Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
Identifieur interne : 000C38 ( Main/Exploration ); précédent : 000C37; suivant : 000C39Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
Auteurs : Robert N. Kirchdoerfer [États-Unis] ; Nianshuang Wang [États-Unis] ; Jesper Pallesen [États-Unis] ; Daniel Wrapp [États-Unis] ; Hannah L. Turner [États-Unis] ; Christopher A. Cottrell [États-Unis] ; Kizzmekia S. Corbett [États-Unis] ; Barney S. Graham [États-Unis] ; Jason S. Mclellan [États-Unis] ; Andrew B. Ward [États-Unis]Source :
- Scientific Reports [ 2045-2322 ] ; 2018.
Descripteurs français
- KwdFr :
- Cellules HEK293, Cryomicroscopie électronique, Glycoprotéine de spicule des coronavirus (), Glycosylation, Humains, Mutation, Peptide hydrolases (), Peptidyl-Dipeptidase A (), Proline (génétique), Protéolyse, Pénétration virale, Récepteurs viraux (), Sites de fixation, Stabilité protéique, Structure secondaire des protéines, Tropisme viral, Trypsine (), Virus du SRAS ().
- MESH :
- génétique : Proline.
- Cellules HEK293, Cryomicroscopie électronique, Glycoprotéine de spicule des coronavirus, Glycosylation, Humains, Mutation, Peptide hydrolases, Peptidyl-Dipeptidase A, Protéolyse, Pénétration virale, Récepteurs viraux, Sites de fixation, Stabilité protéique, Structure secondaire des protéines, Tropisme viral, Trypsine, Virus du SRAS.
English descriptors
- KwdEn :
- Binding Sites, Cryoelectron Microscopy, Glycosylation, HEK293 Cells, Humans, Mutation, Peptide Hydrolases (chemistry), Peptidyl-Dipeptidase A (chemistry), Proline (genetics), Protein Stability, Protein Structure, Secondary, Proteolysis, Receptors, Virus (chemistry), SARS Virus (chemistry), Spike Glycoprotein, Coronavirus (chemistry), Trypsin (chemistry), Viral Tropism, Virus Internalization.
- MESH :
- chemical , chemistry : Peptide Hydrolases, Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus, Trypsin.
- chemical , genetics : Proline.
- chemistry : SARS Virus.
- Binding Sites, Cryoelectron Microscopy, Glycosylation, HEK293 Cells, Humans, Mutation, Protein Stability, Protein Structure, Secondary, Proteolysis, Viral Tropism, Virus Internalization.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 as a highly transmissible pathogenic human betacoronavirus. The viral spike glycoprotein (S) utilizes angiotensin-converting enzyme 2 (ACE2) as a host protein receptor and mediates fusion of the viral and host membranes, making S essential to viral entry into host cells and host species tropism. As SARS-CoV enters host cells, the viral S is believed to undergo a number of conformational transitions as it is cleaved by host proteases and binds to host receptors. We recently developed stabilizing mutations for coronavirus spikes that prevent the transition from the pre-fusion to post-fusion states. Here, we present cryo-EM analyses of a stabilized trimeric SARS-CoV S, as well as the trypsin-cleaved, stabilized S, and its interactions with ACE2. Neither binding to ACE2 nor cleavage by trypsin at the S1/S2 cleavage site impart large conformational changes within stabilized SARS-CoV S or expose the secondary cleavage site, S2′.
