Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
Identifieur interne : 000666 ( PubMed/Corpus ); précédent : 000665; suivant : 000667Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
Auteurs : Jian Shang ; Yushun Wan ; Chang Liu ; Boyd Yount ; Kendra Gully ; Yang Yang ; Ashley Auerbach ; Guiqing Peng ; Ralph Baric ; Fang LiSource :
- PLoS pathogens [ 1553-7374 ] ; 2020.
English descriptors
- KwdEn :
- Animals, Carcinoembryonic Antigen (chemistry), Carcinoembryonic Antigen (metabolism), Carcinoembryonic Antigen (ultrastructure), Cell Line, Tumor, Cryoelectron Microscopy, HEK293 Cells, Humans, Membrane Fusion, Mice, Models, Molecular, Murine hepatitis virus (chemistry), Murine hepatitis virus (physiology), Protein Binding, Protein Conformation, Protein Conformation, alpha-Helical, Protein Domains, Protein Multimerization, Proteolysis, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Receptors, Virus (ultrastructure), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), SARS Virus (chemistry), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure), Virus Attachment, Virus Internalization.
- MESH :
- chemical , chemistry : Carcinoembryonic Antigen, Receptors, Virus, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Carcinoembryonic Antigen, Receptors, Virus, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , ultrastructure : Carcinoembryonic Antigen, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemistry : Murine hepatitis virus, SARS Virus.
- physiology : Murine hepatitis virus.
- Animals, Cell Line, Tumor, Cryoelectron Microscopy, HEK293 Cells, Humans, Membrane Fusion, Mice, Models, Molecular, Protein Binding, Protein Conformation, Protein Conformation, alpha-Helical, Protein Domains, Protein Multimerization, Proteolysis, Virus Attachment, Virus Internalization.
Abstract
Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.
DOI: 10.1371/journal.ppat.1008392
PubMed: 32150576
Links to Exploration step
pubmed:32150576Le document en format XML
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Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Yount, Boyd" sort="Yount, Boyd" uniqKey="Yount B" first="Boyd" last="Yount">Boyd Yount</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Gully, Kendra" sort="Gully, Kendra" uniqKey="Gully K" first="Kendra" last="Gully">Kendra Gully</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Auerbach, Ashley" sort="Auerbach, Ashley" uniqKey="Auerbach A" first="Ashley" last="Auerbach">Ashley Auerbach</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name><affiliation><nlm:affiliation>College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</nlm:affiliation></affiliation></author><author><name sortKey="Baric, Ralph" sort="Baric, Ralph" uniqKey="Baric R" first="Ralph" last="Baric">Ralph Baric</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32150576</idno><idno type="pmid">32150576</idno><idno type="doi">10.1371/journal.ppat.1008392</idno><idno type="wicri:Area/PubMed/Corpus">000666</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000666</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.</title><author><name sortKey="Shang, Jian" sort="Shang, Jian" uniqKey="Shang J" first="Jian" last="Shang">Jian Shang</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Wan, Yushun" sort="Wan, Yushun" uniqKey="Wan Y" first="Yushun" last="Wan">Yushun Wan</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Chang" sort="Liu, Chang" uniqKey="Liu C" first="Chang" last="Liu">Chang Liu</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Yount, Boyd" sort="Yount, Boyd" uniqKey="Yount B" first="Boyd" last="Yount">Boyd Yount</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Gully, Kendra" sort="Gully, Kendra" uniqKey="Gully K" first="Kendra" last="Gully">Kendra Gully</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Auerbach, Ashley" sort="Auerbach, Ashley" uniqKey="Auerbach A" first="Ashley" last="Auerbach">Ashley Auerbach</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name><affiliation><nlm:affiliation>College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</nlm:affiliation></affiliation></author><author><name sortKey="Baric, Ralph" sort="Baric, Ralph" uniqKey="Baric R" first="Ralph" last="Baric">Ralph Baric</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PLoS pathogens</title><idno type="eISSN">1553-7374</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Carcinoembryonic Antigen (chemistry)</term><term>Carcinoembryonic Antigen (metabolism)</term><term>Carcinoembryonic Antigen (ultrastructure)</term><term>Cell Line, Tumor</term><term>Cryoelectron Microscopy</term><term>HEK293 Cells</term><term>Humans</term><term>Membrane Fusion</term><term>Mice</term><term>Models, Molecular</term><term>Murine hepatitis virus (chemistry)</term><term>Murine hepatitis virus (physiology)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Conformation, alpha-Helical</term><term>Protein Domains</term><term>Protein Multimerization</term><term>Proteolysis</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Receptors, Virus (ultrastructure)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Spike Glycoprotein, Coronavirus (ultrastructure)</term><term>Virus Attachment</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carcinoembryonic Antigen</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carcinoembryonic Antigen</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Carcinoembryonic Antigen</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Murine hepatitis virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Cryoelectron Microscopy</term><term>HEK293 Cells</term><term>Humans</term><term>Membrane Fusion</term><term>Mice</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Conformation, alpha-Helical</term><term>Protein Domains</term><term>Protein Multimerization</term><term>Proteolysis</term><term>Virus Attachment</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32150576</PMID><DateCompleted><Year>2020</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1553-7374</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>03</Month></PubDate></JournalIssue><Title>PLoS pathogens</Title><ISOAbbreviation>PLoS Pathog.</ISOAbbreviation></Journal><ArticleTitle>Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.</ArticleTitle><Pagination><MedlinePgn>e1008392</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.ppat.1008392</ELocationID><Abstract><AbstractText>Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shang</LastName><ForeName>Jian</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0003-2600-6059</Identifier><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>Yushun</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chang</ForeName><Initials>C</Initials><Identifier Source="ORCID">0000-0003-1829-0117</Identifier><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yount</LastName><ForeName>Boyd</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gully</LastName><ForeName>Kendra</ForeName><Initials>K</Initials><Identifier Source="ORCID">0000-0001-5742-2341</Identifier><AffiliationInfo><Affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Yang</ForeName><Initials>Y</Initials><Identifier Source="ORCID">0000-0001-9061-3828</Identifier><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Auerbach</LastName><ForeName>Ashley</ForeName><Initials>A</Initials><Identifier Source="ORCID">0000-0001-8505-5905</Identifier><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peng</LastName><ForeName>Guiqing</ForeName><Initials>G</Initials><Identifier Source="ORCID">0000-0001-8813-6663</Identifier><AffiliationInfo><Affiliation>College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baric</LastName><ForeName>Ralph</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0001-6827-8701</Identifier><AffiliationInfo><Affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Fang</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0002-1958-366X</Identifier><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI089728</GrantID><Acronym>AI</Acronym><Agency>NIAID 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>2020</Year><Month>03</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS Pathog</MedlineTA><NlmUniqueID>101238921</NlmUniqueID><ISSNLinking>1553-7366</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002272">Carcinoembryonic Antigen</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C486183">Ceacam1 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002272" MajorTopicYN="N">Carcinoembryonic Antigen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020285" MajorTopicYN="N">Cryoelectron Microscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="N">Membrane Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053585" MajorTopicYN="N">Virus Attachment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053586" MajorTopicYN="Y">Virus Internalization</DescriptorName></MeshHeading></MeshHeadingList><CoiStatement>The authors have declared that no competing interests exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>10</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>03</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32150576</ArticleId><ArticleId IdType="doi">10.1371/journal.ppat.1008392</ArticleId><ArticleId IdType="pii">PPATHOGENS-D-19-01992</ArticleId><ArticleId 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