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J. Biol. Chem., Vol. 278, Issue 34, 31521-31528, August 22, 2003

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Detailed Structural Analysis of the Peptidoglycan of the Human Pathogen Neisseria meningitidis^*

Aude Antignac , Jean-Claude Rousselle , Abdelkader Namane , Agnès Labigne ¶, Muhamed-Kheir Taha  and Ivo G. Boneca ¶ ||

From the Unité des Neisseria and Centre National de Référence des Méningocoques, Plate-forme de Protéomique, and ^¶Unité de Pathogénie Bactérienne des Muqueuses, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France

We used reverse-phase high pressure liquid chromatography (HPLC), matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) and post source decay analysis (MALDI-PSD) to determine the muropeptide composition of the human pathogen Neisseria meningitidis. Structural assignment was determined for 28 muropeptide species isolated after HPLC separation and purification. Fourteen of these muropeptides were O-acetylated to different degrees. We identified the entire O-acetylation spectrum of dimers and trimers both in muropeptides and 1,6-anhydromuropeptides. On average, one of three disaccharides was O-acetylated. Furthermore, the degree of cross-linking of the N. meningitidis peptidoglycan was around 39% in all the strains analyzed. MALDI-PSD analysis of several muropeptide species indicated that meningococci only synthesize D-alanyl-meso-diaminopimelate cross-bridges. No muropeptides representative of covalent linkages of lipoproteins to the peptidoglycan could be identified, unlike in Escherichia coli. Finally, comparison of the muropeptide composition of penicillin-susceptible and penicillin-intermediate clinical strains of meningococci showed a positive correlation between the minimum inhibitory concentration (MIC) of penicillin G and the amount of muropeptides carrying an intact pentapeptide chain in the peptidoglycan. This suggests that reduced susceptibility to penicillin G in N. meningitidis is associated with a decrease in D,D-carboxypeptidase activity and/or D,D-transpeptidase activity.

Received for publication, May 7, 2003 , and in revised form, June 6, 2003.

^* This work was supported by the Pasteur Institute and by European Commission Grant QLK2-CT-2001-01436. 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.

^|| Recipient of a postdoctoral fellowship from the Fundação para a Ciência e a Tecnologia, Portugal (SFRH/BPD/1567/2000). To whom correspondence should be addressed. Tel.: 33-1-40-61-32-73, Fax: 33-1-40-61-36-40; E-mail: bonecai{at}pasteur.fr.

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