Echinococcus granulosus: Antigen characterization by chemical treatment and enzymatic deglycosylation

F. March, C. Enrich, M. Mercader, F. Sánchez, C. Muñoz, P. Coll, G. Prats

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19 Citations (Scopus)


Parasite antigenic fractions obtained by biochemical purification of sheep hydatid fluid were subjected to enzymatic digestion. The relative mobilities of the 5 and B antigens, before and after treatment, were analyzed by polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot. Antigenic fractions transferred to nitrocellulose were also treated with sodium metaperiodate and concanavalin A. The results indicate that antigen 5 contains a substantial amount of carbohydrates covalently linked to a polypeptide backbone, which strongly bind to concanavalin A and is removed by N-glycosidase F (PNGase F). Antigen 5 possesses complex N-linked oligosaccharides (PNGase F sensitive), without terminal N-acetyl-d-glucosamine residues (N-acetyl-d-glucosaminidase nonsensitive) and has no high-mannose oligosaccharides (endo-β-N-acetylglucosaminidase H nonsensitive). In contrast, the antigen B of low molecular weight is not susceptible to either enzymatic digestions (PNGase F, Endo H, and N-acetyl-d-glucosaminidase) or sodium metaperiodate oxidation and it does not bind to concanavalin A. Polyclonal antibodies prepared against the two antigens reacted with the deglycosylated antigen 5 in Western blot. The dominant epitopes are, therefore, polypeptides, although the presence of carbohydrate epitopes in the native glycoproteins cannot be excluded. © 1991.
Original languageEnglish
Pages (from-to)433-439
JournalExperimental Parasitology
Issue number4
Publication statusPublished - 1 Jan 1991


  • Echinococcus granulosus


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