Immunochemical purification and characterization of a 74.0-kDa Schistosoma mansoni antigen
| Autor: | A M, Attallah, S A, El Masry, H, Ismail, H, Attia, M, Abdel Aziz, A S, Shehatta, A, Tabll, A, Soltan, A, El Wassif |
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| Rok vydání: | 1998 |
| Předmět: |
Adult
Mice Inbred BALB C Hybridomas Adolescent Blotting Western Antibodies Helminth Immunization Passive Antibodies Monoclonal Enzyme-Linked Immunosorbent Assay Schistosoma mansoni Middle Aged Peptide Mapping Chromatography Affinity Schistosomiasis mansoni Mice Antigens Helminth Child Preschool Animals Humans Electrophoresis Polyacrylamide Gel Female Amino Acids Child Chromatography High Pressure Liquid Aged |
| Zdroj: | The Journal of parasitology. 84(2) |
| ISSN: | 0022-3395 |
| Popis: | A polypeptide antigen of 74.0 kDa molecular weight was detected in the antigenic extracts of the 3 developmental stages of Schistosoma mansoni (eggs, cercariae, and adult worms) by western blotting using BRL4 monoclonal antibody (mAb) that significantly protected mice at the levels of 51.6%, 42%, and 53.8% against challenge S. mansoni infection in 3 separate experiments. This antigen was isolated and purified from crude soluble worm antigen preparation by immunoaffinity chromatography using CNBr-activated sepharose-4B beads coupled with the BRL4 mAb. The purified antigen showed a single peak when analyzed by both high-performance liquid chromatography and high-performance capillary electrophoresis. The 74-kDa antigen was characterized as a protein in nature with 56.9% hydrophilic amino acids and 43.1% hydrophobic amino acids. This antigen was detected in 93% of urine samples from infected cases with specificity of 89% among noninfected cases using an enzyme immunoassay-fast dot-enzyme-linked immunosorbent assay based on BRL4 mAb. |
| Databáze: | OpenAIRE |
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