Assimilation of metal ions bound to porphyrins or porphyrin-peptides by Vibrio vulnificus, a human pathogen inhabiting estuarine and marine environments

Shin-ichi Miyoshi, Tomoko Sasaki, Nahoko Kaku, Takaharu Inoue, Natsuki Uozumi, Yoko Maehara, Hiroshi Nakao

Research output: Contribution to journalArticle

Abstract

Vibrio vulnificus, a ubiquitous microorganism in aquatic environments, causes serious septicemia to the immunocompromised host. In addition to protoheme, this species can utilize FeTCPP [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.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalBiocontrol Science
Volume15
Issue number1
Publication statusPublished - 2010

Fingerprint

Metalloporphyrins
Vibrio vulnificus
Porphyrins
Heme
Iron
Metals
Ions
Peptides
Immunocompromised Host
Cytochromes c
Zinc
Sepsis
Bacteria
Growth
Proteins
iron 5,10,15,20-tetrakis-4-carboxyphenylporphyrin

Keywords

  • Heme
  • Iron source
  • Metalloporphyrin
  • Vibrio vulnificus

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Public Health, Environmental and Occupational Health

Cite this

Assimilation of metal ions bound to porphyrins or porphyrin-peptides by Vibrio vulnificus, a human pathogen inhabiting estuarine and marine environments. / Miyoshi, Shin-ichi; Sasaki, Tomoko; Kaku, Nahoko; Inoue, Takaharu; Uozumi, Natsuki; Maehara, Yoko; Nakao, Hiroshi.

In: Biocontrol Science, Vol. 15, No. 1, 2010, p. 1-6.

Research output: Contribution to journalArticle

Miyoshi, Shin-ichi ; Sasaki, Tomoko ; Kaku, Nahoko ; Inoue, Takaharu ; Uozumi, Natsuki ; Maehara, Yoko ; Nakao, Hiroshi. / Assimilation of metal ions bound to porphyrins or porphyrin-peptides by Vibrio vulnificus, a human pathogen inhabiting estuarine and marine environments. In: Biocontrol Science. 2010 ; Vol. 15, No. 1. pp. 1-6.
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AU - Kaku, Nahoko

AU - Inoue, Takaharu

AU - Uozumi, Natsuki

AU - Maehara, Yoko

AU - Nakao, Hiroshi

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AB - Vibrio vulnificus, a ubiquitous microorganism in aquatic environments, causes serious septicemia to the immunocompromised host. In addition to protoheme, this species can utilize FeTCPP [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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