Coronavirus Cell Entry Occurs through the Endo-/Lysosomal Pathway in a Proteolysis-Dependent Manner
Identifieur interne : 001D09 ( Main/Exploration ); précédent : 001D08; suivant : 001D10Coronavirus Cell Entry Occurs through the Endo-/Lysosomal Pathway in a Proteolysis-Dependent Manner
Auteurs : Christine Burkard [Pays-Bas] ; Monique H. Verheije [Pays-Bas] ; Oliver Wicht [Pays-Bas] ; Sander I. Van Kasteren [Pays-Bas] ; Frank J. Van Kuppeveld [Pays-Bas] ; Bart L. Haagmans [Pays-Bas] ; Lucas Pelkmans [Suisse] ; Peter J. M. Rottier [Pays-Bas] ; Berend Jan Bosch [Pays-Bas] ; Cornelis A. M. De Haan [Pays-Bas]Source :
- PLoS Pathogens [ 1553-7366 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Cellules HeLa, Cellules Vero, Cellules rénales canines Madin-Darby, Chats, Chiens, Endosomes (métabolisme), Endosomes (virologie), Fusion membranaire, Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Lysosomes (métabolisme), Lysosomes (virologie), Protéolyse, Pénétration virale, Souris, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (métabolisme).
- MESH :
- génétique : Glycoprotéine de spicule des coronavirus, Virus de l'hépatite murine.
- métabolisme : Endosomes, Glycoprotéine de spicule des coronavirus, Lysosomes, Virus de l'hépatite murine.
- virologie : Endosomes, Lysosomes.
- Animaux, Cellules HeLa, Cellules Vero, Cellules rénales canines Madin-Darby, Chats, Chiens, Fusion membranaire, Humains, Protéolyse, Pénétration virale, Souris.
English descriptors
- KwdEn :
- Animals, Cats, Chlorocebus aethiops, Dogs, Endosomes (metabolism), Endosomes (virology), HeLa Cells, Humans, Lysosomes (metabolism), Lysosomes (virology), Madin Darby Canine Kidney Cells, Membrane Fusion, Mice, Murine hepatitis virus (genetics), Murine hepatitis virus (metabolism), Proteolysis, Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Vero Cells, Virus Internalization.
- MESH :
- chemical , genetics : Spike Glycoprotein, Coronavirus.
- genetics : Murine hepatitis virus.
- metabolism : Endosomes, Lysosomes, Murine hepatitis virus, Spike Glycoprotein, Coronavirus.
- virology : Endosomes, Lysosomes.
- Animals, Cats, Chlorocebus aethiops, Dogs, HeLa Cells, Humans, Madin Darby Canine Kidney Cells, Membrane Fusion, Mice, Proteolysis, Vero Cells, Virus Internalization.
Abstract
Enveloped viruses need to fuse with a host cell membrane in order to deliver their genome into the host cell. While some viruses fuse with the plasma membrane, many viruses are endocytosed prior to fusion. Specific cues in the endosomal microenvironment induce conformational changes in the viral fusion proteins leading to viral and host membrane fusion. In the present study we investigated the entry of coronaviruses (CoVs). Using siRNA gene silencing, we found that proteins known to be important for late endosomal maturation and endosome-lysosome fusion profoundly promote infection of cells with mouse hepatitis coronavirus (MHV). Using recombinant MHVs expressing reporter genes as well as a novel, replication-independent fusion assay we confirmed the importance of clathrin-mediated endocytosis and demonstrated that trafficking of MHV to lysosomes is required for fusion and productive entry to occur. Nevertheless, MHV was shown to be less sensitive to perturbation of endosomal pH than vesicular stomatitis virus and influenza A virus, which fuse in early and late endosomes, respectively. Our results indicate that entry of MHV depends on proteolytic processing of its fusion protein S by lysosomal proteases. Fusion of MHV was severely inhibited by a pan-lysosomal protease inhibitor, while trafficking of MHV to lysosomes and processing by lysosomal proteases was no longer required when a furin cleavage site was introduced in the S protein immediately upstream of the fusion peptide. Also entry of feline CoV was shown to depend on trafficking to lysosomes and processing by lysosomal proteases. In contrast, MERS-CoV, which contains a minimal furin cleavage site just upstream of the fusion peptide, was negatively affected by inhibition of furin, but not of lysosomal proteases. We conclude that a proteolytic cleavage site in the CoV S protein directly upstream of the fusion peptide is an essential determinant of the intracellular site of fusion.
