Analysis of lectin- and snail plasma-binding glycopeptides associated with the tegumental surface of the primary sporocysts of Schistosoma mansoni.
Carbohydrates associated with the tegumental surface of Schistosoma mansoni primary sporocyst may serve as potential receptors for mediating recognition by the internal defence system of the molluscan host, Biomphalaria glabrata. Therefore, a combination of SDS-PAGE and lectin probe analyses were carried out on biotin-labelled tegumental glycopeptides as a first step to defining the carbohydrates expressed at the sporocyst surface. The majority of surface polypeptides, ranging in relative molecular masses from 27 to 113 kDa, reacted with horseradish peroxidase-labelled Canavalia ensiformis (Con A), Erythrina corallodendron (ECA), Glycine max (SBA) and Triticum vulgaris (WGA) lectins indicating that most, if not all, tegumental proteins are glycosylated. However, differences in the binding of some lectins to individual glycopeptides suggest a degree of heterogeneity in the structure/composition of sugar moieties comprising these surface glycoconjugates. This notion is supported by the finding that the fucose-specific Tetragonolobus purpureas (TPA) lectin only reacted with approximately 50% of glycopeptides identified at the tegumental surface. Experiments employing biotin-labelled plasma (cell-free haemolymph) from S. mansoni-susceptible and -resistant B. glabrata snails as probes, further demonstrated that many of the identified surface glycoproteins also serve as plasma-binding sites for both snail strains. Binding interactions between plasma and sporocyst surface glycoproteins appeared to be, at least in part, mediated by carbohydrates since periodate treatment of sporocyst proteins or pre-incubation of plasma with the glycoproteins, fetuin or mucin, resulted in a decrease in plasma reactivity to blotted larval proteins.
Johnston
L A
LA
Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison 53706, USA.
Yoshino
T P
TP
D000818:Animals; D001700:Biomphalaria / Q000469:parasitology; D001710:Biotin; D001769:Blood; D006020:Glycopeptides / Q000032:analysis* / Q000737:chemistry; D006031:Glycosylation; D015801:Helminth Proteins / Q000032:analysis* / Q000737:chemistry; D037102:Lectins / Q000378:metabolism*; D008970:Molecular Weight; D012550:Schistosoma mansoni / Q000737:chemistry*; D014357:Trypsin
D006020:Glycopeptides; D015801:Helminth Proteins; D037102:Lectins; D001710:Biotin; D014357:Trypsin