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Precipitation of Iron on the Surface of Leptospira interrogans Is Associated with Mutation of the Stress Response Metalloprotease HtpX

Identifieur interne : 001613 ( Pmc/Curation ); précédent : 001612; suivant : 001614

Precipitation of Iron on the Surface of Leptospira interrogans Is Associated with Mutation of the Stress Response Metalloprotease HtpX

Auteurs : Rebekah Henry ; Miranda Lo ; Chenai Khoo ; Hailong Zhang ; Reinhard I. Boysen ; Mathieu Picardeau ; Gerald L. Murray ; Dieter M. Bulach ; Ben Adler

Source :

RBID : PMC:3719529

Abstract

High concentrations of free metal ions in the environment can be detrimental to bacterial survival. However, bacteria utilize strategies, including the activation of stress response pathways and immobilizing chemical elements on their surface, to limit this toxicity. In this study, we characterized LA4131, the HtpX-like M48 metalloprotease from Leptospira interrogans, with a putative role in bacterial stress response and membrane homeostasis. Growth of the la4131 transposon mutant strain (L522) in 360 μM FeSO4 (10-fold the normal in vitro concentration) resulted in the production of an amorphous iron precipitate. Atomic force microscopy and transmission electron microscopy analysis of the strain demonstrated that precipitate production was associated with the generation and release of outer membrane vesicles (OMVs) from the leptospiral surface. Transcriptional studies indicated that inactivation of la4131 resulted in altered expression of a subset of metal toxicity and stress response genes. Combining these findings, this report describes OMV production in response to environmental stressors and associates OMV production with the in vitro activity of an HtpX-like metalloprotease.


Url:
DOI: 10.1128/AEM.01097-13
PubMed: 23709510
PubMed Central: 3719529

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PMC:3719529

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<p>High concentrations of free metal ions in the environment can be detrimental to bacterial survival. However, bacteria utilize strategies, including the activation of stress response pathways and immobilizing chemical elements on their surface, to limit this toxicity. In this study, we characterized LA4131, the HtpX-like M48 metalloprotease from
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resulted in altered expression of a subset of metal toxicity and stress response genes. Combining these findings, this report describes OMV production in response to environmental stressors and associates OMV production with the
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activity of an HtpX-like metalloprotease.</p>
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<given-names>Rebekah</given-names>
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<xref ref-type="author-notes" rid="FN1">*</xref>
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<sup>a</sup>
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<sup>d</sup>
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<given-names>Chenai</given-names>
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<sup>a</sup>
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<surname>Picardeau</surname>
<given-names>Mathieu</given-names>
</name>
<xref ref-type="aff" rid="aff2">
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<contrib contrib-type="author">
<name>
<surname>Murray</surname>
<given-names>Gerald L.</given-names>
</name>
<xref ref-type="aff" rid="aff1">
<sup>a</sup>
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<given-names>Dieter M.</given-names>
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<aff id="aff1">Department of Microbiology, Monash University, Clayton, Victoria, Australia
<label>a</label>
</aff>
<aff id="aff2">Institut Pasteur, Unité de Biologie des Spirochètes, Paris, France
<label>b</label>
</aff>
<aff id="aff3">Australian Research Council Special Research Centre for Green Chemistry, Monash University, Clayton, Victoria, Australia
<label>c</label>
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<aff id="aff4">Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, Victoria, Australia
<label>d</label>
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<aff id="aff5">Victorian Bioinformatics Consortium, Monash University, Clayton, Victoria, Australia
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<corresp id="cor1">Address correspondence to Ben Adler,
<email>Ben.Adler@monash.edu</email>
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<fn id="FN1" fn-type="present-address">
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<pub-date pub-type="ppub">
<month>8</month>
<year>2013</year>
</pub-date>
<volume>79</volume>
<issue>15</issue>
<fpage>4653</fpage>
<lpage>4660</lpage>
<history>
<date date-type="received">
<day>4</day>
<month>4</month>
<year>2013</year>
</date>
<date date-type="accepted">
<day>22</day>
<month>5</month>
<year>2013</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright © 2013, American Society for Microbiology. All Rights Reserved.</copyright-statement>
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<abstract>
<p>High concentrations of free metal ions in the environment can be detrimental to bacterial survival. However, bacteria utilize strategies, including the activation of stress response pathways and immobilizing chemical elements on their surface, to limit this toxicity. In this study, we characterized LA4131, the HtpX-like M48 metalloprotease from
<named-content content-type="genus-species">Leptospira interrogans</named-content>
, with a putative role in bacterial stress response and membrane homeostasis. Growth of the
<italic>la4131</italic>
transposon mutant strain (L522) in 360 μM FeSO
<sub>4</sub>
(10-fold the normal
<italic>in vitro</italic>
concentration) resulted in the production of an amorphous iron precipitate. Atomic force microscopy and transmission electron microscopy analysis of the strain demonstrated that precipitate production was associated with the generation and release of outer membrane vesicles (OMVs) from the leptospiral surface. Transcriptional studies indicated that inactivation of
<italic>la4131</italic>
resulted in altered expression of a subset of metal toxicity and stress response genes. Combining these findings, this report describes OMV production in response to environmental stressors and associates OMV production with the
<italic>in vitro</italic>
activity of an HtpX-like metalloprotease.</p>
</abstract>
</article-meta>
</front>
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