Url:
DOI: 10.1371/journal.ppat.1004502
PubMed: 25375324
PubMed Central: 4223067
Affiliations:
- Pays-Bas, Suisse
- Canton de Zurich, Hollande-Méridionale, Utrecht (province)
- Leyde, Rotterdam, Utrecht, Zurich
- Université d'Utrecht, Université de Zurich
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Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Cats</term>
<term>Chlorocebus aethiops</term>
<term>Dogs</term>
<term>Endosomes (metabolism)</term>
<term>Endosomes (virology)</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Lysosomes (metabolism)</term>
<term>Lysosomes (virology)</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Murine hepatitis virus (genetics)</term>
<term>Murine hepatitis virus (metabolism)</term>
<term>Proteolysis</term>
<term>Spike Glycoprotein, Coronavirus (genetics)</term>
<term>Spike Glycoprotein, Coronavirus (metabolism)</term>
<term>Vero Cells</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cellules HeLa</term>
<term>Cellules Vero</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chats</term>
<term>Chiens</term>
<term>Endosomes (métabolisme)</term>
<term>Endosomes (virologie)</term>
<term>Fusion membranaire</term>
<term>Glycoprotéine de spicule des coronavirus (génétique)</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Humains</term>
<term>Lysosomes (métabolisme)</term>
<term>Lysosomes (virologie)</term>
<term>Protéolyse</term>
<term>Pénétration virale</term>
<term>Souris</term>
<term>Virus de l'hépatite murine (génétique)</term>
<term>Virus de l'hépatite murine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Virus de l'hépatite murine</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endosomes</term>
<term>Lysosomes</term>
<term>Murine hepatitis virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endosomes</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Lysosomes</term>
<term>Virus de l'hépatite murine</term>
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<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Endosomes</term>
<term>Lysosomes</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Endosomes</term>
<term>Lysosomes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cats</term>
<term>Chlorocebus aethiops</term>
<term>Dogs</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Madin Darby Canine Kidney Cells</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Proteolysis</term>
<term>Vero Cells</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules HeLa</term>
<term>Cellules Vero</term>
<term>Cellules rénales canines Madin-Darby</term>
<term>Chats</term>
<term>Chiens</term>
<term>Fusion membranaire</term>
<term>Humains</term>
<term>Protéolyse</term>
<term>Pénétration virale</term>
<term>Souris</term>
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<front><div type="abstract" xml:lang="en"><p>Enveloped viruses need to fuse with a host cell membrane in order to deliver their genome into the host cell. While some viruses fuse with the plasma membrane, many viruses are endocytosed prior to fusion. Specific cues in the endosomal microenvironment induce conformational changes in the viral fusion proteins leading to viral and host membrane fusion. In the present study we investigated the entry of coronaviruses (CoVs). Using siRNA gene silencing, we found that proteins known to be important for late endosomal maturation and endosome-lysosome fusion profoundly promote infection of cells with mouse hepatitis coronavirus (MHV). Using recombinant MHVs expressing reporter genes as well as a novel, replication-independent fusion assay we confirmed the importance of clathrin-mediated endocytosis and demonstrated that trafficking of MHV to lysosomes is required for fusion and productive entry to occur. Nevertheless, MHV was shown to be less sensitive to perturbation of endosomal pH than vesicular stomatitis virus and influenza A virus, which fuse in early and late endosomes, respectively. Our results indicate that entry of MHV depends on proteolytic processing of its fusion protein S