Biocontrol Science
Online ISSN : 1884-0205
Print ISSN : 1342-4815
ISSN-L : 1342-4815
Original papers
Assimilation of Metal Ions Bound to Porphyrins or Porphyrin-Peptides by Vibrio vulnificus, a Human Pathogen Inhabiting Estuarine and Marine Environments
SHIN-ICHI MIYOSHITOMOKO SASAKINAHOKO KAKUTAKAHARU INOUENATSUKI UOZUMIYOKO MAEHARAHIROSHI NAKAO
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2010 Volume 15 Issue 1 Pages 1-6

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Abstract

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.

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© 2010 The Society for Antibacterial and Antifungal Agents, Japan
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