Serveur d'exploration sur les relations entre la France et l'Australie

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Leptospira interrogans Catalase Is Required for Resistance to H2O2 and for Virulence

Identifieur interne : 005503 ( Main/Exploration ); précédent : 005502; suivant : 005504

Leptospira interrogans Catalase Is Required for Resistance to H2O2 and for Virulence

Auteurs : Azad Eshghi [Canada] ; Kristel Lourdault [France] ; Gerald L. Murray [Australie] ; Thanatchaporn Bartpho [Thaïlande] ; Rasana W. Sermswan [Thaïlande] ; Mathieu Picardeau [France] ; Ben Adler [Australie] ; Brendan Snarr [Canada] ; Richard L. Zuerner [États-Unis, Suède] ; Caroline E. Cameron [Canada]

Source :

RBID : PMC:3486042

Abstract

Pathogenic Leptospira spp. are likely to encounter higher concentrations of reactive oxygen species induced by the host innate immune response. In this study, we characterized Leptospira interrogans catalase (KatE), the only annotated catalase found within pathogenic Leptospira species, by assessing its role in resistance to H2O2-induced oxidative stress and during infection in hamsters. Pathogenic L. interrogans bacteria had a 50-fold-higher survival rate under H2O2-induced oxidative stress than did saprophytic L. biflexa bacteria, and this was predominantly catalase dependent. We also characterized KatE, the only annotated catalase found within pathogenic Leptospira species. Catalase assays performed with recombinant KatE confirmed specific catalase activity, while protein fractionation experiments localized KatE to the bacterial periplasmic space. The insertional inactivation of katE in pathogenic Leptospira bacteria drastically diminished leptospiral viability in the presence of extracellular H2O2 and reduced virulence in an acute-infection model. Combined, these results suggest that L. interrogans KatE confers in vivo resistance to reactive oxygen species induced by the host innate immune response.


Url:
DOI: 10.1128/IAI.00466-12
PubMed: 22927050
PubMed Central: 3486042


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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and for Virulence</title>
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O
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and for Virulence</title>
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<p>Pathogenic
<named-content content-type="genus-species">Leptospira</named-content>
spp. are likely to encounter higher concentrations of reactive oxygen species induced by the host innate immune response. In this study, we characterized
<named-content content-type="genus-species">Leptospira interrogans</named-content>
catalase (KatE), the only annotated catalase found within pathogenic
<named-content content-type="genus-species">Leptospira</named-content>
species, by assessing its role in resistance to H
<sub>2</sub>
O
<sub>2</sub>
-induced oxidative stress and during infection in hamsters. Pathogenic
<named-content content-type="genus-species">L. interrogans</named-content>
bacteria had a 50-fold-higher survival rate under H
<sub>2</sub>
O
<sub>2</sub>
-induced oxidative stress than did saprophytic
<named-content content-type="genus-species">L. biflexa</named-content>
bacteria, and this was predominantly catalase dependent. We also characterized KatE, the only annotated catalase found within pathogenic
<named-content content-type="genus-species">Leptospira</named-content>
species. Catalase assays performed with recombinant KatE confirmed specific catalase activity, while protein fractionation experiments localized KatE to the bacterial periplasmic space. The insertional inactivation of
<italic>katE</italic>
in pathogenic
<named-content content-type="genus-species">Leptospira</named-content>
bacteria drastically diminished leptospiral viability in the presence of extracellular H
<sub>2</sub>
O
<sub>2</sub>
and reduced virulence in an acute-infection model. Combined, these results suggest that
<named-content content-type="genus-species">L. interrogans</named-content>
KatE confers
<italic>in vivo</italic>
resistance to reactive oxygen species induced by the host innate immune response.</p>
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