Mar, 2010
Assimilation of Metal Ions Bound to Porphyrins or Porphyrin-Peptides by Vibrio vulnificus, a Human Pathogen Inhabiting Estuarine and Marine Environments
BIOCONTROL SCIENCE
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- Volume
- 15
- Number
- 1
- First page
- 1
- Last page
- 6
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.4265/bio.15.1
- Publisher
- SOC ANTIBACTERIAL & ANTIFUNGAL AGENTS, JAPAN
Vibrio vulnificus, a ubiquitous microorganism in aquatic environments, causes serious septicemia to the immunocompromised host. In addition to protoheme, this species can utilize Fe-TCPP [ferric tetrakis (4-carboxyphenyl) porphine] as an iron source. In the present study, heme c bound covalently to the protein in cytochrome c, as well as the Fe-TCPP complex formed with a nanopeptide with a high affinity, was found to be useful iron sources for V. vulnificus. This bacterium was also revealed to use Zn-TCPP as a single zinc source. However, other metalloporphyrins such as Mn-TCPP and Pt-TCPP delayed the bacterial growth in the broth containing Fe-TCPP, suggesting interference in the iron assimilation. These results indicate that V. vulnificus may acquire metal ions from both free and peptide-bound metalloporphyrins.
- Link information
- ID information
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- DOI : 10.4265/bio.15.1
- ISSN : 1342-4815
- eISSN : 1884-0205
- Web of Science ID : WOS:000275946600001