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PMID: 7551061 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp.

Microbiology (Reading, England) ·Vol. 141 ( Pt 8) ·1995-08-00 ·Pages 1985-1992

Deneer HG, Healey V, Boychuk I

Abstract

The reduction of exogenous ferric iron by Listeria monocytogenes, a Gram-positive food-borne pathogen, was investigated. Using an assay incorporating the ferrous iron chelator ferrozine, we showed that intact cells of L. monocytogenes, when exposed to ferric iron, were able to rapidly reduce and solubilize the iron to the ferrous form. Reduction occurred only after direct contact between the bacteria and the iron source. A number of different ferric iron chelates, including transferrin and lactoferrin-bound iron, haemoglobin, ferritin, and iron complexed to siderophores, could be reduced. The ferric reductase activity was expressed by both reference strains and clinical isolates of L. monocytogenes and by all other species of Listeria, although significant quantitative differences were observed. In L. monocytogenes, the expression of ferric reductase was not affected by the growth phase of the bacteria nor by the presence or absence of iron in the growth medium. However, expression was greatly reduced in bacteria grown anaerobically and when cultured in media of reduced pH. In addition, bacteria grown at a cold temperature displayed greater ferric reductase activity than cells grown at higher temperatures. A surface-associated ferric reductase system may be one component of a general iron scavenging mechanism which can be used by Listeria growing in a variety of environments.

MeSH Terms
Aerobiosis Bacterial Proteins/metabolism Coenzymes/chemistry FMN Reductase Ferric Compounds/metabolism Ferrozine/chemistry Hydrogen-Ion Concentration Iron Chelating Agents/metabolism Listeria/genetics,metabolism Listeria monocytogenes/growth & development,metabolism Magnesium/chemistry Membrane Proteins/metabolism Metalloproteins/metabolism NADH, NADPH Oxidoreductases/biosynthesis,metabolism Oxidation-Reduction Temperature Time Factors
Chemicals
Bacterial Proteins Coenzymes Ferric Compounds Iron Chelating Agents Membrane Proteins Metalloproteins Ferrozine FMN Reductase NADH, NADPH Oxidoreductases ferric citrate iron reductase Magnesium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Deneer Harry G
Department of MicrobiologyUniversity of SaskatchewanSaskatoon, Saskatchewan, Canada, S7N 5E5.
Healey Vanessa
Division of Clinical MicrobiologyRoyal University Hospital Saskatoon, Saskatchewan, Canada, S7N 5E5.
Boychuk Irene
Department of MicrobiologyUniversity of SaskatchewanSaskatoon, Saskatchewan, Canada, S7N 5E5.
Article Info
Journal
Microbiology (Reading, England)
Abbr.
Microbiology (Reading)
ISSN
1350-0872
Published
1995-08-00
Pages
1985-1992
Language
English
Region
England
NLM ID
9430468
Subset
IM
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