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1997 Fiscal Year Final Research Report Summary

Studies on the heme uptake system of a human pathogenic vibrio

Research Project

Project/Area Number 08670307
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Bacteriology (including Mycology)
Research InstitutionOkayama University

Principal Investigator

MIYOSHI Shin-ichi  Okayama University, Graduate Shool of Natural Science & Technology Research Associate, 大学院・自然科学研究所, 助手 (60182060)

Co-Investigator(Kenkyū-buntansha) TOMOCHIKA Ken-ichi  Okayama University, Faculty of Pharmaceutical Sciences Assistant Professor, 薬学部, 助教授 (00093691)
SHINODA Sumio  Okayama University, Faculty of Pharmaceutical Sciences Professor, 薬学部, 教授 (50029782)
Project Period (FY) 1996 – 1997
KeywordsPathogenic vibrio / Heme compound / Porphyrin
Research Abstract

Vibrio vulnificus, an opprtunistic human pathogen causing septicemia or wound infection, can obtain iron from a variety of heme proteins. This process involves the digestion of heme proteins by an exoprotease to leberate protoheme. In the present study, we investigated the protoheme uptake system of this human pathogenic vibrio.
1. In many human pathogens, protoheme is known to be fixed on the bacterial cell surface by the specific outer membrane receptor. Thus, we initially tested the presence of the protoheme receptor. The bacterium was found to express novel outer membrane proteins in the presence of protoheme. However, any of these proteins could not bind to protoheme, indicating V.vulnificus utilizes protoheme independent of the outer membrane receptor.
2. We isolated and characterized a mutant for protoheme utilization. One mutant isolated by treatment with a chemical mutagen was shown to be unable to use either protoheme or heme proteins, but multiplied in a medium supplemented with an iron-siderophore, uch as iron-vulnibactin. This finding demonstrates that V.vulnificus has the specialized protoheme uptake system.
3.V.vulnificus was found to utilize a synthetic heme compound (Fe-TPPS), as well as natural one(protoheme). The ability to utilize either heme compounds was competitively abolished by an excess amount of Cu-TPPS,an analog of the heme compound. Therefore, the protoheme uptake system in V.vulnificus may be not specific protoheme.

  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Okujo, N.: "Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferin-bound iron by Vibrio vulniticus" Microbiol.Immunol.40 (8). 595-598 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Miyoshi, S.: "Characterization of a mutant of Vibrio vulnificus for heme utilization" FEMS Microbiol.Lett. 146 (1). 101-106 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Miyoshi, S.: "Bacterial metalloprotease as the toxic factor in infection" J.Toxicol.Toxin Rev.16 (4). 177-194 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Okujo, N.: "Involvment of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus" Microbiol.Immunol.40 (8). 595-598 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Miyoshi, S.: "Characterization of a mutant of Vibrio vulnificus for heme utilization" FEMS Microbiuol.Lett.146 (1). 101-106 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Miyoshi, S.: "Bacterial metalloproteas as the toxic factor in infection" J.Toxicol.Toxin Rev.16 (4). 177-194 (1997)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1999-03-16  

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