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Research Article Free access | 10.1172/JCI115606

Diagnostic value of a synthetic peptide derived from Echinococcus granulosus recombinant protein.

M Chamekh, H Gras-Masse, M Bossus, B Facon, C Dissous, A Tartar, and A Capron

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

Find articles by Chamekh, M. in: PubMed | Google Scholar

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

Find articles by Gras-Masse, H. in: PubMed | Google Scholar

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

Find articles by Bossus, M. in: PubMed | Google Scholar

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

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Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

Find articles by Dissous, C. in: PubMed | Google Scholar

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

Find articles by Tartar, A. in: PubMed | Google Scholar

Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U167-CNRS 624, Institut Pasteur, Lille, France.

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Published February 1, 1992 - More info

Published in Volume 89, Issue 2 on February 1, 1992
J Clin Invest. 1992;89(2):458–464. https://doi.org/10.1172/JCI115606.
© 1992 The American Society for Clinical Investigation
Published February 1, 1992 - Version history
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Abstract

A specific monoclonal antibody (MAb; EG 02 154/12) directed against a protein epitope of Echinococcus granulosus antigen 5 was used to screen a cDNA library constructed from E. granulosus protoscoleces RNA. One clone designated Eg14 was selected and shown to code for an amino acid sequence partially homologous to that of the clone Eg6 previously identified with the same MAb. Hydrophobic cluster analysis showed that both recombinant antigens may adopt a similar alpha-helical organization and share a common conformational epitope. A synthetic peptide (89-122) mimicking the conformational site of Eg6 and Eg14 was constructed and demonstrated to be able to inhibit binding of the MAb and human hydatid sera to the Eg6 fusion protein (FP6) or to native hydatid antigens. To assess the diagnostic value of the peptide 89-122, we tested sera from patients infected with different parasites for their antibody reactivity with this peptide in ELISA. A high binding sensitivity and specificity of IgG-A-M antibodies were obtained with E. granulosus-infected patient sera. Moreover, the peptide 89-122 was found to be specifically recognized by IgE antibodies from patients with hydatid disease. These results indicate the particular interest of this synthetic peptide as a standardized antigen in diagnosis and treatment surveillance of hydatidosis.

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