Inhibition of Proprotein Convertases Abrogates Processing of the Middle Eastern Respiratory Syndrome Coronavirus Spike Protein in Infected Cells but Does Not Reduce Viral Infectivity
Identifieur interne : 001C19 ( Main/Exploration ); précédent : 001C18; suivant : 001C20Inhibition of Proprotein Convertases Abrogates Processing of the Middle Eastern Respiratory Syndrome Coronavirus Spike Protein in Infected Cells but Does Not Reduce Viral Infectivity
Auteurs : Stefanie Gierer ; Marcel A. Müller ; Adeline Heurich ; Daniel Ritz ; Benjamin L. Springstein ; Christina B. Karsten [Allemagne] ; Alexander Schendzielorz ; Kerstin Gnir ; Christian Drosten ; Stefan PöhlmannSource :
- The Journal of Infectious Diseases [ 0022-1899 ] ; 2014.
Descripteurs français
- KwdFr :
- Antiviraux (pharmacologie), Cellules HEK293, Coronavirus (physiologie), Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Inhibiteurs de protéases (pharmacologie), Maturation post-traductionnelle des protéines, Proprotein convertases (antagonistes et inhibiteurs), Protéolyse, Pénétration virale, Séquence d'acides aminés, Évaluation préclinique de médicament.
- MESH :
- antagonistes et inhibiteurs : Proprotein convertases.
- métabolisme : Glycoprotéine de spicule des coronavirus.
- pharmacologie : Antiviraux, Inhibiteurs de protéases.
- physiologie : Coronavirus.
- Cellules HEK293, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Humains, Maturation post-traductionnelle des protéines, Protéolyse, Pénétration virale, Séquence d'acides aminés, Évaluation préclinique de médicament.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antiviral Agents (pharmacology), Coronavirus (physiology), Drug Evaluation, Preclinical, HEK293 Cells, Humans, Molecular Sequence Data, Proprotein Convertases (antagonists & inhibitors), Protease Inhibitors (pharmacology), Protein Processing, Post-Translational, Proteolysis, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization.
- MESH :
- chemical , antagonists & inhibitors : Proprotein Convertases.
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Antiviral Agents, Protease Inhibitors.
- physiology : Coronavirus.
- Amino Acid Sequence, Drug Evaluation, Preclinical, HEK293 Cells, Humans, Molecular Sequence Data, Protein Processing, Post-Translational, Proteolysis, Virus Internalization.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) infection is associated with a high case-fatality rate, and the potential pandemic spread of the virus is a public health concern. The spike protein of MERS-CoV (MERS-S) facilitates viral entry into host cells, which depends on activation of MERS-S by cellular proteases. Proteolytic activation of MERS-S during viral uptake into target cells has been demonstrated. However, it is unclear whether MERS-S is also cleaved during S protein synthesis in infected cells and whether cleavage is required for MERS-CoV infectivity. Here, we show that MERS-S is processed by proprotein convertases in MERS-S–transfected and MERS-CoV–infected cells and that several RXXR motifs located at the border between the surface and transmembrane subunit of MERS-S are required for efficient proteolysis. However, blockade of proprotein convertases did not impact MERS-S–dependent transduction of target cells expressing high amounts of the viral receptor, DPP4, and did not modulate MERS-CoV infectivity. These results show that MERS-S is a substrate for proprotein convertases and demonstrate that processing by these enzymes is dispensable for S protein activation. Efforts to inhibit MERS-CoV infection by targeting host cell proteases should therefore focus on enzymes that process MERS-S during viral uptake into target cells.
Url:
DOI: 10.1093/infdis/jiu407
PubMed: 25057042
PubMed Central: 7107327
Affiliations:
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Le document en format XML
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Müller</name><affiliation><nlm:aff id="af2"><addr-line>Institute of Virology</addr-line>,<institution>University of Bonn Medical Center</institution></nlm:aff></affiliation></author><author><name sortKey="Heurich, Adeline" sort="Heurich, Adeline" uniqKey="Heurich A" first="Adeline" last="Heurich">Adeline Heurich</name><affiliation><nlm:aff id="af1"><addr-line>Infection Biology Unit</addr-line>,<institution>German Primate Center</institution>,<addr-line>Göttingen</addr-line></nlm:aff></affiliation></author><author><name sortKey="Ritz, Daniel" sort="Ritz, Daniel" uniqKey="Ritz D" first="Daniel" last="Ritz">Daniel Ritz</name><affiliation><nlm:aff id="af2"><addr-line>Institute of Virology</addr-line>,<institution>University of Bonn Medical Center</institution></nlm:aff></affiliation></author><author><name sortKey="Springstein, Benjamin L" sort="Springstein, Benjamin L" uniqKey="Springstein B" first="Benjamin L." last="Springstein">Benjamin L. Springstein</name><affiliation><nlm:aff id="af1"><addr-line>Infection Biology Unit</addr-line>,<institution>German Primate Center</institution>,<addr-line>Göttingen</addr-line></nlm:aff></affiliation></author><author><name sortKey="Karsten, Christina B" sort="Karsten, Christina B" uniqKey="Karsten C" first="Christina B." last="Karsten">Christina B. 