Url:
DOI: 10.1038/s41598-018-34171-7
PubMed: 30356097
PubMed Central: 6200764
Affiliations:
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Le document en format XML
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Kirchdoerfer</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000000122199231</institution-id><institution-id institution-id-type="GRID">grid.214007.0</institution-id><institution>Department of Integrative Structural and Computational Biology,</institution><institution>The Scripps Research Institute,</institution></institution-wrap>La Jolla, CA 92037 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name><affiliation wicri:level="2"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2179 2404</institution-id><institution-id institution-id-type="GRID">grid.254880.3</institution-id><institution>Department of Biochemistry and Cellular Biology,</institution><institution>Geisel School of Medicine at Dartmouth,</institution></institution-wrap>Hanover, NH 03755 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">New Hampshire</region></placeName><wicri:cityArea>Hanover</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 9924</institution-id><institution-id institution-id-type="GRID">grid.89336.37</institution-id><institution>Present Address: Department of Molecular Biosciences,</institution><institution>The University of Texas at Austin,</institution></institution-wrap>Austin, TX 78712 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Texas</region></placeName><wicri:cityArea>Austin</wicri:cityArea></affiliation></author><author><name sortKey="Pallesen, Jesper" sort="Pallesen, Jesper" uniqKey="Pallesen J" first="Jesper" last="Pallesen">Jesper Pallesen</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000000122199231</institution-id><institution-id institution-id-type="GRID">grid.214007.0</institution-id><institution>Department of Integrative Structural and Computational Biology,</institution><institution>The Scripps Research Institute,</institution></institution-wrap>La Jolla, CA 92037 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Wrapp, Daniel" sort="Wrapp, Daniel" uniqKey="Wrapp D" first="Daniel" last="Wrapp">Daniel Wrapp</name><affiliation wicri:level="2"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2179 2404</institution-id><institution-id institution-id-type="GRID">grid.254880.3</institution-id><institution>Department of Biochemistry and Cellular Biology,</institution><institution>Geisel School of Medicine at Dartmouth,</institution></institution-wrap>Hanover, NH 03755 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">New Hampshire</region></placeName><wicri:cityArea>Hanover</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 9924</institution-id><institution-id institution-id-type="GRID">grid.89336.37</institution-id><institution>Present Address: Department of Molecular Biosciences,</institution><institution>The University of Texas at Austin,</institution></institution-wrap>Austin, TX 78712 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Texas</region></placeName><wicri:cityArea>Austin</wicri:cityArea></affiliation></author><author><name sortKey="Turner, Hannah L" sort="Turner, Hannah L" uniqKey="Turner H" first="Hannah L." last="Turner">Hannah L. Turner</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000000122199231</institution-id><institution-id institution-id-type="GRID">grid.214007.0</institution-id><institution>Department of Integrative Structural and Computational Biology,</institution><institution>The Scripps Research Institute,</institution></institution-wrap>La Jolla, CA 92037 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Cottrell, Christopher A" sort="Cottrell, Christopher A" uniqKey="Cottrell C" first="Christopher A." last="Cottrell">Christopher A. Cottrell</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000000122199231</institution-id><institution-id institution-id-type="GRID">grid.214007.0</institution-id><institution>Department of Integrative Structural and Computational Biology,</institution><institution>The Scripps Research Institute,</institution></institution-wrap>La Jolla, CA 92037 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Corbett, Kizzmekia S" sort="Corbett, Kizzmekia S" uniqKey="Corbett K" first="Kizzmekia S." last="Corbett">Kizzmekia S. Corbett</name><affiliation wicri:level="2"><nlm:aff id="Aff4"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2164 9667</institution-id><institution-id institution-id-type="GRID">grid.419681.3</institution-id><institution>Vaccine Research Center,</institution><institution>National Institute of Allergy and Infectious Diseases,</institution></institution-wrap>Bethesda, MD 20814 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Graham, Barney S" sort="Graham, Barney S" uniqKey="Graham B" first="Barney S." last="Graham">Barney S. Graham</name><affiliation wicri:level="2"><nlm:aff id="Aff4"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2164 9667</institution-id><institution-id institution-id-type="GRID">grid.419681.3</institution-id><institution>Vaccine Research Center,</institution><institution>National Institute of Allergy and Infectious Diseases,</institution></institution-wrap>Bethesda, MD 20814 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Mclellan, Jason S" sort="Mclellan, Jason S" uniqKey="Mclellan J" first="Jason S." last="Mclellan">Jason S. Mclellan</name><affiliation wicri:level="2"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2179 2404</institution-id><institution-id institution-id-type="GRID">grid.254880.3</institution-id><institution>Department of Biochemistry and Cellular Biology,</institution><institution>Geisel School of Medicine at Dartmouth,</institution></institution-wrap>Hanover, NH 03755 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">New Hampshire</region></placeName><wicri:cityArea>Hanover</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 9924</institution-id><institution-id institution-id-type="GRID">grid.89336.37</institution-id><institution>Present Address: Department of Molecular Biosciences,</institution><institution>The University of Texas at Austin,</institution></institution-wrap>Austin, TX 