Molecular and structural analysis of the panallergen profilin B cell epitopes defined by monoclonal antibodies.
Int Immunol
; 14(9): 993-1001, 2002 Sep.
Article
em En
| MEDLINE
| ID: mdl-12202397
ABSTRACT
Interactions of five mouse mAb (10A4, 5F2, 9A7, 9G4 and 3H8) and sunflower profilin were characterized using synthetic overlapping peptides. All the continuous B cell epitopes analyzed in this work were 6-10 amino acids in length, and clustered at the N- and C-terminal alpha-helices and a two-stranded segment composed of residues 40-50. Mutational analysis of the epitopes revealed that single amino acid changes within these peptides had dramatic effects on IgG-binding characteristics. A three-dimensional molecular model of sunflower profilin was generated by homology modeling based on the crystal structure of Arabidopsis thaliana profilin. All but one of the murine B cell epitopes defined in this work were located on the surface of the profilin molecule in the alpha-helices (10A4 and 3H8) or in the turns (5F2 and 9G4). In contrast, 9A7 epitope was located in the profilin core and partially buried by the C-terminal. Two mAb (5F2 and 10A4) inhibited the binding of anti-profilin human IgE up to 52%. In contrast, mAb 3H8 seemed to enhance the binding of anti-profilin IgE of sera from allergic patients.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alérgenos
/
Linfócitos B
/
Mapeamento de Epitopos
/
Epitopos de Linfócito B
/
Proteínas Contráteis
/
Proteínas dos Microfilamentos
/
Anticorpos Monoclonais
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Int Immunol
Ano de publicação:
2002
Tipo de documento:
Article