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Gnir</name><affiliation><nlm:aff id="af1"><addr-line>Infection Biology Unit</addr-line>,<institution>German Primate Center</institution>,<addr-line>Göttingen</addr-line></nlm:aff></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation><nlm:aff id="af2"><addr-line>Institute of Virology</addr-line>,<institution>University of Bonn Medical Center</institution></nlm:aff></affiliation></author><author><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><affiliation><nlm:aff id="af1"><addr-line>Infection Biology Unit</addr-line>,<institution>German Primate Center</institution>,<addr-line>Göttingen</addr-line></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Infectious Diseases</title><idno type="ISSN">0022-1899</idno><idno type="eISSN">1537-6613</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Antiviral Agents (pharmacology)</term><term>Coronavirus (physiology)</term><term>Drug Evaluation, Preclinical</term><term>HEK293 Cells</term><term>Humans</term><term>Molecular Sequence Data</term><term>Proprotein Convertases (antagonists & inhibitors)</term><term>Protease Inhibitors (pharmacology)</term><term>Protein Processing, Post-Translational</term><term>Proteolysis</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux (pharmacologie)</term><term>Cellules HEK293</term><term>Coronavirus (physiologie)</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Inhibiteurs de protéases (pharmacologie)</term><term>Maturation post-traductionnelle des protéines</term><term>Proprotein convertases (antagonistes et inhibiteurs)</term><term>Protéolyse</term><term>Pénétration virale</term><term>Séquence d'acides aminés</term><term>Évaluation préclinique de médicament</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Proprotein Convertases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Proprotein convertases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Inhibiteurs de protéases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Drug Evaluation, Preclinical</term><term>HEK293 Cells</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Processing, Post-Translational</term><term>Proteolysis</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Protéolyse</term><term>Pénétration virale</term><term>Séquence d'acides aminés</term><term>Évaluation préclinique de médicament</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Middle East respiratory syndrome coronavirus (MERS-CoV) infection is associated with a high case-fatality rate, and the potential pandemic spread of the virus is a public health concern. The spike protein of MERS-CoV (MERS-S) facilitates viral entry into host cells, which depends on activation of MERS-S by cellular proteases. Proteolytic activation of MERS-S during viral uptake into target cells has been demonstrated. However, it is unclear whether MERS-S is also cleaved during S protein synthesis in infected cells and whether cleavage is required for MERS-CoV infectivity. Here, we show that MERS-S is processed by proprotein convertases in MERS-S–transfected and MERS-CoV–infected cells and that several RXXR motifs located at the border between the surface and transmembrane subunit of MERS-S are required for efficient proteolysis. However, blockade of proprotein convertases did not impact MERS-S–dependent transduction of target cells expressing high amounts of the viral receptor, DPP4, and did not modulate MERS-CoV infectivity. These results show that MERS-S is a substrate for proprotein convertases and demonstrate that processing by these enzymes is dispensable for S protein activation. Efforts to inhibit MERS-CoV infection by targeting host cell proteases should therefore focus on enzymes that process MERS-S during viral uptake into target cells.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Graham, Rl" uniqKey="Graham R">RL Graham</name></author><author><name sortKey="Donaldson, Ef" uniqKey="Donaldson E">EF Donaldson</name></author><author><name sortKey="Baric, Rs" uniqKey="Baric R">RS Baric</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hilgenfeld, R" uniqKey="Hilgenfeld R">R Hilgenfeld</name></author><author><name sortKey="Peiris, M" uniqKey="Peiris M">M Peiris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drexler, Jf" uniqKey="Drexler J">JF Drexler</name></author><author><name sortKey="Corman, Vm" uniqKey="Corman V">VM Corman</name></author><author><name sortKey="Drosten, C" uniqKey="Drosten C">C 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uniqKey="Vincent M">MJ Vincent</name></author><author><name sortKey="Wickham, L" uniqKey="Wickham L">L Wickham</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Follis, Ke" uniqKey="Follis K">KE Follis</name></author><author><name sortKey="York, J" uniqKey="York J">J York</name></author><author><name sortKey="Nunberg, Jh" uniqKey="Nunberg J">JH Nunberg</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Simmons, G" uniqKey="Simmons G">G Simmons</name></author><author><name sortKey="Bertram, S" uniqKey="Bertram S">S Bertram</name></author><author><name sortKey="Glowacka, I" uniqKey="Glowacka I">I Glowacka</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><name sortKey="Gierer, Stefanie" sort="Gierer, Stefanie" uniqKey="Gierer S" first="Stefanie" last="Gierer">Stefanie Gierer</name><name sortKey="Gnir, Kerstin" sort="Gnir, Kerstin" uniqKey="Gnir K" first="Kerstin" last="Gnir">Kerstin Gnir</name><name sortKey="Heurich, Adeline" sort="Heurich, Adeline" uniqKey="Heurich A" first="Adeline" last="Heurich">Adeline Heurich</name><name sortKey="Muller, Marcel A" sort="Muller, Marcel A" uniqKey="Muller M" first="Marcel A." last="Müller">Marcel A. Müller</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><name sortKey="Ritz, Daniel" sort="Ritz, Daniel" uniqKey="Ritz D" first="Daniel" last="Ritz">Daniel Ritz</name><name sortKey="Schendzielorz, Alexander" sort="Schendzielorz, Alexander" uniqKey="Schendzielorz A" first="Alexander" last="Schendzielorz">Alexander Schendzielorz</name><name sortKey="Springstein, Benjamin L" sort="Springstein, Benjamin L" uniqKey="Springstein B" first="Benjamin L." last="Springstein">Benjamin L. Springstein</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Karsten, Christina B" sort="Karsten, Christina B" uniqKey="Karsten C" first="Christina B." last="Karsten">Christina B. Karsten</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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