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Localization of the discontinous immunodominant region recognized by human anti-thyroperoxidase autoantibodies in autoimmune thyroid diseases Inra
Bresson, D.; Cerutti, M.; Devauchelle, G.; Pugnière, M.; Roquet, F.; Bès, C.; Bossard, C.; Chardès, T.; Péraldi-Roux, S..
The discontinuous immunodominant region (IDR) recognized by autoantibodies directed against the thyroperoxidase (TPO) molecule, a major autoantigen in autoimmune thyroid diseases, has not yet been completely localized. By using peptide phage-displayed technology, we identified three critical motifs, LXPEXD, QSYP, and EX(E/D)PPV, within selected mimotopes which interacted with the human recombinant anti-TPO autoantibody (aAb) T13, derived from an antibody phage-displayed library obtained from thyroid-infiltrating TPO-selected B cells of Graves' disease patients. Mimotope sequence alignment on the TPO molecule, together with the binding analysis of the T13 aAb on TPO mutants expressed by Chinese hamster ovary cells, demonstrated that regions 353–363,...
Tipo: Journal Article Palavras-chave: CELLULE INSECTE; AUTOIMMUNE; THYROIDE; MONOCLONAL.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400025185106077&uri=/notices/prodinra1/2010/11/
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Mapping the paratope of anti-CD4 recombinant fab 13B8.2 by combining parallel peptide synthesis and site-directed mutagenesis Inra
Bès, C.; Briand-Longuet, L.; Cerutti, M.; Heitz, F.; Troadec, S.; Pugnière, M.; Roquet, F.; Molina, F.; Casset, F.; Bresson, D.; Péraldi-Roux, S.; Devauchelle, G.; Devaux, C.; Granier, C.; Chardès, T..
We analyzed antigen-binding residues from the variable domains of anti-CD4 antibody 13B8.2 using the Spot method of parallel peptide synthesis. Sixteen amino acids, defined as Spot critical residues (SCR), were identified on the basis of a 50% decrease in CD4 binding to alanine analogs of reactive peptides. Recombinant Fab 13B8.2 mutants were constructed with alanine residues in place of each of the 16 SCR, expressed in the baculovirus cell system, and purified. CD measurements indicated that the mutated proteins were conformationally intact, with a β-sheet secondary structure similar to that of wild-type Fab. Compared with the CD4-binding capacity of wild-type Fab 13B8.2, 11 light (Y32-L, W35-L, Y36-L, H91-L, and Y92-L) and heavy chain (H35-H, R38-H,...
Tipo: Journal Article Palavras-chave: ANTICORPSMUTATION; CARACTERISATION.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400025195106087&uri=/notices/prodinra1/2010/11/
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