Antigenicity of a viral peptide displayed on beta-galactosidase fusion proteins is influenced by the presence of the homologous partner protein.

Abstract:

: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.

journal_name

FEMS Microbiol Lett

authors

Corchero JL,Villaverde A

doi

10.1111/j.1574-6968.1996.tb08559.x

subject

Has Abstract

pub_date

1996-11-15 00:00:00

pages

77-82

issue

1

eissn

0378-1097

issn

1574-6968

pii

0378109796003904

journal_volume

145

pub_type

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