MersV1, Main, Exploration, bibRecord, 000896

Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.

Identifieur interne : 000896 ( Main/Exploration ); précédent : 000895; suivant : 000897

Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.

Auteurs : Shutoku Matsuyama [Japon] ; Kazuya Shirato [Japon] ; Miyuki Kawase [Japon] ; Yutaka Terada [Japon] ; Kengo Kawachi [Japon] ; Shuetsu Fukushi [Japon] ; Wataru Kamitani [Japon]

Source :

Journal of virology [ 1098-5514 ] ; 2018.

RBID : pubmed:30021905

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Chloromethyl Ketones (pharmacology), Animals, Cathepsin B (antagonists & inhibitors), Cathepsin B (genetics), Cathepsin B (metabolism), Cathepsin L (antagonists & inhibitors), Cathepsin L (genetics), Cathepsin L (metabolism), Chlorocebus aethiops, Furin (antagonists & inhibitors), Furin (genetics), Furin (metabolism), Humans, Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Papain (antagonists & inhibitors), Papain (genetics), Papain (metabolism), Proteolysis, Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Vero Cells, Virus Internalization.
MESH :
- chemical , antagonists & inhibitors : Cathepsin B, Cathepsin L, Furin, Papain.
- chemical , genetics : Cathepsin B, Cathepsin L, Furin, Papain, Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Cathepsin B, Cathepsin L, Furin, Papain, Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Amino Acid Chloromethyl Ketones.
- genetics : Middle East Respiratory Syndrome Coronavirus.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- Animals, Chlorocebus aethiops, Humans, Proteolysis, Vero Cells, Virus Internalization.

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes host cellular proteases to enter cells. A previous report shows that furin, which is distributed mainly in the Golgi apparatus and cycled to the cell surface and endosomes, proteolytically activates the MERS-CoV spike (S) protein following receptor binding to mediate fusion between the viral and cellular membranes. In this study, we reexamined furin usage by MERS-CoV using a real-time PCR-based virus cell entry assay after inhibition of cellular proteases. We found that the furin inhibitor dec-RVKR-CMK blocked entry of MERS-CoV harboring an S protein lacking furin cleavage sites; it even blocked entry into furin-deficient LoVo cells. In addition, dec-RVKR-CMK inhibited not only the enzymatic activity of furin but also those of cathepsin L, cathepsin B, trypsin, papain, and TMPRSS2. Furthermore, a virus cell entry assay and a cell-cell fusion assay provided no evidence that the S protein was activated by exogenous furin. Therefore, we conclude that furin does not play a role in entry of MERS-CoV into cells and that the inhibitory effect of dec-RVKR-CMK is specific for TMPRSS2 and cathepsin L rather than furin.IMPORTANCE Previous studies using the furin inhibitor dec-RVKR-CMK suggest that MERS-CoV utilizes a cellular protease, furin, to activate viral glycoproteins during cell entry. However, we found that dec-RVKR-CMK inhibits not only furin but also other proteases. Furthermore, we found no evidence that MERS-CoV uses furin. These findings suggest that previous studies in the virology field based on dec-RVKR-CMK should be reexamined carefully. Here we describe appropriate experiments that can be used to assess the effect of protease inhibitors on virus cell entry.

DOI: 10.1128/JVI.00683-18
PubMed: 30021905

Affiliations:

Le document en format XML

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<term>Cathepsin B (antagonists & inhibitors)</term>
<term>Cathepsin B (genetics)</term>
<term>Cathepsin B (metabolism)</term>
<term>Cathepsin L (antagonists & inhibitors)</term>
<term>Cathepsin L (genetics)</term>
<term>Cathepsin L (metabolism)</term>
<term>Chlorocebus aethiops</term>
<term>Furin (antagonists & inhibitors)</term>
<term>Furin (genetics)</term>
<term>Furin (metabolism)</term>
<term>Humans</term>
<term>Middle East Respiratory Syndrome Coronavirus (genetics)</term>
<term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term>
<term>Papain (antagonists & inhibitors)</term>
<term>Papain (genetics)</term>
<term>Papain (metabolism)</term>
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<term>Serine Endopeptidases (metabolism)</term>
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<term>Cathepsine L (génétique)</term>
<term>Cathepsine L (métabolisme)</term>
<term>Cellules Vero</term>
<term>Chlorométhyl cétones d'acides aminés (pharmacologie)</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient (génétique)</term>
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<term>Serine Endopeptidases</term>
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<term>Papain</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Papaïne</term>
<term>Serine endopeptidases</term>
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<term>Chlorocebus aethiops</term>
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<term>Vero Cells</term>
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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) utilizes host cellular proteases to enter cells. A previous report shows that furin, which is distributed mainly in the Golgi apparatus and cycled to the cell surface and endosomes, proteolytically activates the MERS-CoV spike (S) protein following receptor binding to mediate fusion between the viral and cellular membranes. In this study, we reexamined furin usage by MERS-CoV using a real-time PCR-based virus cell entry assay after inhibition of cellular proteases. We found that the furin inhibitor dec-RVKR-CMK blocked entry of MERS-CoV harboring an S protein lacking furin cleavage sites; it even blocked entry into furin-deficient LoVo cells. In addition, dec-RVKR-CMK inhibited not only the enzymatic activity of furin but also those of cathepsin L, cathepsin B, trypsin, papain, and TMPRSS2. Furthermore, a virus cell entry assay and a cell-cell fusion assay provided no evidence that the S protein was activated by exogenous furin. Therefore, we conclude that furin does not play a role in entry of MERS-CoV into cells and that the inhibitory effect of dec-RVKR-CMK is specific for TMPRSS2 and cathepsin L rather than furin.<b>IMPORTANCE</b>
 Previous studies using the furin inhibitor dec-RVKR-CMK suggest that MERS-CoV utilizes a cellular protease, furin, to activate viral glycoproteins during cell entry. However, we found that dec-RVKR-CMK inhibits not only furin but also other proteases. Furthermore, we found no evidence that MERS-CoV uses furin. These findings suggest that previous studies in the virology field based on dec-RVKR-CMK should be reexamined carefully. Here we describe appropriate experiments that can be used to assess the effect of protease inhibitors on virus cell entry.</div>
</front>
</TEI>
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<name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name>
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Serveur d'exploration MERS

Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.

Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.

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