Release of Glycoprotein (GP1) from the Tegumental Surface ofTaenia soliumby Phospholipase C fromClostridium perfringensSuggests a Novel Protein-Anchor to Membranes

[摘要] In order to explore how molecules are linked to the membrane surface in larvalTaenia solium, whole cysticerci were incubated in the presence of phospholipase C fromClostridium perfringens(PLC). Released material was collected and analyzed in polyacrylamide gels with sodium dodecyl sulfate. Two major bands with apparent molecular weights of 180 and 43 kDa were observed. Western blot of released material and localization assays in cysticerci tissue sections using antibodies against five known surface glycoproteins ofT. soliumcysticerciindicated that only one, previously called GP1, was released. Similar localization studies using the lectins wheat-germ-agglutinin and Concanavalin A showed that N-acetyl-D-glucosamine, N-acetylneuraminic, sialic acid,αmethyl-D-mannoside, D-manose/glucose, and N-acetyl-D-glucosamine residues are abundantly present on the surface. On the other hand, we find that treatment with PLC releases molecules from the surface; they do not reveal Cross Reacting Determinant (CRD), suggesting a novel anchor to the membrane for the glycoprotein GP1.

[学科分类] 基础医学