Candida albicans産生酵素の生体防御機構におよぼす影響

概要

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An aspartic protease from the opportunistic pathogen Candida albicans assessed for both its ability to reduce opsonization and to inactivate the bactericidal activity of normal human serum. Prior to beginning the phagocytosis assay using human polymorphonuclear leukocytes or the bactericidal assay using human serum, human serum was pretreated with the protease. The protease showed strong reduction of the serum bactericidal activity against Escherichia coli and an obvious decrease in the potential for opsonization against Staphylococcus aureus. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the protease degraded immunoglobulin G and complement factor C3. To confirm the degradation of immunoglobulin G by the protease, immunoglobulin G Fc and Fab fragments were used. The protease destroyed Fc, but not Fab fragments as shown by the SDS-PAGE and gel precipitation reaction. Furthermore, the protease degraded α1-protease inhibitor and α2-macroglobulin, well-known as host defense factors, and resulted in a loss of their actions as protease inhibitors against trypsin or chymotrypsin. In conclusion, this study suggests an important function of C. albicans protease. This destruction of serum bactericidal and opsonization reaction may favor the establishment of candidosis.
福岡歯科大学学会の論文
1994-12-31