| Abstract: | ![]()
Six peptides corresponding to various segments of the B subunit of cholera toxin have been synthesized and covalently linked to tetanus toxoid. Of the antibodies raised in rabbits against these conjugates, four crossreacted to different extents with the intact B subunit and whole native cholera toxin. Antisera to the peptide of sequence 75-85 were not crossreactive, whereas elongation by six amino acid residues resulted in a peptide (69-85) leading to antibodies crossreactive with the cholera toxin. Of most interest was peptide CTP3 (50-64), which was the only one that reacted with antisera to cholera toxin and which led to antibodies reacting with the cholera toxin to a similar level as its homologous peptide-antipeptide reaction. Indeed, antisera to CTP3 neutralized significantly the biological activity of cholera toxin, as followed by skin vascular permeability and by fluid accumulation in ligated small intestinal loops of rabbits. |
