The identification of surface interaction of apotransferrin with Candida albicans

다국어 초록 (Multilingual Abstract)

Our recent data indicate that apotransferrin, aniron-chelating protein, has anti-candidal activity by bindingto the Candida albicans surface rather than just simpleiron-chelation. Following that study, in this present study,we investigated the nature of the candidal surface substancethat is responsible for the anticandidal activity byusing 59Fe3?-apotransferrin and biological assay methods.
Data resulting from the binding studies showed that theyeast cells had one class of binding sites as analyzed by theScatchard equation, and the binding was specific asdetermined by competitive binding assay with unlabeledand labeled transferrin. All these observations indicate thatthere is a substance(s) that mediates the binding. Thus, amannoprotein-like substance was extracted from C. albicanssurface using hot water-treatment. Radioisotopebinding study revealed that the substance blocked thetransferrin binding. At 25 lg of IHS (inhibitory substance)addition, there was 65 % inhibition of the transferrinbinding to C. albicans (5 9 107 cells/ml) (P\0.05). Theblockage of the transferrin binding disrupted the anticandidalactivity of transferrin, resulting in a full recoveryfrom growth inhibition. These results explain our previousobservation that there is partial growth inhibition when C.
albicans interacts directly with iron-saturated transferrin(100 %). Thus, it was concluded that a candidate fortransferrin receptor is involved in the anticandidal activityof transferrin when in direct contact with C. albicans.

참고문헌 (Reference)

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