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Molecular characterization of a 23-kilodalton major antigen secreted by Toxoplasma gondii.

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Affiliations

  • 1. Unité Mixte Institut National de la Sante et de la Recherche Medicale U167, Institut Pasteur, Lille, France.
      Authors
    • Cesbron-Delauw MF 1
    (1 author)

Proceedings of the National Academy of Sciences of the United States of America, 01 Oct 1989, 86(19):7537-7541
https://doi.org/10.1073/pnas.86.19.7537 PMID: 2798425 PMCID: PMC298100

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Abstract 

The strategy chosen for cloning potential vaccine antigens of Toxoplasma gondii was based on the hypothesis that the definitive protection observed in natural infection is due to the presence of encysted bradyzoite forms in host tissues throughout life. The antigens released by the bradyzoites would maintain an immune response against the invading tachyzoites. This led us to identify in tachyzoite in vitro translation products a polypeptide of 24 kDa that is an excreted-secreted antigen (ESA) and is cross-reactive with bradyzoites. In addition, the detection of anti-P24 IgG antibodies is correlated with the chronic infection in man. The gene encoding P24 has been isolated, sequenced, and expressed in Escherichia coli and eukaryotic cells. The recombinant proteins were immunogenic in mice, producing anti-native P23 antibodies. Immunocytochemical analysis located the native antigen in the dense granules of both tachyzoite and bradyzoite forms and showed that it is secreted within host-cell-modified phagosome. Moreover 45Ca2+ labeling as well as regional homologies indicate that this protein has Ca2+-binding properties, suggesting its physiological importance in host-cell invasion. P23 is of diagnostic interest as a marker of chronic toxoplasmosis and is proposed as a vaccine component.

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Proc Natl Acad Sci U S A. 1989 Oct; 86(19): 7537–7541.
PMCID: PMC298100
PMID: 2798425

Molecular characterization of a 23-kilodalton major antigen secreted by Toxoplasma gondii.

M F Cesbron-Delauw, B Guy, G Torpier, R J Pierce, G Lenzen, J Y Cesbron, H Charif, P Lepage, F Darcy, J P Lecocq
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Abstract

The strategy chosen for cloning potential vaccine antigens of Toxoplasma gondii was based on the hypothesis that the definitive protection observed in natural infection is due to the presence of encysted bradyzoite forms in host tissues throughout life. The antigens released by the bradyzoites would maintain an immune response against the invading tachyzoites. This led us to identify in tachyzoite in vitro translation products a polypeptide of 24 kDa that is an excreted-secreted antigen (ESA) and is cross-reactive with bradyzoites. In addition, the detection of anti-P24 IgG antibodies is correlated with the chronic infection in man. The gene encoding P24 has been isolated, sequenced, and expressed in Escherichia coli and eukaryotic cells. The recombinant proteins were immunogenic in mice, producing anti-native P23 antibodies. Immunocytochemical analysis located the native antigen in the dense granules of both tachyzoite and bradyzoite forms and showed that it is secreted within host-cell-modified phagosome. Moreover 45Ca2+ labeling as well as regional homologies indicate that this protein has Ca2+-binding properties, suggesting its physiological importance in host-cell invasion. P23 is of diagnostic interest as a marker of chronic toxoplasmosis and is proposed as a vaccine component.

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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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