and Lassa fever virus.</ArticleTitle>
<Pagination><MedlinePgn>1511-1523</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1080/22221751.2019.1677446</ELocationID>
<Abstract><AbstractText>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.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Danying</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Institute of Infectious disease, Beijing Ditan Hospital, Capital Medical University , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hou</LastName>
<ForeName>Zhifei</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Institute of Infectious disease, Beijing Ditan Hospital, Capital Medical University , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Pulmonary and Critical Care Medicine, General Hospital of Datong Coal Mine Group Co., Ltd. , People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jiang</LastName>
<ForeName>Dong</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Institute of Infectious disease, Beijing Ditan Hospital, Capital Medical University , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Zheng</LastName>
<ForeName>Mei</ForeName>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
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<Author ValidYN="Y"><LastName>Li</LastName>
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<Initials>G</Initials>
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<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
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<ForeName>Rui</ForeName>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lin</LastName>
<ForeName>Hanxin</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, Western University , London , Ontario , Canada.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chang</LastName>
<ForeName>Jinhong</ForeName>
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<Author ValidYN="Y"><LastName>Zeng</LastName>
<ForeName>Hui</ForeName>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
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<Author ValidYN="Y"><LastName>Guo</LastName>
<ForeName>Ju-Tao</ForeName>
<Initials>JT</Initials>
<AffiliationInfo><Affiliation>Baruch S. Blumberg Institute, Hepatitis B Foundation , Doylestown , PA , USA.</Affiliation>
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<Author ValidYN="Y"><LastName>Zhao</LastName>
<ForeName>Xuesen</ForeName>
<Initials>X</Initials>
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<AffiliationInfo><Affiliation>Institute of Infectious disease, Beijing Ditan Hospital, Capital Medical University , Beijing , People's Republic of China.</Affiliation>
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<AffiliationInfo><Affiliation>Beijing Key Laboratory of Emerging Infectious Disease , Beijing , People's Republic of China.</Affiliation>
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