Molecular analysis of peptides from the GH loop of foot-and-mouth disease virus C-S30 using surface plasmon resonance: a role for kinetic rate constants

• Tipo: Artigo em Revista Científica Internacional
• Data: 2000

Autores

Gomes, P (Autor) FCUP; Giralt, E (Autor) Outra; Andreu, D (Autor) Outra

Revista

Título: Molecular Immunology

Vol. 37

Páginas: 975-985

ISSN: 0161-5890

Editora: Elsevier

Indexação

ISI Web of Knowledge - 4 Citações

Scopus - 6 Citações

Classificação Científica

FOS: Ciências médicas e da saúde > Medicina básica

Outras Informações

ID Authenticus: P-007-9JY

DOI: 10.1016/s0161-5890(01)00014-1

Abstract (EN): A foot-and-mouth disease virus (FMDV) field variant, isolate C-S30 (also named C-1-Barcelona), is known to contain four changes within the main antigenic site A (GH loop of capsid protein VP1, residues 136-150), at least one of which (Leu147 --> Val) involves a highly conserved position, critical for antibody recognition in the reference strain C-S8c1. However, immunoenzymatic analysis of FMDV C-S30 showed it was recognised by 4C4, a monoclonal antibody that specifically targets site A. This remarkable behaviour has led us to analyse the individual and combined contributions of the four mutations to the antigenicity of C-S30, by surface plasmon resonance (SPR) and enzyme-linked immunosorbent assay (ELISA) studies of pentadecapeptides displaying all possible combinations of the four replacements. Analysis of this family of C-S30-derived analogues shows a certain level of antibody recognition by SPR. In addition, SPR data suggest that kinetic rate constants provide an indirect measure, on the one hand, of paratope accessibility (association rate constant) and, on the other hand, of peptide fitness to the same paratope (dissociation rate constant).

Idioma: Inglês

Tipo (Avaliação Docente): Científica