| <i>Helicobacter pylori</i> has an unprecedented nitric oxide detoxifying system. | |
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MedLine Citation:
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PMID: 22236381 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Aims: The ability of pathogens to cope with the damaging effects of nitric oxide (NO), present in certain host niches and produced by phagocytes that support innate immunity, relies on multiple strategies that include the action of detoxifying enzymes. As for many other pathogens, these systems remained unknown for <i>Helicobacter pylori</i>. This work aimed at identifying and functionally characterizing an <i>H. pylori</i> system involved in NO protection. Results: In the present work, the <i>hp0013</i> gene of <i>H. pylori</i> is shown to be related to NO resistance as its inactivation increases the susceptibility of <i>H. pylori</i> to nitrosative stress, and significantly decreases the NADPH-dependent NO reduction activity of <i>H. pylori</i> cells. The recombinant HP0013 protein is able to complement an NO reductase-deficient <i>E. coli</i> strain and exhibits significant NO reductase activity. Mutation of <i>hp0013</i> renders <i>H. pylori</i> more vulnerable to nitric oxide synthase-dependent macrophage killing, and decreases the ability of the pathogen to colonize mice stomachs. Innovation: Phylogenetic studies reveal that HP0013, which shares no significant amino acid sequence similarity to the other so far known microbial NO detoxifiers, belongs to a novel family of proteins with a widespread distribution in the microbial world. Conclusion: <i>H. pylori</i> HP0013 represents an unprecedented enzymatic NO detoxifying system for the in vivo microbial protection against nitrosative stress. |
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Authors:
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Marta Campos Justino; Chantal Ecobichon; André F Fernandes; Ivo Gomperts Boneca; Lígia M Saraiva |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-1-11 |
Journal Detail:
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Title: Antioxidants & redox signaling Volume: - ISSN: 1557-7716 ISO Abbreviation: - Publication Date: 2012 Jan |
Date Detail:
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Created Date: 2012-1-12 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100888899 Medline TA: Antioxid Redox Signal Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal; mscampos@itqb.unl.pt. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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