HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 42, 31812-31822, October 20, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/42/31812    most recent M606249200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Archambaud, C. Articles by Dussurget, O. Search for Related Content PubMed PubMed Citation Articles by Archambaud, C. Articles by Dussurget, O. Social Bookmarking                      What's this?

Control of Listeria Superoxide Dismutase by Phosphorylation^*

From the Institut Pasteur, Unité des Interactions Bactéries-Cellules, Inserm, U604, INRA, USC2020, F-75015 Paris, France

Superoxide dismutases (SODs) are enzymes that protect organisms against superoxides and reactive oxygen species (ROS) produced during their active metabolism. ROS are major mediators of phagocytes microbicidal activity. Here we show that the cytoplasmic Listeria monocytogenes MnSOD is phosphorylated on serine and threonine residues and less active when bacteria reach the stationary phase. We also provide evidence that the most active nonphosphorylated form of MnSOD can be secreted via the SecA2 pathway in culture supernatants and in infected cells, where it becomes phosphorylated. A sod deletion mutant is impaired in survival within macrophages and is dramatically attenuated in mice. Together, our results demonstrate that the capacity to counteract ROS is an essential component of L. monocytogenes virulence. This is the first example of a bacterial SOD post-translationally controlled by phosphorylation, suggesting a possible new host innate mechanism to counteract a virulence factor.

Received for publication, June 29, 2006 , and in revised form, July 27, 2006.

^* This work was supported in part from Institut Pasteur (GPH N°9); INRA, INSERM, and the French Ministry of Research (Programme de Microbiologie Fondamentale et Appliquée, Maladies Infectieuses, Environment et Bioterrorisme ACI N° MIC 0312). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two supplemental experimental procedures, one supplemental Table S1, and four supplemental Figs. S1-S4.

¹ Supported by fellowships from the Ministère de la Recherche, the Pasteur-Weizmann Foundation, EuroPathoGenomics (NoE, Contract N° LSHB-CT-2005-512061) and the Howard Hughes Medical Institute.

² An International Research Scholar of the Howard Hughes Medical Institute. To whom correspondence may be addressed. Tel.: 33-1-40-61-30-32; Fax: 33-1-45-68-87-06; E-mail: pcossart{at}pasteur.fr.

³ To whom correspondence may be addressed: Unité des Interactions Bactéries-Cellules, Institut Pasteur, 25 rue du Dr. Roux, 75015 Paris, France. E-mail: odussur{at}pasteur.fr.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. M. Hou, N. G. D'Lima, N. W. Rigel, H. S. Gibbons, J. R. McCann, M. Braunstein, and C. M. Teschke ATPase Activity of Mycobacterium tuberculosis SecA1 and SecA2 Proteins and Its Importance for SecA2 Function in Macrophages J. Bacteriol., July 15, 2008; 190(14): 4880 - 4887. [Abstract] [Full Text] [PDF]

				I. R. Monk, C. G. M. Gahan, and C. Hill Tools for Functional Postgenomic Analysis of Listeria monocytogenes Appl. Envir. Microbiol., July 1, 2008; 74(13): 3921 - 3934. [Abstract] [Full Text] [PDF]

				H. S. Gibbons, F. Wolschendorf, M. Abshire, M. Niederweis, and M. Braunstein Identification of Two Mycobacterium smegmatis Lipoproteins Exported by a SecA2-Dependent Pathway J. Bacteriol., July 15, 2007; 189(14): 5090 - 5100. [Abstract] [Full Text] [PDF]

				H. Bierne and P. Cossart Listeria monocytogenes Surface Proteins: from Genome Predictions to Function Microbiol. Mol. Biol. Rev., June 1, 2007; 71(2): 377 - 397. [Abstract] [Full Text] [PDF]