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PMID: 1309510 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Siderophore production and membrane alterations by Bordetella pertussis in response to iron starvation.

Infection and immunity ·Vol. 60 ·No. 1 ·1992-01-00 ·Pages 117-23

Agiato LA, Dyer DW

Abstract

Bordetella pertussis was grown in iron (Fe)-free defined medium to limit the growth of the organism. Doubling times of the Fe-starved organism increased by approximately 1 h, and a 40% reduction in the final extent of growth in Fe-depleted medium was observed. Under these conditions, a hydroxamate siderophore named bordetellin was secreted by B. pertussis. Lactoferrin and transferrin supported growth of B. pertussis even when the protein was sequestered inside dialysis tubing. This suggested that binding of lactoferrin and transferrin to B. pertussis was not essential and that bordetellin production plays a major role in Fe uptake. Solid-phase dot blot assays indicated weak binding of lactoferrin to the cell surface, consistent with previous reports of a lactoferrin receptor. Three new proteins of 97, 77, and 63 kDa were synthesized in response to Fe starvation. Fe-inducible proteins of 103, 72, 24, 21, and 18 kDa were also observed. The synthesis of lipopolysaccharide was also altered by Fe availability.

MeSH Terms
Blotting, Western Bordetella pertussis/drug effects,metabolism,ultrastructure Cell Division/drug effects Cell Membrane/drug effects,metabolism Electrophoresis, Polyacrylamide Gel Ferrous Compounds/pharmacology Hemin/pharmacology Hydrogen-Ion Concentration Iron/pharmacology Iron Chelating Agents/metabolism Iron Deficiencies Lactoferrin/pharmacology Lipopolysaccharides/analysis Membrane Proteins/analysis Models, Biological Receptors, Cell Surface/analysis Receptors, Transferrin/analysis Siderophores Transferrin/pharmacology
Chemicals
Ferrous Compounds Iron Chelating Agents Lipopolysaccharides Membrane Proteins Receptors, Cell Surface Receptors, Transferrin Siderophores Transferrin lactoferrin receptors ferrous sulfate Hemin Iron Lactoferrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Agiato L A
Department of Microbiology, State University of New York, Buffalo 14214.
Dyer D W
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.60.1.117-123.1992
Published
1992-01-00
Pages
117-23
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC257511
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.60.1.117-123.1992 PMC Full Text View journal details
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