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PMID: 1903349 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Pyoverdine-mediated iron transport in Pseudomonas aeruginosa: involvement of a high-molecular-mass outer membrane protein.

FEMS microbiology letters ·Vol. 62 ·No. 1 ·1991-02-00 ·Pages 1-5

Poole K, Neshat S, Heinrichs D

Abstract

Reduced expression of an iron-regulated outer membrane protein (IROMP) of approximate molecular mass 90,000 was observed in Pseudomonas aeruginosa concomitant with a loss of pyoverdine production in a wild type strain grown at 43 degrees C and in a mutant deficient in pyoverdine production. Consistent with an implied role in pyoverdine-mediated iron transport a mutant lacking the 90 kDa protein transported barely detectable levels of ferri-pyoverdine. Interestingly, the mutant still exhibited pyoverdine-dependent growth in an iron-deficient medium containing the synthetic iron chelator ethylene diamine-di(omicron-hydroxyphenol acetic acid) (EDDHA) suggesting that a second uptake system for ferri-pyoverdine may exist in P. aeruginosa.

MeSH Terms
Bacterial Outer Membrane Proteins/metabolism Biological Transport, Active Electrophoresis, Polyacrylamide Gel Iron/metabolism Kinetics Molecular Weight Oligopeptides Pigments, Biological/isolation & purification,metabolism Pseudomonas aeruginosa/growth & development,metabolism
Chemicals
Bacterial Outer Membrane Proteins Oligopeptides Pigments, Biological pyoverdin Iron
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Poole K
Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada.
Neshat S
Heinrichs D
Article Info
Journal
FEMS microbiology letters
Abbr.
FEMS Microbiol Lett
ISSN
0378-1097
Published
1991-02-00
Pages
1-5
Language
English
Region
England
NLM ID
7705721
Subset
IM
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