Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 595-598 |
| Number of pages | 4 |
| Journal | MICROBIOLOGY and IMMUNOLOGY |
| Volume | 40 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 1996 |
Keywords
- Exocellular protease
- Iron assimilation
- Siderophore
- Vibrio vulnificus
ASJC Scopus subject areas
- Microbiology
- Immunology
- Virology
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