Proteomic analysis of a 120 kDa protein complex in cyst fluid of Taenia solium metacestode and preliminary evaluation of its value for the serodiagnosis of neurocysticercosis.

Cyst fluid (CF) of Taenia solium metacestode (TsM) is an important source of serodiagnostic antigens. We have investigated the molecular characteristics of the 120 kDa protein complex in TsM CF purified by fast performance liquid chromatography. The structure of the purified protein was characterized by a variety of proteomic analyses. The protein was found to consist of 2 major components of 42-46 and 22-28 kDa, and shared 3 subunits of 14, 16 and 18 kDa. The 42-46 kDa component was determined to contain 3 additional subunits of 22, 28 and 38 kDa. These 6 subunits were shown to originate from either the 14 or 18 kDa precursor. We assessed the antibody reactivity of the native protein, its individual subunits and the recombinant 14 and 18 kDa proteins, and found that the 120 kDa protein, particularly 14 and 18 kDa subunits revealed high reliability for differentiation of active and mixed stage NC from chronic NC. The subunits of the 120 kDa protein complex identified herein represent some of the low-molecular weight glycoproteins which have been described in several previous studies. Recognizing and understanding the structural and immunological relationship of these proteins will facilitate the development of new serodiagnostic assays.