Antigenicity of a viral peptide displayed on beta-galactosidase fusion proteins is influenced by the presence of the homologous partner protein.
Several beta-galactosidase fusion proteins have been constructed containing the entire VP1 protein from foot-and-mouth disease virus (FMDV) [Corchero et al. (1996) J. Biotechnol. in press]. The antigenicity of the major immunodominant site A (13 amino acids in length) within the VP1 protein has been studied in competitive ELISA using a panel of seven monoclonal antibodies elicited against the whole virus and recognizing B-cell epitopes within this site. None of the fusion proteins is able to reproduce the antigenic profile of FMDV, all of them being less immunoreactive than the virus particles. On the other hand, significant differences in the reactivity of site A are displayed on the different fusion proteins, being for some antibodies about 10-fold. This indicates that the reactivity of a small peptide included in its natural place inside the heterologous domain can be significantly influenced by the position of the homologous partner in the fusion protein.
Corchero
J L
JL
Institut de Biologia Fonamental, Universitat Autònoma de Barcelona, Spain.
Villaverde
A
A
D005537:Aphthovirus / Q000201:enzymology* / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D010446:Peptide Fragments / Q000276:immunology; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000302:isolation & purification; D014764:Viral Proteins / Q000276:immunology*; D001616:beta-Galactosidase / Q000737:chemistry / Q000276:immunology*
D000939:Epitopes; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; D001616:beta-Galactosidase