Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation.
10.3347/kjp.2004.42.2.57
- Author:
Young Bae CHUNG
;
Yoon KONG
;
Hyun Jong YANG
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
sparganum;
antigenicity;
N-glycosylation;
ELISA
- MeSH:
Animals;
Antigens, Helminth/*analysis/chemistry/immunology/metabolism;
Carbohydrates/analysis/immunology;
Chromatography, Affinity;
Chromatography, Ion Exchange;
Electrophoresis, Polyacrylamide Gel;
Enzyme-Linked Immunosorbent Assay;
Epitopes/analysis/immunology;
Glucosaminidase/metabolism;
Human;
Peptide-N4- (N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism;
Periodic Acid/chemistry;
Sparganosis/*parasitology;
Sparganum/immunology/metabolism;
Spirometra/immunology/*metabolism;
Support, Non-U.S. Gov't
- From:The Korean Journal of Parasitology
2004;42(2):57-60
- CountryRepublic of Korea
- Language:English
-
Abstract:
A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electrophoretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-glycosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.
