MersV1, Main, Exploration, bibRecord, 002636

Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase.

Identifieur interne : 002636 ( Main/Exploration ); précédent : 002635; suivant : 002637

Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase.

Auteurs : Barbara Hjelm [Suède] ; Carmen Díez Fernández ; John Löfblom ; Stefan St Hl ; Henrik Johannesson ; Johan Rockberg ; Mathias Uhlén

Source :

New biotechnology [ 1876-4347 ] ; 2010.

RBID : pubmed:19913117

Descripteurs français

KwdFr :
- Anticorps (), Anticorps (immunologie), Cartographie épitopique (), Humains, Tryptophane-tRNA ligase (), Tryptophane-tRNA ligase (immunologie).
MESH :
- immunologie : Anticorps, Tryptophane-tRNA ligase.
- Anticorps, Cartographie épitopique, Humains, Tryptophane-tRNA ligase.

English descriptors

KwdEn :
- Antibodies (chemistry), Antibodies (immunology), Epitope Mapping (methods), Humans, Tryptophan-tRNA Ligase (chemistry), Tryptophan-tRNA Ligase (immunology).
MESH :
- chemical , chemistry : Antibodies, Tryptophan-tRNA Ligase.
- chemical , immunology : Antibodies, Tryptophan-tRNA Ligase.
- methods : Epitope Mapping.
- Humans.

Abstract

There is a need to characterize the epitopes of affinity reagents to develop high quality affinity reagents for research, diagnostics and therapy. Here, we describe the analysis of epitopes of antibodies generated toward human tryptophanyl-tRNA synthetase (WARS) using both combinatorial bacterial display and suspension bead array. The bacterial display revealed that the polyclonal antibody binds to three separate epitopes and peptide scanning using 15-mers revealed binding to a 13 amino acid consensus sequence (ELINRIERATGQR). A mouse monoclonal antibody was generated and the mapping approach revealed binding toward a slightly shifted position of the same epitope. Structural analysis showed that the antibodies bind to alpha-helical regions on the surface of the target protein. An alanine-scanning experiment showed binding to four specific residues. The implications for the systematic analysis of antibody epitopes on the basis of these results are discussed.

DOI: 10.1016/j.nbt.2009.11.001
PubMed: 19913117

Affiliations:

Le document en format XML

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<series><title level="j">New biotechnology</title>
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<front><div type="abstract" xml:lang="en">There is a need to characterize the epitopes of affinity reagents to develop high quality affinity reagents for research, diagnostics and therapy. Here, we describe the analysis of epitopes of antibodies generated toward human tryptophanyl-tRNA synthetase (WARS) using both combinatorial bacterial display and suspension bead array. The bacterial display revealed that the polyclonal antibody binds to three separate epitopes and peptide scanning using 15-mers revealed binding to a 13 amino acid consensus sequence (ELINRIERATGQR). A mouse monoclonal antibody was generated and the mapping approach revealed binding toward a slightly shifted position of the same epitope. Structural analysis showed that the antibodies bind to alpha-helical regions on the surface of the target protein. An alanine-scanning experiment showed binding to four specific residues. The implications for the systematic analysis of antibody epitopes on the basis of these results are discussed.</div>
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Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase.

Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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