Lectin interactions with the variant surface glycoprotein from Trypanosoma brucei brucei incorporated into liposomes.
The variant specific surface glycoprotein from Trypanosoma brucei brucei is incorporated into lipid vesicles using 8M urea as an unfolding reagent. Pronase treatment of these proteoliposomes removes most of the protein, leaving a glycophospholipopeptide which is the membrane attachment site. We show here that lectins, specific for mannose and galactose are able to recognize oligosaccharide residues on these proteoliposomes, using a straightforward aggregation assay. The relevance of these results obtained with the liposome model system to the accessibility of the surface antigens in living trypanosomes is discussed.
D000818:Animals; D002462:Cell Membrane / Q000032:analysis; D003208:Concanavalin A / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism*; D008358:Mannose; D009844:Oligosaccharides / Q000378:metabolism; D019887:Peanut Agglutinin; D014346:Trypanosoma brucei brucei / Q000032:analysis*; D014508:Urea; D014643:Variant Surface Glycoproteins, Trypanosoma
D006023:Glycoproteins; D037102:Lectins; D008081:Liposomes; D009844:Oligosaccharides; D019887:Peanut Agglutinin; D014643:Variant Surface Glycoproteins, Trypanosoma; D003208:Concanavalin A; D014508:Urea; D008358:Mannose; D005690:Galactose