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Original Articles |
Effect of Iron-Uptake Mechanisms of Staphylococcus
Aureus on the Growth in Human Body Fluids |
Sung-Heui Shin, M.D., Jin-Ho Kim*, Kang-Kil Lee, M.D., Myung-Hee Lee, M.D.
Nam-Woong Yang, M.D. and Yong Lim, M.D. |
Department of Microbiology and Department of Neurology*,
Chosun University School of Medicine, Seoul, Korea |
Vol.32 Num.5 (p366~372)
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Background:We could establish a streptonigrin- resistant strain called SR-1 strain from Staphylococcus aureus ATCC 6538 as a parental strain and characterize SR-1 strain as defective in the iron-uptake mechanisms including production of siderophores and expression of transferrin-binding protein on the cell wall. We performed this study to elucidate effect of the iron- uptake mechanisms on the growth in human body fluids.
Methods:Growth kinetics of SR-1 strain were compared with those of the parental strain and the increase of unsaturated iron-binding capacity (UIBC) was measured. Siderophore production and expression of transferrin-inding protein were detected by CAS diffusion assay and ligand-blot method probed with human transferrin conjugated horseradish peroxidase, respectively, as the strains were cultivated in normal pooled sera, ascitic fluid and pleural effusion.
Results:Siderophores activity in the body fluids could not be detected by the CAS diffusion assay. The parental strain expressed the transferrin-binding protein on the cell wall during the growth in ascites and pleural effusion except the sera whereas SR-1 strain did not. Growth kinetics showed that SR-1 strain grew sluggish compared to the parental strain. The peak of increase of UIBC of the parental strain was observed at the mid-exponential growth phase and the increase of UIBC of SR-1 strain was either lower than that of the parental strain or not changed.
Conclusion:The iron-uptake mechanisms of S. aureus, especially expression of transferrin-binding protein, play a significant role in growing in the body fluids. |
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Keywords : Staphylococcus aureus, Iron, Streptonigrin, Transferrin-binding protein, Siderophores |
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