Okujo N, Akiyama T, Miyoshi S, Shinoda S, Yamamoto S
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
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.
进行了体外生长实验，以评估创伤弧菌产生的一种铁载体——创伤弧菌素，螯合与转铁蛋白或乳铁蛋白结合的铁以供生长的能力。对产生创伤弧菌素的菌株及其细胞外蛋白酶缺陷型突变体进行的比较研究表明，除创伤弧菌素外，蛋白酶也参与了对与转铁蛋白和乳铁蛋白结合的铁离子（Fe3+）的有效利用。看来蛋白酶会导致这些蛋白质的裂解，从而使结合的铁更容易被创伤弧菌素获取。
