Lectinhistochemical detection of terminal carbohydrate residues in the enteric myxozoan Enteromyxum leei parasitizing gilthead seabream Sparus aurata (Pisces: Teleostei): a study using light and transmission electron microscopy
| Autor: | María J. Redondo, Pilar Alvarez-Pellitero |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Glycan
Glycosylation biology Carbohydrates Lectin Mannose biology.organism_classification Ulex europaeus Immunohistochemistry Wheat germ agglutinin Fucose Enteritis Sea Bream chemistry.chemical_compound Fish Diseases Agglutinin Biochemistry chemistry Concanavalin A Lectins biology.protein Animals Parasitology Myxozoa Protein Binding |
| Zdroj: | Folia parasitologica. 56(4) |
| ISSN: | 0015-5683 |
| Popis: | The presence of terminal carbohydrate residues in Enteromyxum leei (Diamant, Lom et Dyková, 1994) Palenzuela, Redondo et Alvarez-Pellitero, 2002 stages in gilthead seabream intestines was studied at light microscopy (LM) and transmission electron microscopy (TEM) level using lectin histochemical techniques. Abundant mannose and/or glucose residues were demonstrated by the intense staining caused by binding of biotinylated concanavalin A (Con A), at both LM and TEM. A clear positivity was also obtained with Ulex europaeus (UEA I) agglutinin specific for fucose residues. Both lectins stained E. leei proliferative and sporogonic stages, though glycan patterns varied between these developmental stages. Wheat germ agglutinin (WGA) and Bandeiraea simplicifolia lectin I (BSL I) recognised only structures in the sporogonic stages. Faint labelling occurred with Glycine max (SBA) lectin. No staining was obtained with Sambucus nigra (SNA) agglutinin. The TEM studies demonstrated a restricted presence of N-acetyl-D-galactosamine and alpha-D-galactose, whereas glucose/mannose and fucose, the dominant structures, were also present at the parasite membranes and host-parasite interface, suggesting a role in host-parasite interaction. |
| Databáze: | OpenAIRE |
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