SrasV1, PubMed, Checkpoint, bibRecord, 001813

Protease-mediated entry via the endosome of human coronavirus 229E.

Identifieur interne : 001813 ( PubMed/Checkpoint ); précédent : 001812; suivant : 001814

Protease-mediated entry via the endosome of human coronavirus 229E.

Auteurs : Miyuki Kawase [Japon] ; Kazuya Shirato ; Shutoku Matsuyama ; Fumihiro Taguchi

Source :

Journal of virology [ 1098-5514 ] ; 2009.

RBID : pubmed:18971274

Descripteurs français

KwdFr :
- Cathepsine L, Cathepsines (antagonistes et inhibiteurs), Cathepsines (métabolisme), Cellules HeLa, Concentration en ions d'hydrogène, Coronavirus humain 229E (physiologie), Cysteine endopeptidases (métabolisme), Endosomes (virologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Méthode des plages virales, Peptide hydrolases (métabolisme), Petit ARN interférent (génétique), Petit ARN interférent (métabolisme), Protéines de l'enveloppe virale (métabolisme), Pénétration virale, Techniques de knock-down de gènes, Virus de l'hépatite murine (physiologie), Virus du SRAS (physiologie).
MESH :
- antagonistes et inhibiteurs : Cathepsines.
- génétique : Petit ARN interférent.
- métabolisme : Cathepsines, Cysteine endopeptidases, Glycoprotéines membranaires, Peptide hydrolases, Petit ARN interférent, Protéines de l'enveloppe virale.
- physiologie : Coronavirus humain 229E, Virus de l'hépatite murine, Virus du SRAS.
- virologie : Endosomes.
- Cathepsine L, Cellules HeLa, Concentration en ions d'hydrogène, Glycoprotéine de spicule des coronavirus, Humains, Méthode des plages virales, Pénétration virale, Techniques de knock-down de gènes.

English descriptors

KwdEn :
- Cathepsin L, Cathepsins (antagonists & inhibitors), Cathepsins (metabolism), Coronavirus 229E, Human (physiology), Cysteine Endopeptidases (metabolism), Endosomes (virology), Gene Knockdown Techniques, HeLa Cells, Humans, Hydrogen-Ion Concentration, Membrane Glycoproteins (metabolism), Murine hepatitis virus (physiology), Peptide Hydrolases (metabolism), RNA, Small Interfering (genetics), RNA, Small Interfering (metabolism), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Viral Plaque Assay, Virus Internalization.
MESH :
- chemical , antagonists & inhibitors : Cathepsins.
- chemical , genetics : RNA, Small Interfering.
- chemical , metabolism : Cathepsins, Cysteine Endopeptidases, Membrane Glycoproteins, Peptide Hydrolases, RNA, Small Interfering, Viral Envelope Proteins.
- chemical : Cathepsin L, Spike Glycoprotein, Coronavirus.
- physiology : Coronavirus 229E, Human, Murine hepatitis virus, SARS Virus.
- virology : Endosomes.
- Gene Knockdown Techniques, HeLa Cells, Humans, Hydrogen-Ion Concentration, Viral Plaque Assay, Virus Internalization.

Abstract

Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry.

DOI: 10.1128/JVI.01933-08
PubMed: 18971274

Affiliations:

Links toward previous steps (curation, corpus...)

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pubmed:18971274

Le document en format XML

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<front><div type="abstract" xml:lang="en">Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry.</div>
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<Abstract><AbstractText>Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry.</AbstractText>
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Protease-mediated entry via the endosome of human coronavirus 229E.

Protease-mediated entry via the endosome of human coronavirus 229E.

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