Go to JCI Insight
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Alerts
  • Advertising/recruitment
  • Subscribe
  • Contact
  • Current Issue
  • Past Issues
  • By specialty
    • COVID-19
    • Cardiology
    • Gastroenterology
    • Immunology
    • Metabolism
    • Nephrology
    • Neuroscience
    • Oncology
    • Pulmonology
    • Vascular biology
    • All ...
  • Videos
    • Conversations with Giants in Medicine
    • Author's Takes
  • Reviews
    • View all reviews ...
    • 100th Anniversary of Insulin's Discovery (Jan 2021)
    • Hypoxia-inducible factors in disease pathophysiology and therapeutics (Oct 2020)
    • Latency in Infectious Disease (Jul 2020)
    • Immunotherapy in Hematological Cancers (Apr 2020)
    • Big Data's Future in Medicine (Feb 2020)
    • Mechanisms Underlying the Metabolic Syndrome (Oct 2019)
    • Reparative Immunology (Jul 2019)
    • View all review series ...
  • Viewpoint
  • Collections
    • Recently published
    • In-Press Preview
    • Commentaries
    • Concise Communication
    • Editorials
    • Viewpoint
    • Top read articles
  • Clinical Medicine
  • JCI This Month
    • Current issue
    • Past issues

  • Current issue
  • Past issues
  • Specialties
  • Reviews
  • Review series
  • Conversations with Giants in Medicine
  • Author's Takes
  • Recently published
  • In-Press Preview
  • Commentaries
  • Concise Communication
  • Editorials
  • Viewpoint
  • Top read articles
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Alerts
  • Advertising/recruitment
  • Subscribe
  • Contact
Top
  • View PDF
  • Download citation information
  • Send a letter
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need Help? E-mail the JCI
  • Top
  • Abstract
  • Version history
  • Article usage
  • Citations to this article

Advertisement

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: JCI | 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: JCI | 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: JCI | PubMed | Google Scholar

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

Find articles by Facon, B. in: JCI | PubMed | Google Scholar

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

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

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

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

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
View PDF
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.

Browse pages

Click on an image below to see the page. View PDF of the complete article

icon of scanned page 458
page 458
icon of scanned page 459
page 459
icon of scanned page 460
page 460
icon of scanned page 461
page 461
icon of scanned page 462
page 462
icon of scanned page 463
page 463
icon of scanned page 464
page 464
Version history
  • Version 1 (February 1, 1992): No description

Article tools

  • View PDF
  • Download citation information
  • Send a letter
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need Help? E-mail the JCI

Metrics

  • Article usage
  • Citations to this article

Go to

  • Top
  • Abstract
  • Version history
Advertisement
Advertisement
Follow JCI:
Copyright © 2021 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

Sign up for email alerts