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Diagnostic potential of Fasciola gigantica-derived 14.5 kDa fatty acid binding protein in the immunodiagnosis of bubaline fascioliasis

Published online by Cambridge University Press:  13 March 2012

G. Allam*
Affiliation:
Department of Zoology, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt Department of Microbiology, College of Medicine, Taif University, Taif, Saudi Arabia
I.R. Bauomy
Affiliation:
Department of Parasitology, Theodor Bilharz Research Institute, Giza, Egypt
Z.M. Hemyeda
Affiliation:
Department of Zoology, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt
T.M. Diab
Affiliation:
Department of Parasitology, Theodor Bilharz Research Institute, Giza, Egypt
T.F. Sakran
Affiliation:
Department of Zoology, Faculty of Science, Beni-Suef University, Beni-Suef, Egypt
*
*Fax: +966 2 7250528 E-mail: g.allam@tu.edu.sa; gm_allam@yahoo.com

Abstract

The 14.5 kDa fatty acid binding protein (FABP) was isolated from the crude extract of adult Fasciola gigantica worms. Polyclonal anti-FABP IgG was generated in rabbits immunized with prepared FABP antigen. Sandwich enzyme-linked immunosorbent assay (ELISA) was applied to detect coproantigen in stools and circulating Fasciola antigen (CA) in sera of 126 water buffaloes by using purified and horseradish peroxidase (HRP)-conjugated anti-FABP IgG. Sandwich ELISA sensitivity was 96.97% and 94.95%; while specificity was 94.12% and 82.35% for coproantigen and CA detection, respectively. However, sensitivity and specificity of the Kato–Katz technique was 73.74% and 100%, respectively. The diagnostic efficacy of sandwich ELISA was 96.55% and 93.1% for coproantigen and CA detection, respectively. In contrast, the diagnostic efficacy of the Kato–Katz technique was 77.59%. In conclusion, these results demonstrate that the purified 14.5 kDa FABP provides a more suitable antigen for immunodiagnosis of early and current bubaline fascioliasis by using sandwich ELISA.

Type
Research Papers
Copyright
Copyright © Cambridge University Press 2012 

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