Resolution of two overlapping neutralizing B cell epitopes within a solvent exposed, immunodominant α-helix in ricin toxin's enzymatic subunit.
Identifieur interne : 002211 ( Main/Exploration ); précédent : 002210; suivant : 002212Resolution of two overlapping neutralizing B cell epitopes within a solvent exposed, immunodominant α-helix in ricin toxin's enzymatic subunit.
Auteurs : David J. Vance [États-Unis] ; Nicholas J. MantisSource :
- Toxicon : official journal of the International Society on Toxinology [ 1879-3150 ] ; 2012.
Descripteurs français
- KwdFr :
- Anticorps monoclonaux (métabolisme), Banque de peptides, Domaine catalytique (génétique), Données de séquences moléculaires, Déterminants antigéniques des lymphocytes B (génétique), Déterminants antigéniques des lymphocytes B (métabolisme), Modèles moléculaires, Ricine (génétique), Structure secondaire des protéines (génétique), Séquence d'acides aminés.
- MESH :
- génétique : Domaine catalytique, Déterminants antigéniques des lymphocytes B, Ricine, Structure secondaire des protéines.
- métabolisme : Anticorps monoclonaux, Déterminants antigéniques des lymphocytes B.
- Banque de peptides, Données de séquences moléculaires, Modèles moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Epitopes, B-Lymphocyte, Ricin.
- chemical , metabolism : Antibodies, Monoclonal, Epitopes, B-Lymphocyte.
- genetics : Catalytic Domain, Protein Structure, Secondary.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Peptide Library.
Abstract
Residues Y₉₁-T₁₁₆ of ricin toxin's enzymatic subunit (RTA) constitute an immunodominant loop-helix-loop motif that is the target of two potent toxin neutralizing monoclonal antibodies (mAbs), PB10 and R70. To define the exact epitope(s) recognized by these mAbs, we affinity enriched from a phage-displayed peptide library 12 mers that bound one or both of these mAbs. We report that PB10 recognizes a distinct but overlapping epitope with R70, in which residues Q₉₈, E₁₀₂, T₁₀₅, and H₁₀₆ are central to mAb recognition.
DOI: 10.1016/j.toxicon.2012.06.014
PubMed: 22750533
Affiliations:
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Le document en format XML
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<term>Données de séquences moléculaires</term>
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<term>Déterminants antigéniques des lymphocytes B (métabolisme)</term>
<term>Modèles moléculaires</term>
<term>Ricine (génétique)</term>
<term>Structure secondaire des protéines (génétique)</term>
<term>Séquence d'acides aminés</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Catalytic Domain</term>
<term>Protein Structure, Secondary</term>
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<term>Structure secondaire des protéines</term>
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<front><div type="abstract" xml:lang="en">Residues Y₉₁-T₁₁₆ of ricin toxin's enzymatic subunit (RTA) constitute an immunodominant loop-helix-loop motif that is the target of two potent toxin neutralizing monoclonal antibodies (mAbs), PB10 and R70. To define the exact epitope(s) recognized by these mAbs, we affinity enriched from a phage-displayed peptide library 12 mers that bound one or both of these mAbs. We report that PB10 recognizes a distinct but overlapping epitope with R70, in which residues Q₉₈, E₁₀₂, T₁₀₅, and H₁₀₆ are central to mAb recognition.</div>
</front>
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