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pubmed:abstractText |
Although Neisseria gonorrhoeae can use haem as the sole exogenous iron source for growth in vitro, the mechanism of haem-iron uptake in the gonococcus is unknown. Two haemin-binding proteins (HmBPs) of 97 and 44 Kda were isolated by batch ligand affinity-chromatography from whole cells or total membranes of gonococci grown under iron-limited conditions but not from those grown under iron-sufficient conditions. Competition binding experiments indicated that the haemin-protein interaction was specific; only haemin or haem-containing proteins, such as human haemoglobin or equine cytochrome c111, but not protoporphyrin IX, iron loaded human transferrin or lactoferrin, could abrogate binding. Identical HmBPs were isolated from three other clinical gonococcal strains, suggesting that these may be interstrain structural and functional homogeneity amongst these polypeptides.
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