78712 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Texas</region></placeName><wicri:cityArea>Austin</wicri:cityArea></affiliation></author><author><name sortKey="Ward, Andrew B" sort="Ward, Andrew B" uniqKey="Ward A" first="Andrew B." last="Ward">Andrew B. Ward</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000000122199231</institution-id><institution-id institution-id-type="GRID">grid.214007.0</institution-id><institution>Department of Integrative Structural and Computational Biology,</institution><institution>The Scripps Research Institute,</institution></institution-wrap>La Jolla, CA 92037 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>La Jolla</wicri:cityArea></affiliation></author></analytic><series><title level="j">Scientific Reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cryoelectron Microscopy</term><term>Glycosylation</term><term>HEK293 Cells</term><term>Humans</term><term>Mutation</term><term>Peptide Hydrolases (chemistry)</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Proline (genetics)</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Proteolysis</term><term>Receptors, Virus (chemistry)</term><term>SARS Virus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Trypsin (chemistry)</term><term>Viral Tropism</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293</term><term>Cryomicroscopie électronique</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycosylation</term><term>Humains</term><term>Mutation</term><term>Peptide hydrolases ()</term><term>Peptidyl-Dipeptidase A ()</term><term>Proline (génétique)</term><term>Protéolyse</term><term>Pénétration virale</term><term>Récepteurs viraux ()</term><term>Sites de fixation</term><term>Stabilité protéique</term><term>Structure secondaire des protéines</term><term>Tropisme viral</term><term>Trypsine ()</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Hydrolases</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term><term>Trypsin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proline</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Proline</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Cryoelectron Microscopy</term><term>Glycosylation</term><term>HEK293 Cells</term><term>Humans</term><term>Mutation</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Proteolysis</term><term>Viral Tropism</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Cryomicroscopie électronique</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycosylation</term><term>Humains</term><term>Mutation</term><term>Peptide hydrolases</term><term>Peptidyl-Dipeptidase A</term><term>Protéolyse</term><term>Pénétration virale</term><term>Récepteurs viraux</term><term>Sites de fixation</term><term>Stabilité protéique</term><term>Structure secondaire des protéines</term><term>Tropisme viral</term><term>Trypsine</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="Par1">Severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 as a highly transmissible pathogenic human betacoronavirus. The viral spike glycoprotein (S) utilizes angiotensin-converting enzyme 2 (ACE2) as a host protein receptor and mediates fusion of the viral and host membranes, making S essential to viral entry into host cells and host species tropism. As SARS-CoV enters host cells, the viral S is believed to undergo a number of conformational transitions as it is cleaved by host proteases and binds to host receptors. We recently developed stabilizing mutations for coronavirus spikes that prevent the transition from the pre-fusion to post-fusion states. Here, we present cryo-EM analyses of a stabilized trimeric SARS-CoV S, as well as the trypsin-cleaved, stabilized S, and its interactions with ACE2. Neither binding to ACE2 nor cleavage by trypsin at the S1/S2 cleavage site impart large conformational changes within stabilized SARS-CoV S or expose the secondary cleavage site, S2′.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="De Wit, E" uniqKey="De Wit E">E de Wit</name></author><author><name sortKey="Van Doremalen, N" uniqKey="Van Doremalen N">N van Doremalen</name></author><author><name sortKey="Falzarano, D" uniqKey="Falzarano D">D Falzarano</name></author><author><name sortKey="Munster, Vj" uniqKey="Munster V">VJ Munster</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Menachery, Vd" uniqKey="Menachery V">VD Menachery</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Belouzard, S" uniqKey="Belouzard S">S Belouzard</name></author><author><name sortKey="Millet, Jk" uniqKey="Millet J">JK Millet</name></author><author><name sortKey="Licitra, Bn" 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Kirchdoerfer</name></region><name sortKey="Corbett, Kizzmekia S" sort="Corbett, Kizzmekia S" uniqKey="Corbett K" first="Kizzmekia S." last="Corbett">Kizzmekia S. Corbett</name><name sortKey="Cottrell, Christopher A" sort="Cottrell, Christopher A" uniqKey="Cottrell C" first="Christopher A." last="Cottrell">Christopher A. Cottrell</name><name sortKey="Graham, Barney S" sort="Graham, Barney S" uniqKey="Graham B" first="Barney S." last="Graham">Barney S. Graham</name><name sortKey="Mclellan, Jason S" sort="Mclellan, Jason S" uniqKey="Mclellan J" first="Jason S." last="Mclellan">Jason S. Mclellan</name><name sortKey="Mclellan, Jason S" sort="Mclellan, Jason S" uniqKey="Mclellan J" first="Jason S." last="Mclellan">Jason S. Mclellan</name><name sortKey="Pallesen, Jesper" sort="Pallesen, Jesper" uniqKey="Pallesen J" first="Jesper" last="Pallesen">Jesper Pallesen</name><name sortKey="Turner, Hannah L" sort="Turner, Hannah L" uniqKey="Turner H" first="Hannah L." last="Turner">Hannah L. Turner</name><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name><name sortKey="Ward, Andrew B" sort="Ward, Andrew B" uniqKey="Ward A" first="Andrew B." last="Ward">Andrew B. Ward</name><name sortKey="Wrapp, Daniel" sort="Wrapp, Daniel" uniqKey="Wrapp D" first="Daniel" last="Wrapp">Daniel Wrapp</name><name sortKey="Wrapp, Daniel" sort="Wrapp, Daniel" uniqKey="Wrapp D" first="Daniel" last="Wrapp">Daniel Wrapp</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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