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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 : 002212

Resolution 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. Mantis

Source :

RBID : pubmed:22750533

Descripteurs français

English descriptors

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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<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>
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