Identification of a Gardnerella vaginalis hemoglobin-binding protein.
Previous studies have shown that Gardnerella vaginalis can utilize human hemoglobin as a sole source of iron. In this study, the interaction between human hemoglobin and G. vaginalis cells was investigated. With a solid phase dot blot assay, G. vaginalis cells were shown to bind digoxigenin (DIG)-labeled human hemoglobin. A human hemoglobin-binding protein with an estimated molecular weight of 124 kilodaltons (kDa) was detected by Western blot analysis of G. vaginalis proteins. The hemoglobin-binding activity of this protein was found to be heat stable and was observed in G. vaginalis cells grown under iron-restrictive and iron-replete conditions. The 124-kDa hemoglobin-binding protein was not detected from intact G. vaginalis cells treated with trypsin prior to Western blot analysis, suggesting that this protein was surface exposed.
Jarosik
G P
GP
Department of Biological Sciences, 508 Life Sciences Building, Louisiana State University, Baton Rouge, LA 70803, USA. gjarosi@unix1.sncc.lsu.edu
D001426:Bacterial Proteins; D001667:Binding, Competitive / Q000276:immunology*; D001692:Biological Transport; D015153:Blotting, Western; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006194:Gardnerella vaginalis / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism; D006801:Humans; D011485:Protein Binding
D001426:Bacterial Proteins; D002352:Carrier Proteins; D006454:Hemoglobins; C017206:hemoglobin-binding protein, bacteria