Hindawi Publishing Corporation Journal of Biomedicine and Biotechnology Volume 2010, Article ID 910375, 6 pages doi:10.1155/2010/910375 Research Article Release of Glycoprotein (GP1) from the Tegumental Surface of Taenia solium by Phospholipase C from Clostridium perfringens Suggests a Novel Protein-Anchor to Membranes Abraham Landa, 1 Kaethe Willms, 1 and Juan Pedro Laclette 2 1 Departamento de Microbiolog´ ıa y Parasitolog´ ıa, Facultad de Medicina, UNAM, M´ exico 04510, DF, Mexico 2 Departamento de Inmunolog´ ıa, Instituto de Investigaciones Biom´ edicas, UNAM, M´ exico 04510, DF, Mexico Correspondence should be addressed to Abraham Landa, landap@servidor.unam.mx Received 21 August 2009; Accepted 12 October 2009 Academic Editor: Luis I. Terrazas Copyright © 2010 Abraham Landa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. In order to explore how molecules are linked to the membrane surface in larval Taenia solium, whole cysticerci were incubated in the presence of phospholipase C from Clostridium 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 43kDa were observed. Western blot of released material and localization assays in cysticerci tissue sections using antibodies against five known surface glycoproteins of T. solium cysticerci indicated 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. 1. Introduction The tegumental surface of larval cestodes is in direct contact with the host tissues and plays a crucial role in the survival of the parasite. Glycoproteins and complex carbohydrates have been detected on the surface of the larvae in several species of cestodes through the use of histochemical techniques [1–4]. The tegumental membrane of Taenia solium cysticerci exhibits a dense glycocalyx composed of abundant carbo- hydrates and glycoproteins such as GP1, GP2-3, GP6, and GP7 [5–7]. However, little is known about the anchorage of the glycoproteins and glycolipids to the membrane. In other platyhelminths, several studies have also shown that alka- line phosphatase, acetyl-cholinesterase, and several surface proteins of 18, 22, 28, 32, 38, and 200 kDa are anchored to the tegumental membrane via glycosyl-phosphatidyl-inositol (GPI) in adult and somules of Schistosoma mansoni [8– 10]. Moreover, the apical gut surface protein (p46 Ga1 ) of Haemonchus contortus is also anchored through GPI [11]. Likewise, Sm25, a major schistosome tegumental glycopro- tein, is attached by palmitic acid to the membrane [12]. Cestodes, trematodes, and other platyhelminths have triglycerides and cholesterol as the major neutral lipids and phosphatidylcholine, phospatidylethanolamine, and phos- phatidylserine as the major phospholipids [13, 14]. Gly- colipids, galactosylceramides, and glycosphingolipids have been identified in tegumental membranes of Spirometra mansonoides, Echinococcus multilocularis, and Hymenolepis diminuta [15–17]. A novel glycosphingolipid named AGL containing inositol phosphate as acidic group has been found in the nematode Ascaris sum [18]. The purpose of this study was to determine the compo- nents that are released from the surface of T. solium cysticerci by phospholipase C from Clostridium perfringens (PLCs). The GP1 molecule was removed by PLC. Finally, complex carbohydrates that are ligands for wheat germ agglutinin (WGA) and concanavalin A (ConA) were also released from the tegumental surface. These results suggest that a different kind of glycoprotein anchor might be present in taeniids.