Siderophore-Mediated Utilization of Iron Bound to Transferrin by Vibrio parahaemolyticus

Shigeo Yamamoto, Noriyuki Okujo, Shyoko Matsuura, Ikuko Fujiwara, Yasuhiro Fujita, Sumio Shinoda

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Vibrio parahaemolyticus produces a structurally novel type of siderophore, termed vibrioferrin, in response to iron-limitation. This study was performed to examine whether vibrioferrin can assimilate iron from human iron-binding proteins for growth. Comparison of the growth rates between V. parahaemolyticus AQ 3354 and its spontaneously arising, vibrioferrin-deficient mutant revealed that vibrioferrin was able to sequester iron from 30% iron-saturated human transferrin for growth, but not from human lactoferrin even if fully saturated with iron. In both strains, iron limitation induced two high-molecular-weight outer membrane proteins with apparent molecular masses of approximately 78 and 83 kDa. Since only the outer membrane fraction including these proteins showed a binding capacity to ferric vibrioferrin complex, either of them may function as its cell surface receptor. These results suggested that the organism might utilize such a source of host iron through the action of vibrioferrin during in vivo survival and proliferation, although its importance in pathogenesis is unknown.

Original languageEnglish
Pages (from-to)687-693
Number of pages7
Issue number9
Publication statusPublished - 1994


  • Iron source
  • Transferrin
  • Vibrio parahaemolyticus
  • Vibrioferrin

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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