Abstract:
: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.
journal_name
Parasitologyjournal_title
Parasitologyauthors
Lee EG,Bae YA,Jeong YT,Chung JY,Je EY,Kim SH,Na BK,Ju JW,Kim TS,Ma L,Cho SY,Kong Ydoi
10.1017/S0031182005008504subject
Has Abstractpub_date
2005-12-01 00:00:00pages
867-79issue
Pt 6eissn
0031-1820issn
1469-8161pii
S0031182005008504journal_volume
131pub_type
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