Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus

Microbiol Immunol. 1996;40(8):595-8. doi: 10.1111/j.1348-0421.1996.tb01114.x.


In vitro growth experiments were conducted to evaluate the ability of vulnibactin, a siderophore produced by Vibrio vulnificus, to sequester transferrin- or lactoferrin bound iron for growth. Comparative studies with the strain producing vulnibactin and its exocellular protease-deficient mutant revealed the involvement of the protease in addition to vulnibactin in effective utilization of iron ion (Fe3+) bound to transferrin and lactoferrin. It appears that the protease causes cleavage of these proteins, thereby making bound iron more accessible to vulnibactin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amides / metabolism*
  • Bacterial Proteins*
  • Ferric Compounds / metabolism
  • Iron / metabolism*
  • Lactoferrin / metabolism
  • Metalloendopeptidases / deficiency
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism*
  • Mutation
  • Oxazoles / metabolism*
  • Siderophores / metabolism*
  • Transferrin / metabolism
  • Vibrio / metabolism*


  • Amides
  • Bacterial Proteins
  • Ferric Compounds
  • Oxazoles
  • Siderophores
  • Transferrin
  • vulnibactin
  • Iron
  • Lactoferrin
  • Metalloendopeptidases
  • vvP protein, Vibrio vulnificus