Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin

Gerald Laurence Murray, Kathyrn Ellis, Miranda Lo, Ben Adler

Research output: Contribution to journalArticleResearchpeer-review

53 Citations (Scopus)

Abstract

The transposon TnSC189 was used to construct a mutant in the putative heme oxygenase gene hemO (LB186) of Leptospira interrogans. Unlike its parent strain, the mutant grew poorly in medium in which hemoglobin was the sole iron source. The putative heme oxygenase was over expressed in a His-tagged form, purified and was demonstrated to degrade heme in vitro. Unexpectedly, it was also found that the L. interrogans growth rate was significantly increased when medium was supplemented with hemoglobin, but only if ferrous iron sources were absent. This result was mirrored in the expression of some iron-related genes and suggests the presence of regulatory mechanisms detecting Fe(2+) and hemoglobin. This is the first demonstration of a functional heme oxygenase from a spirochete.
Original languageEnglish
Pages (from-to)791 - 797
Number of pages7
JournalMicrobes and Infection
Volume10
Issue number7
Publication statusPublished - 2008

Cite this