Siderophore-mediated utilization of iron bound to transferrin by Vibrio parahaemolyticus.
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.
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
S
S
Yamamoto
N
N
Okujo
S
S
Matsuura
I
I
Fujiwara
Y
Y
Fujita
S
S
Shinoda
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002951:Citrates / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000378:metabolism*; D008970:Molecular Weight; D011760:Pyrrolidinones / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism; D017262:Siderophores / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*; D014736:Vibrio parahaemolyticus / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D002951:Citrates; D011760:Pyrrolidinones; D011956:Receptors, Cell Surface; D017262:Siderophores; D014168:Transferrin; C090126:vibrioferrin; D007501:Iron