Provided are antibodies detected C. albicans antigens by indirect immunofluorescence assay, enzyme-linked immunosorbent assay ELISA, and Western blotting. The antigens containing the epitopes recognized by the antibody could be extracted from blastoconidia by dithiothreitol, suggesting attachment to the cell wall via sulfhydryl bonds. Epitope detection by the antibody was sensitive to treatment of C.albicans blastoconidia with sodium periodate, but not proteinase K, indicating the cognate epitopes were composed of carbohydrate.
Figure 1 Human Anti-C. albicans Antibody (λ2-18) in IF.
IFA detection of binding of scFv5 and scFv12 to Candida species. Paired panels are immunofluorescent and bright-field photomicrographs of the same microscopic fields. (A) scFv λ2-18 binding to C. albicans, showing the highest intensity for binding to the blastoconidia as previously described.
Bliss, J. M., Sullivan, M. A., Malone, J., & Haidaris, C. G. (2003). Differentiation of Candida albicans and Candida dubliniensis by using recombinant human antibody single-chain variable fragments specific for hyphae. Journal of clinical microbiology, 41(3), 1152-1160.
Figure 2 Human Anti-C. albicans Antibody (λ2-18) in IF.
IFA detection of scFv5 and scFv12 binding to C. albicans after proteinase K treatment. Paired panels are immunofluorescent and bright-field photomicrographs of the same microscopic fields. C. albicans filaments were subjected to proteinase K digestion, and the presence of antigen was detected by IFA. Mock-treated cells were treated with buffer alone. scFv λ2-18 has previously been shown to recognize a carbohydrate epitope.
Bliss, J. M., Sullivan, M. A., Malone, J., & Haidaris, C. G. (2003). Differentiation of Candida albicans and Candida dubliniensis by using recombinant human antibody single-chain variable fragments specific for hyphae. Journal of clinical microbiology, 41(3), 1152-1160.
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