作者: Martin Knaus
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摘要: Glycans and sugar binding molecules (lectins) form a mutual recognition system which enables parasitic organisms to adhere on host cells migrate target tissue. The aim of the present study was detect localize carbohydrate-binding activities in developmental stages M. cerebralis. The patterns thirteen biotin-labelled neoglycoconjugates were examined histochemically thin-sections infected rainbow trout (Oncorhynchus mykiss) oligochaete (Tubifex tubifex) preparations waterborne triactinomyxon spores. A further characterise glycan epitopes myxospore stage Lectin Western blotting analyses performed by using selected plant lectins (GSA-I, PHA-E, SJA, GSA-II) TAM-antiserum. Glycoproteins isolated lectin affinity chromatography prominent bands characterised mass spectrometry (MALDI/MS). Distinct structure-selective stage-regulated expression certain classes carbohydrate observed. In TAM spores, activity specific for alpha-L-Fuc-BSA-biotin, alpha-D-GalNAc-BSA-biotin, Lac-BSA-biotin und ASF-biotin up-regulated polar capsules; shell valves showed no activity. gut T. tubifex, capsules parasite strong positive reaction only with beta-D-GlcNAc-BSA-biotin. fish cartilage negative, but spore broad range activities. No detected either alpha 2-6- or 2-3-linked N-acetyl-D-neuraminic acid. An adhesion assay myxospores found specifically matrices containing residues lactose, fucose, galactose, N-acetyl-D-galactosamine N-acetyl-D-glucosamine. Furthermore it identified that glycoepitopes contain motifs reactive PHA-E (proteins 7-70 kDa), SJA (7-70 GSA-I (10-209 kDa) GSA-II (5-40 kDa). Mcgp33, glycoprotein is (about 33 exclusively expressed stage. application antiserum against spores cerebralis indicates differences antigenicity glycoproteins from both, myxospores. This first investigation identifies phylum myxozoa. participation suspected mediate complex process recognition, invasion. Furthermore, can participate protection environmental forces may generate immune reactions during migration