SDS-PAGE Protein Pattern and Antigenicity Cross Reaction of Human Schistosomes
Nahed A.A. EL-Ossily, Doaa A. Yones, Mohamed El-Salahy M.M. Monib, Ahmed S.A. Hassanin and Refaat M.A. Khalifa
DOI : 10.3844/ajidsp.2016.20.29
American Journal of Infectious Diseases
Volume 12, Issue 1
Schistosomiasis is one of the most important neglected tropical diseases. Its control depends on treatment with the available drug praziquantel. No vaccine exists despite the intense search for molecular candidates and adjuvant formulations over the last three decades. The present study aimed to compare the antigenic protein structures of Schistosoma mansoni, S. haematobium, Fasciola. hepatica and Echinococus granulosus hydatid cyst and to find out shared antigens among these species which could be recognized by S. mansoni antibodies. Antigenic protein structures were recognized through the use of Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) after Coomassie blue staining. Antigenic differences between the detected polypeptides and positive S. mansoni serum were performed using Western blotting. The SDS-PAGE profiles of the tested parasites revealed many polypeptides ranging from 15-206 kDa. Some of these proteins were shared between all the examined parasites e.g.: 52-47 and 15-25 kDa. Some ranged from 42-38 kDa were shared with both examined schistosomes and hydatid cyst fluid. Bands ranged from 58-55 kDa were common in S. mansoni, S. haematobium and F. hepatica. The protein bands of about 60 kDa crossly reacted with S. mansoni serum and detected in all used antigens. The detected immunoreactive proteins from other helminthes could be used to develop potential vaccine against schistosomiasis.
© 2016 Nahed A.A. EL-Ossily, Doaa A. Yones, Mohamed El-Salahy M.M. Monib, Ahmed S.A. Hassanin and Refaat M.A. Khalifa. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.