Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus.
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.
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
N
N
Okujo
T
T
Akiyama
S
S
Miyoshi
S
S
Shinoda
S
S
Yamamoto
D000577:Amides / Q000378:metabolism*; D001426:Bacterial Proteins; D005290:Ferric Compounds / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D007781:Lactoferrin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D010080:Oxazoles / Q000378:metabolism*; D017262:Siderophores / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism; D014733:Vibrio / Q000378:metabolism*
D000577:Amides; D001426:Bacterial Proteins; D005290:Ferric Compounds; D010080:Oxazoles; D017262:Siderophores; D014168:Transferrin; C086667:vulnibactin; D007501:Iron; D007781:Lactoferrin; D008666:Metalloendopeptidases; C070101:vvP protein, Vibrio vulnificus