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. 1995 Nov;63(11):4476–4480. doi: 10.1128/iai.63.11.4476-4480.1995

Helicobacter pylori cytotoxin: importance of native conformation for induction of neutralizing antibodies.

R Manetti 1, P Massari 1, D Burroni 1, M de Bernard 1, A Marchini 1, R Olivieri 1, E Papini 1, C Montecucco 1, R Rappuoli 1, J L Telford 1
PMCID: PMC173637  PMID: 7591088

Abstract

We have attempted to express the Helicobacter pylori vacuolating cytotoxin in Escherichia coli. Although the 95-kDa VacA polypeptide was expressed abundantly, it completely lacked any biological activity. In addition, this material failed to induce neutralizing antibodies after immunization of rabbits. In contrast, highly purified high-molecular-mass cytotoxin from the supernatant of H. pylori cultures was active in a HeLa cell assay and effectively induced a neutralizing response in rabbits. Neutralizing sera were shown to contain a high proportion of antibodies which recognized conformational epitopes found only on the native toxin. The data indicate that toxin-neutralizing epitopes are conformational and that potential vaccines based on the cytotoxin may benefit from the use of the intact molecule.

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Selected References

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