Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion
Identifieur interne : 000541 ( Main/Curation ); précédent : 000540; suivant : 000542Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion
Auteurs : Shuai Xia [République populaire de Chine] ; Meiqin Liu [République populaire de Chine] ; Chao Wang [République populaire de Chine] ; Wei Xu [République populaire de Chine] ; Qiaoshuai Lan [République populaire de Chine] ; Siliang Feng [République populaire de Chine] ; Feifei Qi [République populaire de Chine] ; Linlin Bao [République populaire de Chine] ; Lanying Du [États-Unis] ; Shuwen Liu [République populaire de Chine] ; Chuan Qin [République populaire de Chine] ; Fei Sun [République populaire de Chine] ; Zhengli Shi [République populaire de Chine] ; Yun Zhu [République populaire de Chine] ; Shibo Jiang [République populaire de Chine, États-Unis] ; Lu Lu [République populaire de Chine]Source :
- Cell Research [ 1001-0602 ] ; 2020.
Descripteurs français
- KwdFr :
- Administration par voie nasale, Alignement de séquences, Animaux, Cellules HEK293, Cellules Vero, Fusion cellulaire, Fusion membranaire, Glycoprotéine de spicule des coronavirus (antagonistes et inhibiteurs), Humains, Infections à coronavirus (), Lipopeptides (pharmacologie), Motifs et domaines d'intéraction protéique, Pandémies (), Pneumopathie virale (), Relation structure-activité, Souris, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS.
- MESH :
- antagonistes et inhibiteurs : Glycoprotéine de spicule des coronavirus.
- pharmacologie : Lipopeptides.
- Administration par voie nasale, Alignement de séquences, Animaux, Cellules HEK293, Cellules Vero, Fusion cellulaire, Fusion membranaire, Humains, Infections à coronavirus, Motifs et domaines d'intéraction protéique, Pandémies, Pneumopathie virale, Relation structure-activité, Souris, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS.
English descriptors
- KwdEn :
- Administration, Intranasal, Amino Acid Sequence, Animals, Betacoronavirus (drug effects), Betacoronavirus (physiology), Cell Fusion, Chlorocebus aethiops, Coronavirus Infections (prevention & control), HEK293 Cells, Humans, Lipopeptides (pharmacology), Membrane Fusion, Mice, Pandemics (prevention & control), Pneumonia, Viral (prevention & control), Protein Interaction Domains and Motifs, Protein Structure, Secondary, SARS Virus, Sequence Alignment, Spike Glycoprotein, Coronavirus (antagonists & inhibitors), Structure-Activity Relationship, Vero Cells.
- MESH :
- chemical , antagonists & inhibitors : Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Lipopeptides.
- drug effects : Betacoronavirus.
- physiology : Betacoronavirus.
- prevention & control : Coronavirus Infections, Pandemics, Pneumonia, Viral.
- Administration, Intranasal, Amino Acid Sequence, Animals, Cell Fusion, Chlorocebus aethiops, HEK293 Cells, Humans, Membrane Fusion, Mice, Protein Interaction Domains and Motifs, Protein Structure, Secondary, SARS Virus, Sequence Alignment, Structure-Activity Relationship, Vero Cells.
Abstract
The recent outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 infection in Wuhan, China has posed a serious threat to global public health. To develop specific anti-coronavirus therapeutics and prophylactics, the molecular mechanism that underlies viral infection must first be defined. Therefore, we herein established a SARS-CoV-2 spike (S) protein-mediated cell–cell fusion assay and found that SARS-CoV-2 showed a superior plasma membrane fusion capacity compared to that of SARS-CoV. We solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain. We previously developed a pan-coronavirus fusion inhibitor, EK1, which targeted the HR1 domain and could inhibit infection by divergent human coronaviruses tested, including SARS-CoV and MERS-CoV. Here we generated a series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection with IC50s of 1.3 and 15.8 nM, about 241- and 149-fold more potent than the original EK1 peptide, respectively. EK1C4 was also highly effective against membrane fusion and infection of other human coronavirus pseudoviruses tested, including SARS-CoV and MERS-CoV, as well as SARSr-CoVs, and potently inhibited the replication of 5 live human coronaviruses examined, including SARS-CoV-2. Intranasal application of EK1C4 before or after challenge with HCoV-OC43 protected mice from infection, suggesting that EK1C4 could be used for prevention and treatment of infection by the currently circulating SARS-CoV-2 and other emerging SARSr-CoVs.