by lysosomal proteases. Fusion of MHV was severely inhibited by a pan-lysosomal protease inhibitor, while trafficking of MHV to lysosomes and processing by lysosomal proteases was no longer required when a furin cleavage site was introduced in the S protein immediately upstream of the fusion peptide. Also entry of feline CoV was shown to depend on trafficking to lysosomes and processing by lysosomal proteases. In contrast, MERS-CoV, which contains a minimal furin cleavage site just upstream of the fusion peptide, was negatively affected by inhibition of furin, but not of lysosomal proteases. We conclude that a proteolytic cleavage site in the CoV S protein directly upstream of the fusion peptide is an essential determinant of the intracellular site of fusion.</p>
</div>
</front>
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</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="De Haan, Ca" uniqKey="De Haan C">CA de Haan</name>
</author>
<author><name sortKey="Haijema, Bj" uniqKey="Haijema B">BJ Haijema</name>
</author>
<author><name sortKey="Masters, Ps" uniqKey="Masters P">PS Masters</name>
</author>
<author><name sortKey="Rottier, Pj" uniqKey="Rottier P">PJ Rottier</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Kuo, L" uniqKey="Kuo L">L Kuo</name>
</author>
<author><name sortKey="Godeke, Gj" uniqKey="Godeke G">GJ Godeke</name>
</author>
<author><name sortKey="Raamsman, Mj" uniqKey="Raamsman M">MJ Raamsman</name>
</author>
<author><name sortKey="Masters, Ps" uniqKey="Masters P">PS Masters</name>
</author>
<author><name sortKey="Rottier, Pj" uniqKey="Rottier P">PJ Rottier</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Vonderheit, A" uniqKey="Vonderheit A">A Vonderheit</name>
</author>
<author><name sortKey="Helenius, A" uniqKey="Helenius A">A Helenius</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Schulze, H" uniqKey="Schulze H">H Schulze</name>
</author>
<author><name sortKey="Kolter, T" uniqKey="Kolter T">T Kolter</name>
</author>
<author><name sortKey="Sandhoff, K" uniqKey="Sandhoff K">K Sandhoff</name>
</author>
</analytic>
</biblStruct>
</listBibl>
</div1>
</back>
</TEI>
<affiliations><list><country><li>Pays-Bas</li>
<li>Suisse</li>
</country>
<region><li>Canton de Zurich</li>
<li>Hollande-Méridionale</li>
<li>Utrecht (province)</li>
</region>
<settlement><li>Leyde</li>
<li>Rotterdam</li>
<li>Utrecht</li>
<li>Zurich</li>
</settlement>
<orgName><li>Université d'Utrecht</li>
<li>Université de Zurich</li>
</orgName>
</list>
<tree><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Burkard, Christine" sort="Burkard, Christine" uniqKey="Burkard C" first="Christine" last="Burkard">Christine Burkard</name>
</region>
<name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name>
<name sortKey="De Haan, Cornelis A M" sort="De Haan, Cornelis A M" uniqKey="De Haan C" first="Cornelis A. M." last="De Haan">Cornelis A. M. De Haan</name>
<name sortKey="Haagmans, Bart L" sort="Haagmans, Bart L" uniqKey="Haagmans B" first="Bart L." last="Haagmans">Bart L. Haagmans</name>
<name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J. M." last="Rottier">Peter J. M. Rottier</name>
<name sortKey="Van Kasteren, Sander I" sort="Van Kasteren, Sander I" uniqKey="Van Kasteren S" first="Sander I." last="Van Kasteren">Sander I. Van Kasteren</name>
<name sortKey="Van Kuppeveld, Frank J" sort="Van Kuppeveld, Frank J" uniqKey="Van Kuppeveld F" first="Frank J." last="Van Kuppeveld">Frank J. Van Kuppeveld</name>
<name sortKey="Verheije, Monique H" sort="Verheije, Monique H" uniqKey="Verheije M" first="Monique H." last="Verheije">Monique H. Verheije</name>
<name sortKey="Wicht, Oliver" sort="Wicht, Oliver" uniqKey="Wicht O" first="Oliver" last="Wicht">Oliver Wicht</name>
</country>
<country name="Suisse"><region name="Canton de Zurich"><name sortKey="Pelkmans, Lucas" sort="Pelkmans, Lucas" uniqKey="Pelkmans L" first="Lucas" last="Pelkmans">Lucas Pelkmans</name>
</region>
</country>
</tree>
</affiliations>
</record>
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