Probing degeneracy in antigen-antibody recognition at the immunodominant site of foot-and-mouth disease virus

• Tipo: Artigo em Revista Científica Internacional
• Data: 2002

Autores

Gomes, P (Autor) FCUP; Giralt, E (Autor) Outra; Ochoa, W (Autor) Outra; Verdaguer, N (Autor) Outra; Andreu, D (Autor) Outra

Revista

Título: Journal of Peptide Research

Vol. 59

Páginas: 221-231

ISSN: 1397-002X

Editora: Blackwell

Indexação

ISI Web of Knowledge - 3 Citações

Scopus - 3 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-000-PHR

DOI: 10.1034/j.1399-3011.2002.01959.x

Abstract (EN): Antigen-antibody binding is regarded as one of the most representative examples of specific molecular recognition in nature. The simplistic view of antigenic recognition in terms of a lock-and-key mechanism is obsolete, as it is evident that both antigens and antibodies are flexible and can undergo substantial mutual adaptation. This flexibility is the source of complexities such as degeneracy and nonadditivity in antigenic recognition. We have used surface plasmon resonance to study the effects of combining multiple amino acid replacements within the sequence of the antigenic GH loop of foot-and-mouth disease virus, Our aim was 2-fold: to explore the extent to which antigenic degeneracy can be extended in this particular case, and to search for potential nonadditive effects in introducing multiple amino acid replacements. Combined Spain analysis of one such multiply substituted peptide by SPR, solution NMR and X-ray diffraction shows that antigenic degeneracy can be expected as long as residues directly interacting with the paratope are conserved and the peptide bioactive folding is unaltered.

Idioma: Inglês

Tipo (Avaliação Docente): Científica