Url:
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104723
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7118126
DOI: 10.1038/s41422-020-0305-x
PubMed: NONE
PubMed Central: 7104723
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PMC:7104723Le document en format XML
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27 Tai-Ping Road, Beijing, 100850 China</nlm:aff>
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<institution>Peking Union Medical College,</institution>
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Beijing, 100021 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Beijing</wicri:regionArea>
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<institution>Peking Union Medical College,</institution>
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Beijing, 100021 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Beijing</wicri:regionArea>
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<author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name>
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<institution>Lindsley F. Kimball Research Institute, New York Blood Center,</institution>
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New York, NY 10065 USA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>New York</wicri:cityArea>
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<author><name sortKey="Liu, Shuwen" sort="Liu, Shuwen" uniqKey="Liu S" first="Shuwen" last="Liu">Shuwen Liu</name>
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<institution>Guangzhou Key Laboratory of Drug Research for Emerging Virus Prevention and Treatment, School of Pharmaceutical Sciences, Southern Medical University,</institution>
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Guangzhou, 510515 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Guangzhou</wicri:regionArea>
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</author>
<author><name sortKey="Qin, Chuan" sort="Qin, Chuan" uniqKey="Qin C" first="Chuan" last="Qin">Chuan Qin</name>
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<institution>Peking Union Medical College,</institution>
</institution-wrap>
Beijing, 100021 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Beijing</wicri:regionArea>
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<author><name sortKey="Sun, Fei" sort="Sun, Fei" uniqKey="Sun F" first="Fei" last="Sun">Fei Sun</name>
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<institution-id institution-id-type="GRID">grid.418856.6</institution-id>
<institution>National Laboratory of Biomacromolecules,</institution>
<institution>Institute of Biophysics, Chinese Academy of Sciences,</institution>
</institution-wrap>
Beijing, 100101 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Beijing</wicri:regionArea>
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</author>
<author><name sortKey="Shi, Zhengli" sort="Shi, Zhengli" uniqKey="Shi Z" first="Zhengli" last="Shi">Zhengli Shi</name>
<affiliation wicri:level="1"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000119573309</institution-id>
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Wuhan, 430071 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Wuhan</wicri:regionArea>
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</author>
<author><name sortKey="Zhu, Yun" sort="Zhu, Yun" uniqKey="Zhu Y" first="Yun" last="Zhu">Yun Zhu</name>
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<institution-id institution-id-type="GRID">grid.418856.6</institution-id>
<institution>National Laboratory of Biomacromolecules,</institution>
<institution>Institute of Biophysics, Chinese Academy of Sciences,</institution>
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Beijing, 100101 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Beijing</wicri:regionArea>
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</author>
<author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
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<institution>Fudan University,</institution>
</institution-wrap>
Shanghai, 200032 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Shanghai</wicri:regionArea>
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<affiliation wicri:level="2"><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0442 2075</institution-id>
<institution-id institution-id-type="GRID">grid.250415.7</institution-id>
<institution>Lindsley F. Kimball Research Institute, New York Blood Center,</institution>
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New York, NY 10065 USA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>New York</wicri:cityArea>
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<author><name sortKey="Lu, Lu" sort="Lu, Lu" uniqKey="Lu L" first="Lu" last="Lu">Lu Lu</name>
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<institution-id institution-id-type="GRID">grid.8547.e</institution-id>
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<institution>Fudan University,</institution>
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Shanghai, 200032 China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Shanghai</wicri:regionArea>
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<series><title level="j">Cell Research</title>
<idno type="ISSN">1001-0602</idno>
<idno type="eISSN">1748-7838</idno>
<imprint><date when="2020">2020</date>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Betacoronavirus (drug effects)</term>
<term>Betacoronavirus (physiology)</term>
<term>Cell Fusion</term>
<term>Chlorocebus aethiops</term>
<term>Coronavirus Infections (prevention & control)</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Lipopeptides (pharmacology)</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Pandemics (prevention & control)</term>
<term>Pneumonia, Viral (prevention & control)</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus</term>
<term>Sequence Alignment</term>
<term>Spike Glycoprotein, Coronavirus (antagonists & inhibitors)</term>
<term>Structure-Activity Relationship</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Administration par voie nasale</term>
<term>Alignement de séquences</term>
<term>Animaux</term>
<term>Cellules HEK293</term>
<term>Cellules Vero</term>
<term>Fusion cellulaire</term>
<term>Fusion membranaire</term>
<term>Glycoprotéine de spicule des coronavirus (antagonistes et inhibiteurs)</term>
<term>Humains</term>
<term>Infections à coronavirus ()</term>
<term>Lipopeptides (pharmacologie)</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Pandémies ()</term>
<term>Pneumopathie virale ()</term>
<term>Relation structure-activité</term>
<term>Souris</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Lipopeptides</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Betacoronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Lipopeptides</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Betacoronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Coronavirus Infections</term>
<term>Pandemics</term>
<term>Pneumonia, Viral</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Administration, Intranasal</term>
<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cell Fusion</term>
<term>Chlorocebus aethiops</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus</term>
<term>Sequence Alignment</term>
<term>Structure-Activity Relationship</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Administration par voie nasale</term>
<term>Alignement de séquences</term>
<term>Animaux</term>
<term>Cellules HEK293</term>
<term>Cellules Vero</term>
<term>Fusion cellulaire</term>
<term>Fusion membranaire</term>
<term>Humains</term>
<term>Infections à coronavirus</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Pandémies</term>
<term>Pneumopathie virale</term>
<term>Relation structure-activité</term>
<term>Souris</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en"><p id="Par1">The recent outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 infection in Wuhan, China has posed a serious threat to global public health. To develop specific anti-coronavirus therapeutics and prophylactics, the molecular mechanism that underlies viral infection must first be defined. Therefore, we herein established a SARS-CoV-2 spike (S) protein-mediated cell–cell fusion assay and found that SARS-CoV-2 showed a superior plasma membrane fusion capacity compared to that of SARS-CoV. We solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain. We previously developed a pan-coronavirus fusion inhibitor, EK1, which targeted the HR1 domain and could inhibit infection by divergent human coronaviruses tested, including SARS-CoV and MERS-CoV. Here we generated a series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection with IC50s of 1.3 and 15.8 nM, about 241- and 149-fold more potent than the original EK1 peptide, respectively. EK1C4 was also highly effective against membrane fusion and infection of other human coronavirus pseudoviruses tested, including SARS-CoV and MERS-CoV, as well as SARSr-CoVs, and potently inhibited the replication of 5 live human coronaviruses examined, including SARS-CoV-2. Intranasal application of EK1C4 before or after challenge with HCoV-OC43 protected mice from infection, suggesting that EK1C4 could be used for prevention and treatment of infection by the currently circulating SARS-CoV-2 and other emerging SARSr-CoVs.</p>
</div>
</front>
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<biblStruct><analytic><author><name sortKey="Morris, Gm" uniqKey="Morris G">GM Morris</name>
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