Preliminary analysis of taenia multiceps metacestode antigens by two-dimensional electrophoresis

ABSTRACT

Taenia multiceps is a cestode parasite with its larval stage [metacestode], Coenurus cerebralis, mainly encysts in the central nervous system of sheep and other livestock causing cerebralis coenurosis. Since treatment of coenurosis with chemotherapy showed little effect and surgical removal of cysts is not advisable in field conditions, vaccination is useful to control coenurosis. Previous study indicated that immunization with T. multiceps metacestode antigens could induce protection in sheep against coenurosis, so the aim of this study was to identify T. multiceps metacestode antigens in order to find potential vaccine development candidates for further study. The protein extracts from the larval T. multiceps were analyzed by twodimensional electrophoresis [2-DE] and characterized by mass spectrometry. A total of 150 protein spots were detected with isoelectric point [pI] value from 4.97 to 9.65 and molecular weight from 14 to 98 kDa. Twenty-two protein identities were determined by mass spectrometry and 15 unique proteins were obtained. Functional annotation revealed that some of these proteins are involved in catalytic activity, binding, metabolic, cellular process and stress response. Among these molecules are antioxidant proteins [peroxiredoxin and glutathione-S-transferase], glycolytic enzymes [malate dehydrogenase and enolase], proteins with chaperone activity [heat shock protein 70 and small heat shock protein], and structural proteins [actin, actin modulator protein and paramyosin]. The identification of T. multiceps metacestode protein will provide valuable information to elucidate their specific roles in the parasitism and screen new targets for vaccine development