Six Gardnerella vaginalis strains were examined for the ability to utilize various iron-containing compounds as iron sources. In a plate bioassay, all six strains acquired iron from ferrous chloride, ferric chloride, ferrous sulfate, ferric ammonium citrate, ferrous ammonium sulfate, bovine and equine hemin, bovine catalase, and equine, bovine, rabbit, and human hemoglobin. All six strains also acquired iron from human lactoferrin, but not from human transferrin, as determined by a liquid broth growth assay. Siderophore production was detected in eight G. vaginalis strains by the chrome azurol S universal chemical assay. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the cytoplasmic membrane proteins isolated from G. vaginalis 594 grown under iron-replete and iron-restricted conditions revealed several iron-regulated proteins ranging in molecular mass from 33 to 94 kDa. These results indicate that G. vaginalis may acquire iron from iron salts and host iron compounds.
Previous studies have shown that Gardnerella vaginalis can utilize iron-loaded human lactoferrin as a sole source of iron. In this study, G. vaginalis cells were shown to bind digoxigenin (DIG)-labeled human lactoferrin in a dot blot assay. Using the DIG-labeled human lactoferrin, a 120-kDa human lactoferrin-binding protein was detected by Western blot analysis of G. vaginalis proteins. The lactoferrin-binding activity of this protein was found to be heat stable. Competition studies indicated that this binding activity was specific for human lactoferrin. Treatment of G. vaginalis cells with proteases suggested that this protein was surface exposed. An increase in lactoferrin binding by the 120-kDa protein was observed in G. vaginalis cells grown under ironrestrictive conditions, suggesting that this activity may be iron regulated.
It has been previously demonstrated that Gardnerella vaginalis could acquire iron from a number of different iron‐containing compounds, including heme. In this study, the direct binding of heme by G. vaginalis strains was demonstrated utilizing a liquid broth heme‐binding assay. Competition studies demonstrated that pretreatment of G. vaginalis cells with other iron sources such as hemoglobin, catalase, and lactoferrin did not affect heme binding. Also, heme binding was not inhibited by preincubation of G. vaginalis cells with protoporphyrin IX. Two potential heme‐binding proteins with estimated molecular weights of 30 and 70 kDa were isolated using heme‐agarose batch affinity chromatography.
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