Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis.
Identifieur interne : 000962 ( PubMed/Corpus ); précédent : 000961; suivant : 000963Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis.
Auteurs : Robert N. Kirchdoerfer ; Nianshuang Wang ; Jesper Pallesen ; Daniel Wrapp ; Hannah L. Turner ; Christopher A. Cottrell ; Kizzmekia S. Corbett ; Barney S. Graham ; Jason S. Mclellan ; Andrew B. WardSource :
- Scientific reports [ 2045-2322 ] ; 2018.
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'.
DOI: 10.1038/s41598-018-34171-7
PubMed: 30356097
Links to Exploration step
pubmed:30356097Le document en format XML
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Kirchdoerfer</name><affiliation><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name><affiliation><nlm:affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Pallesen, Jesper" sort="Pallesen, Jesper" uniqKey="Pallesen J" first="Jesper" last="Pallesen">Jesper Pallesen</name><affiliation><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Wrapp, Daniel" sort="Wrapp, Daniel" uniqKey="Wrapp D" first="Daniel" last="Wrapp">Daniel Wrapp</name><affiliation><nlm:affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Turner, Hannah L" sort="Turner, Hannah L" uniqKey="Turner H" first="Hannah L" last="Turner">Hannah L. 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Corbett</name><affiliation><nlm:affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20814, USA.</nlm:affiliation></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><nlm:affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20814, USA.</nlm:affiliation></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><nlm:affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</nlm:affiliation></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><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA. andrew@scripps.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2018" type="published">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="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" 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></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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'.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30356097</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>26</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>1</Issue><PubDate><Year>2018</Year><Month>10</Month><Day>24</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis.</ArticleTitle><Pagination><MedlinePgn>15701</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-018-34171-7</ELocationID><Abstract><AbstractText>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'.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kirchdoerfer</LastName><ForeName>Robert N</ForeName><Initials>RN</Initials><AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Nianshuang</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pallesen</LastName><ForeName>Jesper</ForeName><Initials>J</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-3270-1587</Identifier><AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wrapp</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>Hannah L</ForeName><Initials>HL</Initials><AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cottrell</LastName><ForeName>Christopher A</ForeName><Initials>CA</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-3364-3083</Identifier><AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corbett</LastName><ForeName>Kizzmekia S</ForeName><Initials>KS</Initials><AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20814, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Graham</LastName><ForeName>Barney S</ForeName><Initials>BS</Initials><AffiliationInfo><Affiliation>Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD, 20814, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McLellan</LastName><ForeName>Jason S</ForeName><Initials>JS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Cellular Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ward</LastName><ForeName>Andrew B</ForeName><Initials>AB</Initials><AffiliationInfo><Affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA. andrew@scripps.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>K99 AI123498</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R00 AI123498</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI127521</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>S10 OD021634</GrantID><Acronym>OD</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>10</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>9DLQ4CIU6V</RegistryNumber><NameOfSubstance UI="D011392">Proline</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Sci Rep. 2018 Dec 10;8(1):17823</RefSource><PMID 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