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SDS-PAGE Protein Pattern and Antigenicity Cross Reaction
of Human Schistosomes

Research Authors
Nahed A.A. EL-Ossily, 1Doaa A. Yones, 1Mohamed El-Salahy M.M. Monib,
2Ahmed S.A. Hassanin and 1Refaat M.A. Khalifa
Research Department
Research Journal
American Journal of Infectious Diseases
Research Publisher
Science Publication
Research Rank
1
Research Vol
12 (1)
Research Website
http://thescipub.com/journals/ajid/apc
Research Year
2016
Research_Pages
20.29
Research Abstract

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.