Generation and characterization of human monoclonal neutralizing antibodies with distinct binding and sequence features against SARS coronavirus using XenoMouse®
Identifieur interne : 003E90 ( Main/Exploration ); précédent : 003E89; suivant : 003E91Generation 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 [États-Unis] ; Osvaldo Martinez [États-Unis] ; Stephanie K. Masterman [Canada] ; Ole A. Olsen [Canada] ; Angelica A. Moksa [Canada] ; Michael Farzan [États-Unis] ; John S. Babcook [Canada] ; Bellur S. Prabhakar [États-Unis]Source :
- Virology [ 0042-6822 ] ; 2006.
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 200TCID50 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.
Url:
DOI: 10.1016/j.virol.2006.09.029
PubMed: 17161858
PubMed Central: 7103293
Affiliations:
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Le document en format XML
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<country xml:lang="fr">États-Unis</country>
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</placeName>
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<author><name sortKey="Babcook, John S" sort="Babcook, John S" uniqKey="Babcook J" first="John S." last="Babcook">John S. Babcook</name>
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<wicri:regionArea>Amgen British Columbia Inc., 7990 Enterprise Street Burnaby</wicri:regionArea>
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<placeName><region type="state">Illinois</region>
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<term>Antibodies, Monoclonal (genetics)</term>
<term>Antibodies, Monoclonal (immunology)</term>
<term>Antibodies, Viral (biosynthesis)</term>
<term>Antibodies, Viral (genetics)</term>
<term>Antibodies, Viral (immunology)</term>
<term>Antibody Specificity</term>
<term>Hemagglutinins, Viral (immunology)</term>
<term>Humans</term>
<term>Hybridomas</term>
<term>Immunoglobulins (genetics)</term>
<term>Immunoglobulins (metabolism)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Mice</term>
<term>Mice, Transgenic</term>
<term>Molecular Sequence Data</term>
<term>Neutralization Tests</term>
<term>SARS Virus (immunology)</term>
<term>Sequence Alignment</term>
<term>Severe Acute Respiratory Syndrome</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (immunology)</term>
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<term>Anticorps antiviraux (immunologie)</term>
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<term>Anticorps monoclonaux (génétique)</term>
<term>Anticorps monoclonaux (immunologie)</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Humains</term>
<term>Hybridomes</term>
<term>Hémagglutinines virales (immunologie)</term>
<term>Immunoglobulines (génétique)</term>
<term>Immunoglobulines (métabolisme)</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
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<term>Antibodies, Viral</term>
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<term>Anticorps monoclonaux</term>
<term>Glycoprotéines membranaires</term>
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<term>Animals</term>
<term>Antibody Specificity</term>
<term>Humans</term>
<term>Hybridomas</term>
<term>Mice</term>
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<term>Molecular Sequence Data</term>
<term>Neutralization Tests</term>
<term>Sequence Alignment</term>
<term>Severe Acute Respiratory Syndrome</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Données de séquences moléculaires</term>
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<term>Spécificité des anticorps</term>
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<front><div type="abstract" xml:lang="en"><p>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<sub>50</sub>
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.</p>
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<affiliations><list><country><li>Canada</li>
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<region><li>Illinois</li>
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</record>
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