Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology.
Identifieur interne : 001746 ( PubMed/Corpus ); précédent : 001745; suivant : 001747Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology.
Auteurs : Jody D. Berry ; Kevin Hay ; James M. Rini ; Meng Yu ; Linfa Wang ; Francis A. Plummer ; Cindi R. Corbett ; Anton AndonovSource :
- mAbs [ 1942-0870 ]
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (genetics), Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (metabolism), Antibodies, Neutralizing (chemistry), Antibodies, Neutralizing (genetics), Antibodies, Neutralizing (immunology), Antibodies, Neutralizing (metabolism), Antibody Affinity, Biomedical Technology, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Immunodominant Epitopes (immunology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Mice, Protein Binding, Protein Conformation, Receptor, Angiotensin, Type 2 (metabolism), Receptors, Antigen, B-Cell (immunology), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (immunology), Recombinant Fusion Proteins (metabolism), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (prevention & control), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism), Viral Vaccines.
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Antibodies, Neutralizing, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , genetics : Antibodies, Monoclonal, Antibodies, Neutralizing, Recombinant Fusion Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Neutralizing, Immunodominant Epitopes, Membrane Glycoproteins, Receptors, Antigen, B-Cell, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , metabolism : Antibodies, Monoclonal, Antibodies, Neutralizing, Membrane Glycoproteins, Receptor, Angiotensin, Type 2, Recombinant Fusion Proteins, Viral Envelope Proteins.
- immunology : SARS Virus, Severe Acute Respiratory Syndrome.
- prevention & control : Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Antibody Affinity, Biomedical Technology, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Mice, Protein Binding, Protein Conformation, Spike Glycoprotein, Coronavirus, Viral Vaccines.
Abstract
Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro. Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TO R2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.
DOI: 10.4161/mabs.2.1.10788
PubMed: 20168090
Links to Exploration step
pubmed:20168090Le document en format XML
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Rini</name></author><author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name></author><author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</name></author><author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name></author><author><name sortKey="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. 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Corbett</name></author><author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name></author></analytic><series><title level="j">mAbs</title><idno type="eISSN">1942-0870</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (chemistry)</term><term>Antibodies, Monoclonal (genetics)</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Monoclonal (metabolism)</term><term>Antibodies, Neutralizing (chemistry)</term><term>Antibodies, Neutralizing (genetics)</term><term>Antibodies, Neutralizing (immunology)</term><term>Antibodies, Neutralizing (metabolism)</term><term>Antibody Affinity</term><term>Biomedical Technology</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitope Mapping</term><term>Humans</term><term>Immunodominant Epitopes (immunology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (immunology)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Protein Binding</term><term>Protein Conformation</term><term>Receptor, Angiotensin, Type 2 (metabolism)</term><term>Receptors, Antigen, B-Cell (immunology)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (immunology)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (immunology)</term><term>Severe Acute Respiratory Syndrome (immunology)</term><term>Severe Acute Respiratory Syndrome (prevention & control)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (immunology)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Vaccines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Neutralizing</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Neutralizing</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Neutralizing</term><term>Immunodominant Epitopes</term><term>Membrane Glycoproteins</term><term>Receptors, Antigen, B-Cell</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Neutralizing</term><term>Membrane Glycoproteins</term><term>Receptor, Angiotensin, Type 2</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Affinity</term><term>Biomedical Technology</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitope Mapping</term><term>Humans</term><term>Mice</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Vaccines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro. Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TO R2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20168090</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>14</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1942-0870</ISSN><JournalIssue CitedMedium="Internet"><Volume>2</Volume><Issue>1</Issue><PubDate><MedlineDate>2010 Jan-Feb</MedlineDate></PubDate></JournalIssue><Title>mAbs</Title><ISOAbbreviation>MAbs</ISOAbbreviation></Journal><ArticleTitle>Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology.</ArticleTitle><Pagination><MedlinePgn>53-66</MedlinePgn></Pagination><Abstract><AbstractText>Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro. Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TO R2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Berry</LastName><ForeName>Jody D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Department of Medical Microbiology, University of Manitoba, Winnipeg, Canada. jberry@cangene.com</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hay</LastName><ForeName>Kevin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Rini</LastName><ForeName>James M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Meng</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Linfa</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Plummer</LastName><ForeName>Francis A</ForeName><Initials>FA</Initials></Author><Author ValidYN="Y"><LastName>Corbett</LastName><ForeName>Cindi R</ForeName><Initials>CR</Initials></Author><Author ValidYN="Y"><LastName>Andonov</LastName><ForeName>Anton</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>01</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>MAbs</MedlineTA><NlmUniqueID>101479829</NlmUniqueID><ISSNLinking>1942-0862</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D057134">Antibodies, 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Epitopes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044139" MajorTopicYN="N">Receptor, Angiotensin, Type 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011947" MajorTopicYN="N">Receptors, Antigen, B-Cell</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000517" MajorTopicYN="Y">prevention & control</QualifierName><QualifierName 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