The University of Southampton
University of Southampton Institutional Repository

A study of iron acquisition mechanisms of Legionella pneumophila grown in chemostat culture

A study of iron acquisition mechanisms of Legionella pneumophila grown in chemostat culture
A study of iron acquisition mechanisms of Legionella pneumophila grown in chemostat culture

We recently demonstrated that the virulence of a clinical isolate of Legionella pneumophila is significantly attenuated when cultured in an iron- limited environment. In this study the influence of iron limitation on the expression of enzyme activities and iron-transport mechanisms was investigated. Expression of the important pathogenicity factor, the zinc metalloprotease, was reduced fivefold in response to iron limitation. Ferric citrate reductase activity was demonstrated in both iron-limited and replete cell fractions. Activity was located principally in the cytoplasm and periplasm, and was not enhanced by iron restriction. Optimum activity was observed with NADPH as reductant. Siderophores were not elaborated under these culture conditions. Iron-loaded transferrin enhanced the growth of steady-state, iron-limited cultures, demonstrating that transferrin represents a potentially important iron source for L. pneumophila in vivo. Although cell surface transferrin receptors were not detected, in vitro experiments demonstrated digestion of transferrin by the zinc metalloprotease activity of culture supernatants.

0343-8651
238-243
James, Brian W.
2982ef34-33f6-4dd1-bc54-03b0333f3339
Mauchline, W. Stuart
80ed42b2-235d-4e4b-998b-bb928a52daa2
Dennis, P. Julian
25bd2523-2802-498f-9a17-80ecea7db112
Keevil, C. William
cb7de0a7-ce33-4cfa-af52-07f99e5650eb
James, Brian W.
2982ef34-33f6-4dd1-bc54-03b0333f3339
Mauchline, W. Stuart
80ed42b2-235d-4e4b-998b-bb928a52daa2
Dennis, P. Julian
25bd2523-2802-498f-9a17-80ecea7db112
Keevil, C. William
cb7de0a7-ce33-4cfa-af52-07f99e5650eb

James, Brian W., Mauchline, W. Stuart, Dennis, P. Julian and Keevil, C. William (1997) A study of iron acquisition mechanisms of Legionella pneumophila grown in chemostat culture. Current Microbiology, 34 (4), 238-243. (doi:10.1007/s002849900176).

Record type: Article

Abstract

We recently demonstrated that the virulence of a clinical isolate of Legionella pneumophila is significantly attenuated when cultured in an iron- limited environment. In this study the influence of iron limitation on the expression of enzyme activities and iron-transport mechanisms was investigated. Expression of the important pathogenicity factor, the zinc metalloprotease, was reduced fivefold in response to iron limitation. Ferric citrate reductase activity was demonstrated in both iron-limited and replete cell fractions. Activity was located principally in the cytoplasm and periplasm, and was not enhanced by iron restriction. Optimum activity was observed with NADPH as reductant. Siderophores were not elaborated under these culture conditions. Iron-loaded transferrin enhanced the growth of steady-state, iron-limited cultures, demonstrating that transferrin represents a potentially important iron source for L. pneumophila in vivo. Although cell surface transferrin receptors were not detected, in vitro experiments demonstrated digestion of transferrin by the zinc metalloprotease activity of culture supernatants.

This record has no associated files available for download.

More information

Published date: 1 April 1997

Identifiers

Local EPrints ID: 431349
URI: http://eprints.soton.ac.uk/id/eprint/431349
ISSN: 0343-8651
PURE UUID: 4ff82f6b-937d-48af-b87e-76b09e56f80d
ORCID for C. William Keevil: ORCID iD orcid.org/0000-0003-1917-7706

Catalogue record

Date deposited: 29 May 2019 16:30
Last modified: 16 Mar 2024 03:24

Export record

Altmetrics

Contributors

Author: Brian W. James
Author: W. Stuart Mauchline
Author: P. Julian Dennis

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×