Identification of a Gardnerella vaginalis hemoglobin-binding protein

Curr Microbiol. 2001 Jan;42(1):49-52. doi: 10.1007/s002840010177.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Binding, Competitive / immunology*
  • Biological Transport
  • Blotting, Western
  • Carrier Proteins / chemistry
  • Carrier Proteins / isolation & purification*
  • Carrier Proteins / metabolism
  • Gardnerella vaginalis / metabolism*
  • Hemoglobins / metabolism
  • Humans
  • Protein Binding


  • Bacterial Proteins
  • Carrier Proteins
  • Hemoglobins
  • hemoglobin-binding protein, bacteria