Papers

Peer-reviewed Lead author
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
  • Shin-Ichi Miyoshi
  • ,
  • Tomoko Sasaki
  • ,
  • Nahoko Kaku
  • ,
  • Takaharu Inoue
  • ,
  • Natsuki Uozumi
  • ,
  • Yoko Maehara
  • ,
  • Hiroshi Nakao

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
DOI
https://doi.org/10.4265/bio.15.1
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000275946600001&DestApp=WOS_CPL
ID information
  • DOI : 10.4265/bio.15.1
  • ISSN : 1342-4815
  • eISSN : 1884-0205
  • Web of Science ID : WOS:000275946600001

Export
BibTeX RIS