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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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