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IgE response in schistosomiasis japonica: characterization of a cercarial allergen in comparison with purified egg allergens

Published online by Cambridge University Press:  05 June 2009

M. Owhashi ,
Y. Horii  and
A. Ishii
M. Owhashi
Affiliation:
Faculty of Integrated Arts and Sciences, The University of Tokushima, Minami-Johsanjima, Tokushima 770, Japan
Y. Horii
Affiliation:
Department of Veterinary Medicine, Faculty of Agriculture, Miyazaki University, Miyazaki 880, Japan
A. Ishii
Affiliation:
Department of Medical Zoology, Jichi Medical School, Minami-Kawachi, Tochigi 329-04, Japan
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Abstract

The relationship between the cercarial allergen and two previously isolated egg allergens (J1, J2) of Schistosoma japonicum was examined especially in terms of the cross-reactivity between them. Semi-purified cercarial allergen (JAC) was obtained from the crude extract of S. japonicum cercariae by gel chromatography on Sephadex G-200. The apparent molecular weight of JAC was estimated approximately as 60–100 kDa. JAC could bind to Con A-Sepharose, indicating its glycoprotein nature. Three groups of BALB/c mice were immunized with JAC, J1 or J2 using A1(OH)3 as adjuvant, and the cross-reactivity of each antiserum was examined by PCA. Anti-JAC, anti-Jl or anti-J2 serum was highly specific to the corresponding antigen. When IgE-ELISA of S. japonicum patient sera was performed using JAC, J1 or J2 as an antigen, the correlation between anti-J1 and anti-J2 (r = 0.78) was high, whereas the correlation between anti-JAC and anti-J1 (r = 0.27) or between anti-JAC and anti-J2 (r = 0.12) was low. These results suggest that most IgE epitopes on cercarial allergen are independent from those on egg allergens in S. japonicum.

Type
Research Papers
Information
Journal of Helminthology , Volume 71 , Issue 3 , September 1997 , pp. 221 - 226
Copyright
Copyright © Cambridge University Press 1997

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