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. 1987 Nov;55(11):2541–2545. doi: 10.1128/iai.55.11.2541-2545.1987

Immunization of mice against tetanus with fragments of tetanus toxin synthesized in Escherichia coli.

N F Fairweather 1, V A Lyness 1, D J Maskell 1
PMCID: PMC259939  PMID: 3312002

Abstract

Two recombinant plasmids, pTet11 and pTet18, which express nontoxic protein fragments of tetanus toxin in Escherichia coli, were constructed. pTet11 protein (86 kilodaltons) is a fusion between part of the E. coli trpE protein and 441 amino acids of tetanus fragment C, and pTet18 (63 kilodaltons) consists of part of fragment B and all of fragment C of tetanus toxin. The synthesis of these proteins was induced in E. coli cultures, and the proteins were partially purified. Mice were immunized with these proteins, and dose-dependent titers of anti-tetanus toxoid antibodies were obtained. The proteins were able to induce neutralizing antibodies in mice, as demonstrated by the ability of mice immunized with 1 microgram or more of protein to survive challenge with 10 50% lethal doses of tetanus toxin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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