Reactivity of Synthetic SAG1 (p30) Peptide Sequences with RH, S273 and Beverley Strain-Induced Anti-Toxoplasma gondii Antibodies
| Autor: | Florencia G. Claveria, Yoshiyuki Maki, Hideyuki Nagasawa, Yoshitaka Omata, Naoyoshi Suzuki, M. Kato, T. Tanaka, K Sanda |
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| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
Virulence Toxoplasma gondii Peptide Cell Biology General Medicine Biology biology.organism_classification Virology Pathology and Forensic Medicine Amino acid Microbiology law.invention chemistry Antigen law parasitic diseases Recombinant DNA biology.protein Antibody Molecular Biology Peptide sequence |
| Zdroj: | Pathobiology. 74:50-56 |
| ISSN: | 1423-0291 1015-2008 |
| Popis: | Objectives: We compared the reactivity of IgG1 and IgG2a antibodies in mouse sera after infection with virulent RH and low-virulent S273 and Beverley strains of Toxoplasma gondii against RH SAG1 recombinant p30 (rp30) and synthetic SAG1 peptides. Methods: Infected mouse serum samples were collected 9 days after infection, and the level of total IgG, IgG1 and IgG2a against the RH SAG1 rp30 protein and twenty peptides of the RH SAG1 protein were assessed. The glycosylphosphatidylinositol (GPI) modification site, the hydrophilic-hydrophobic structure, the transmembrane region and the secondary structure of the SAG1 sequence of virulent and low-virulent strains were analyzed using software. Results: The virulent strain-infected mice produced a higher level of IgG1 but a lower IgG2a against the rp30 antigen, while the low-virulent strain-infected mice produced a higher level of IgG2a than the virulent strain. The difference in the secondary structure of SAG1 protein between the virulent and low-virulent strain was largely confined to amino acid positions 291–336, showing mutations and GPI anchor site. Conclusion:The difference in the reactivity of IgG against the rp30 antigen and synthetic peptides between virulent and low-virulent strains points to the importance of the primary and secondary structure assumed by antigens in the activation of Th cells and, subsequently, in the induction of IgG and its subclasses. |
| Databáze: | OpenAIRE |
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