A fusion protein consisting of beta-galactosidase (GZ) to which was attached at its N-terminus the amino acid sequence corresponding to residues 142-160 of the immunogenic protein VP1 of foot-and-mouth disease virus (FMDV) has been expressed in E. coli. A chemically synthesized section of DNA corresponding to the amino acid sequence 142-160 was inserted into a vector (pXY410) designed to express fusion proteins with the carboxy terminal 1015 amino acids of GZ. The hybrid protein immunopurified by a GZ-specific monoclonal antibody was soluble, retained full GZ activity, and induced virus-neutralizing antibody in guinea pigs and mice. There were significant differences between the responses of individual mice to the FMDV peptide sequence, although the titers against GZ were uniformly high. This variable pattern did not change after hyperimmunization and was demonstrable in a range of mouse strains of different haplotype. The same results were obtained whether the response was measured by virus neutralization or by RIA against the FMDV peptide sequence. The possible reasons for the variable recognition of the FMDV epitopes by individual mice are discussed.

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