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PMID: 2533128 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Utilization of transferrin-bound iron by Haemophilus species of human and porcine origins.

FEMS microbiology letters ·Vol. 53 ·No. 1-2 ·1989-11-00 ·Pages 123-7

Morton DJ, Williams P

Abstract

Haemophilus influenzae and H. haemolyticus acquired iron bound to human transferrin but not to human lactoferrin, ovo- or porcine transferrins. Conversely the swine pathogens H. pleuropneumoniae and H. parasuis used iron bound only to porcine transferrin. Growth under conditions of iron deprivation induced the production of siderophores and iron-repressible outer membrane proteins in H. parainfluenzae, H. paraphrophilus and H. parasuis but not in H. influenzae, H. haemolyticus or H. pleuropneumoniae. The latter 3 Haemophilus species appear to sequester transferrin bound iron via a siderophore-independent mechanism. However, the ability to produce iron chelating compounds did not enable H. parainfluenzae or H. paraphrophilus to utilize transferrin bound iron.

MeSH Terms
Animals Electrophoresis, Polyacrylamide Gel Haemophilus/metabolism Haemophilus influenzae/metabolism Humans Iron/metabolism Iron Chelating Agents/metabolism Lactoferrin/metabolism Siderophores Species Specificity Swine/microbiology Transferrin/metabolism
Chemicals
Iron Chelating Agents Siderophores Transferrin Iron Lactoferrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Morton D J
Department of Pharmaceutical Sciences, University of Nottingham, U.K.
Williams P
Article Info
Journal
FEMS microbiology letters
Abbr.
FEMS Microbiol Lett
ISSN
0378-1097
Published
1989-11-00
Pages
123-7
Language
English
Region
England
NLM ID
7705721
Subset
IM
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