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Involvement of Vulnibactin and Exocellular Protease in Utilization of Transferrin‐ and Lactoferrin‐Bound Iron by Vibrio vulnificus
Author(s) -
Okujo Noriyuki,
Akiyama Toshihito,
Miyoshi ShinIchi,
Shinoda Sumio,
Yamamoto Shigeo
Publication year - 1996
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1996.tb01114.x
Subject(s) - vibrio vulnificus , lactoferrin , transferrin , protease , siderophore , microbiology and biotechnology , biology , hemin , biochemistry , in vitro , vibrionaceae , vibrio , heme , enzyme , bacteria , genetics , gene
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 (Fe 3+ ) bound to transferrin and lactoferrin. It appears that the protease causes cleavage of these proteins, thereby making bound iron more accessible to vulnibactin.