Generation and characterization of human monoclonal neutralizing antibodies with distinct binding and sequence features against SARS coronavirus using XenoMouse.
Identifieur interne : 001E04 ( PubMed/Checkpoint ); précédent : 001E03; suivant : 001E05Generation and characterization of human monoclonal neutralizing antibodies with distinct binding and sequence features against SARS coronavirus using XenoMouse.
Auteurs : Melissa Coughlin [États-Unis] ; Gin Lou ; Osvaldo Martinez ; Stephanie K. Masterman ; Ole A. Olsen ; Angelica A. Moksa ; Michael Farzan ; John S. Babcook ; Bellur S. PrabhakarSource :
- Virology [ 0042-6822 ] ; 2007.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Anticorps antiviraux (biosynthèse), Anticorps antiviraux (génétique), Anticorps antiviraux (immunologie), Anticorps monoclonaux (biosynthèse), Anticorps monoclonaux (génétique), Anticorps monoclonaux (immunologie), Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (immunologie), Humains, Hybridomes, Hémagglutinines virales (immunologie), Immunoglobulines (génétique), Immunoglobulines (métabolisme), Protéines de l'enveloppe virale (immunologie), Souris, Souris transgéniques, Spécificité des anticorps, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Tests de neutralisation, Virus du SRAS (immunologie).
- MESH :
- biosynthèse : Anticorps antiviraux, Anticorps monoclonaux.
- génétique : Anticorps antiviraux, Anticorps monoclonaux, Immunoglobulines.
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Glycoprotéines membranaires, Hémagglutinines virales, Protéines de l'enveloppe virale, Virus du SRAS.
- métabolisme : Immunoglobulines.
- Alignement de séquences, Animaux, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Humains, Hybridomes, Souris, Souris transgéniques, Spécificité des anticorps, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Tests de neutralisation.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (biosynthesis), Antibodies, Monoclonal (genetics), Antibodies, Monoclonal (immunology), Antibodies, Viral (biosynthesis), Antibodies, Viral (genetics), Antibodies, Viral (immunology), Antibody Specificity, Hemagglutinins, Viral (immunology), Humans, Hybridomas, Immunoglobulins (genetics), Immunoglobulins (metabolism), Membrane Glycoproteins (immunology), Mice, Mice, Transgenic, Molecular Sequence Data, Neutralization Tests, SARS Virus (immunology), Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (immunology).
- MESH :
- chemical , biosynthesis : Antibodies, Monoclonal, Antibodies, Viral.
- chemical , genetics : Antibodies, Monoclonal, Antibodies, Viral, Immunoglobulins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Hemagglutinins, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Immunoglobulins.
- immunology : SARS Virus.
- Amino Acid Sequence, Animals, Antibody Specificity, Humans, Hybridomas, Mice, Mice, Transgenic, Molecular Sequence Data, Neutralization Tests, Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus.
Abstract
Passive therapy with neutralizing human monoclonal antibodies (mAbs) could be an effective therapy against severe acute respiratory syndrome coronavirus (SARS-CoV). Utilizing the human immunoglobulin transgenic mouse, XenoMouse, we produced fully human SARS-CoV spike (S) protein specific antibodies. Antibodies were examined for reactivity against a recombinant S1 protein, to which 200 antibodies reacted. Twenty-seven antibodies neutralized 200TCID(50) SARS-CoV (Urbani). Additionally, 57 neutralizing antibodies were found that are likely specific to S2. Mapping of the binding region was achieved with several S1 recombinant proteins. Most S1 reactive neutralizing mAbs bound to the RBD, aa 318-510. However, two S1 specific mAbs reacted with a domain upstream of the RBD between aa 12 and 261. Immunoglobulin gene sequence analyses suggested at least 8 different binding specificities. Unique human mAbs could be used as a cocktail that would simultaneously target several neutralizing epitopes and prevent emergence of escape mutants.
DOI: 10.1016/j.virol.2006.09.029
PubMed: 17161858
Affiliations:
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pubmed:17161858Le document en format XML
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Utilizing the human immunoglobulin transgenic mouse, XenoMouse, we produced fully human SARS-CoV spike (S) protein specific antibodies. Antibodies were examined for reactivity against a recombinant S1 protein, to which 200 antibodies reacted. Twenty-seven antibodies neutralized 200TCID(50) SARS-CoV (Urbani). Additionally, 57 neutralizing antibodies were found that are likely specific to S2. Mapping of the binding region was achieved with several S1 recombinant proteins. Most S1 reactive neutralizing mAbs bound to the RBD, aa 318-510. However, two S1 specific mAbs reacted with a domain upstream of the RBD between aa 12 and 261. Immunoglobulin gene sequence analyses suggested at least 8 different binding specificities. Unique human mAbs could be used as a cocktail that would simultaneously target several neutralizing epitopes and prevent emergence of escape mutants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17161858</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>361</Volume><Issue>1</Issue><PubDate><Year>2007</Year><Month>Apr</Month><Day>25</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Generation and characterization of human monoclonal neutralizing antibodies with distinct binding and sequence features against SARS coronavirus using XenoMouse.</ArticleTitle><Pagination><MedlinePgn>93-102</MedlinePgn></Pagination><Abstract><AbstractText>Passive therapy with neutralizing human monoclonal antibodies (mAbs) could be an effective therapy against severe acute respiratory syndrome coronavirus (SARS-CoV). Utilizing the human immunoglobulin transgenic mouse, XenoMouse, we produced fully human SARS-CoV spike (S) protein specific antibodies. Antibodies were examined for reactivity against a recombinant S1 protein, to which 200 antibodies reacted. Twenty-seven antibodies neutralized 200TCID(50) SARS-CoV (Urbani). Additionally, 57 neutralizing antibodies were found that are likely specific to S2. Mapping of the binding region was achieved with several S1 recombinant proteins. Most S1 reactive neutralizing mAbs bound to the RBD, aa 318-510. However, two S1 specific mAbs reacted with a domain upstream of the RBD between aa 12 and 261. Immunoglobulin gene sequence analyses suggested at least 8 different binding specificities. Unique human mAbs could be used as a cocktail that would simultaneously target several neutralizing epitopes and prevent emergence of escape mutants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Coughlin</LastName><ForeName>Melissa</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology (MC790) College of Medicine, University of Illinois at Chicago, Room E705. 835 S. Wolcott AveChicago, IL 60612, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lou</LastName><ForeName>Gin</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Martinez</LastName><ForeName>Osvaldo</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Masterman</LastName><ForeName>Stephanie K</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Olsen</LastName><ForeName>Ole A</ForeName><Initials>OA</Initials></Author><Author ValidYN="Y"><LastName>Moksa</LastName><ForeName>Angelica A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Farzan</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Babcook</LastName><ForeName>John S</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Prabhakar</LastName><ForeName>Bellur S</ForeName><Initials>BS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>12</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006389">Hemagglutinins, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007136">Immunoglobulins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000918" MajorTopicYN="N">Antibody Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006389" MajorTopicYN="N">Hemagglutinins, Viral</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006825" MajorTopicYN="N">Hybridomas</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007136" MajorTopicYN="N">Immunoglobulins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008822" MajorTopicYN="N">Mice, Transgenic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009500" MajorTopicYN="N">Neutralization Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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IdType="pubmed">16195424</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li></region><settlement><li>Chicago</li></settlement><orgName><li>Université de l'Illinois à Chicago</li></orgName></list><tree><noCountry><name sortKey="Babcook, John S" sort="Babcook, John S" uniqKey="Babcook J" first="John S" last="Babcook">John S. 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