TlpAs (thioredoxin-like proteins) are bacterial thioredoxin-like periplasmic disulfide oxidoreductases generally involved in cytochrome c maturation (Ccm) process. They contain a characteristic CXXC active site motif involved in disulfide exchange reaction. In the human pathogenic Neisseria meningitidis species, no TlpA has been characterized so far. In the present study, using an in silico analysis, we identified a putative periplasmic TlpA, called TlpA2. Biochemical and kinetic characterizations of the soluble form of TlpA2, tTlpA2 (truncated TlpA2), were performed. A reduction potential of −0.230 V at pH 7 was calculated, suggesting that TlpA2 acts as a reductant in the oxidative environment of the periplasm. Using a second-order reactive probe, high pKapp (apparent pKa) values were determined for the two cysteines of the SCXXC motif. The tTlpA2 was shown to be efficiently reduced by the N-terminal domain of the DsbD, whereas tTlpA2 reduced a mimetic peptide of cytochrome c′ with a catalytic efficiency similar to that observed with other disulfide oxidoreductase like ResA. Moreover, the corresponding gene tlpA2 was shown to be essential for the pathogen viability and able to partially complement a Bordetella pertussis CcsX mutant. Together, these data support an essential role of TlpA2 in the Ccm process in N. meningitidis.
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Research Article|
May 22 2015
Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability
Adeline Gand;
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
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Laure Selme-Roussel;
Laure Selme-Roussel
2
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
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Sabrina Collin;
Sabrina Collin
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
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Guy Branlant;
Guy Branlant
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
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Christophe Jacob;
Christophe Jacob
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
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Sandrine Boschi-Muller
Sandrine Boschi-Muller
3
*IMoPA, Équipe Enzymologie Moléculaire et Structurale, UMR 7365 CNRS-Université de Lorraine, Bâtiment Biopôle, Faculté de Médecine, 9 avenue de la Foreât de Haye, CS 50184, 54505 Vandoeuvre-les-Nancy, France
3To whom correspondence should be addressed (email sandrine.boschi@univ-lorraine.fr).
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Publisher: Portland Press Ltd
Received:
July 16 2014
Revision Received:
March 04 2015
Accepted:
March 31 2015
Accepted Manuscript online:
March 31 2015
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem J (2015) 468 (2): 271–282.
Article history
Received:
July 16 2014
Revision Received:
March 04 2015
Accepted:
March 31 2015
Accepted Manuscript online:
March 31 2015
Citation
Adeline Gand, Laure Selme-Roussel, Sabrina Collin, Guy Branlant, Christophe Jacob, Sandrine Boschi-Muller; Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability. Biochem J 1 June 2015; 468 (2): 271–282. doi: https://doi.org/10.1042/BJ20140868
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