1921
Volume 35, Issue 4
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

soluble egg antigen (Sh) was prepared from eggs isolated from the livers of hamsters or mice infected for at least 3 months. Immunoaffinity purified egg antigens (Sh) were isolated by first passing Sh through a column containing anti- hamster IgG coupled to CNBr-activated Sepharose 4B, and recycling the unbound fraction until no more bound material could be eluted with an acid wash. The unbound fraction was then filtered through a second antibody affinity column containing anti- hamster IgG, and in the acid eluate the Sh antigens were obtained. This antigenic preparation was shown by PAGE to contain at least 6 distinct bands ranging in molecular weight (M) from 116 to <31 Kd. A 40 Kd polypeptide was identified by both silver staining and EITB as specific for eggs. In addition, a 55 Kd worm-egg shared antigen was identified as a prominent band in EITB expressed during a primary hamster infection. The sera from hamsters harboring patent or infections were reacted by ELISA with Sh antigens. The anti-Sh sera showed significantly higher absorbance values than the anti-Sm sera, demonstrating that only a minor population of cross-reactive egg antigens is still present in the Sh antigens. Sera collected weekly for 13 weeks from hamsters with a primary infection of were then tested by ELISA against Sh, Sh and Sm antigens. Antibody levels against both Sh and Sm were shown to increase early in infection (2 weeks). Moreover, antibody levels to Sh did not increase until week 5 post-infection. These findings suggest that the purification procedure utilized results in the elimination of most of the worm antigens cross-reactive with eggs. The Sh antigens had shown a high degree of of sensitivity and stage-species specificity also suggesting their potential as antigens for the immunodiagnosis of schistosomiasis haematobia.

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/content/journals/10.4269/ajtmh.1986.35.777
1986-07-01
2017-11-21
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http://instance.metastore.ingenta.com/content/journals/10.4269/ajtmh.1986.35.777
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  • Accepted : 03 Mar 1986

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