Purification of Yersiniabactin: A Siderophore and Possible Virulence Factor of Yersinia Enterocolitica

J Gen Microbiol. 1993 Sep;139(9):2159-65. doi: 10.1099/00221287-139-9-2159.


HPLC analysis revealed that Yersinia enterocolitica WA-C produced two substances under iron-limiting conditions one of which was identified as 2,3-dihydroxybenzoyl-L-serine. The other compound had iron-complexing activity and was called yersiniabactin. The fur mutant H1852 was shown to produce yersiniabactin constitutively in an iron-independent manner. Yersiniabactin was isolated by ethyl acetate extraction from the spent medium of H1852, size-fractionation chromatography and preparative HPLC. A catechol function was demonstrated with different chemical assays and by UV-visible spectroscopy. The molecular mass of yersiniabactin was determined to be 482 Da. Purified yersiniabactin stimulated growth of Y. enterocolitica and Escherichia coli phi under iron-limiting conditions and apparently served as an iron carrier. Transport of 55Fe-yersiniabactin was TonB-dependent, indicating a receptor-mediated uptake across the outer membrane. A pesticin-resistant mutant missing the receptor protein FyuA was unable to transport and use yersiniabactin as a siderophore.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / isolation & purification*
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacteriocins / isolation & purification
  • Bacteriocins / metabolism
  • Biological Transport, Active
  • Fermentation
  • Iron / metabolism
  • Iron Chelating Agents / isolation & purification
  • Iron Chelating Agents / metabolism
  • Molecular Weight
  • Siderophores / isolation & purification*
  • Siderophores / metabolism
  • Virulence
  • Yersinia enterocolitica / growth & development
  • Yersinia enterocolitica / metabolism*
  • Yersinia enterocolitica / pathogenicity


  • Bacterial Outer Membrane Proteins
  • Bacteriocins
  • Iron Chelating Agents
  • Siderophores
  • Iron