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 Lettjournal_title
FEMS microbiology lettersauthors
Corchero JL,Villaverde Adoi
10.1111/j.1574-6968.1996.tb08559.xsubject
Has Abstractpub_date
1996-11-15 00:00:00pages
77-82issue
1eissn
0378-1097issn
1574-6968pii
0378109796003904journal_volume
145pub_type
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