Immunological characterization of a rotavirus-neutralizing epitope fused to the cholera toxin B subunit.

@article{Gonzlez1993ImmunologicalCO,
  title={Immunological characterization of a rotavirus-neutralizing epitope fused to the cholera toxin B subunit.},
  author={Ra{\'u}l C{\'e}sar Romero Gonz{\'a}lez and Joaqu{\'i}n S{\'a}nchez and BarbaraJ. Stoll Jan Holmgren and Susana Gonz{\'a}lez L{\'o}pez and Carlos F Arias},
  journal={Gene},
  year={1993},
  volume={133 2},
  pages={
          227-32
        }
}
A highly conserved neutralizing epitope from the surface protein VP4 (amino acids 296-313) of human rotaviruses was genetically fused to the B subunit of cholera toxin (CTB). Synthetic oligodeoxyribonucleotides encoding the VP4 peptide were inserted between the 3' end of the DNA that codes for the leader peptide, and the 5' end of the gene encoding mature CTB. The hybrid protein synthesized in Escherichia coli was found to maintain the ability of CTB to pentamerize, and to adhere to its cell… CONTINUE READING
BETA