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J. Biol. Chem., Vol. 278, Issue 34, 31529-31535, August 22, 2003

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Correlation between Alterations of the Penicillin-binding Protein 2 and Modifications of the Peptidoglycan Structure in Neisseria meningitidis with Reduced Susceptibility to Penicillin G^*

Aude Antignac , Ivo G. Boneca  ¶, Jean-Claude Rousselle ||, Abdelkader Namane ||, Jean-Philippe Carlier **, Julio A. Vázquez , Andrew Fox ¶¶, Jean-Michel Alonso  and Muhamed-Kheir Taha  ||||

From the Unité des Neisseria and Centre National de Référence des Méningocoques, Unité de Pathogénie Bactérienne des Muqueuses, ^||Plate-forme de Protéomique, ^**Unité des Bactéries Anaérobies et des Toxines, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France, Spanish Reference Laboratory for Meningococci, National Center for Microbiology, Instituto de Salud Carlos III, Majadahonda, Madrid, 28220, Spain, and ^¶¶Meningococcal Reference Unit, Manchester Public Health Laboratory, Withington Hospital, Manchester, M20 2LR, England

Reduced susceptibility to penicillin G in Neisseria meningitidis is directly correlated with alterations in the penA gene, which encodes the penicillin-binding protein 2 (PBP2). Using purified PBP2s from different backgrounds, we confirmed that the reduced susceptibility to penicillin G is associated with a decreased affinity of altered PBP2s for penicillin G. Infrared spectroscopy analysis using isogenic penicillin-susceptible strains and strains with reduced susceptibility to penicillin G suggested that the meningococcal cell wall is also modified in a penA-dependent manner. Moreover, reverse-phase high pressure liquid chromatography and mass spectrometry analysis of these meningococcal strains confirmed the modifications of peptidoglycan components and showed an increase in the peaks corresponding to pentapeptide-containing muropeptides. These results suggest that the D,D-transpeptidase and/or D,D-carboxypeptidase activities of PBP2 are modified by the changes in penA gene.

Received for publication, May 2, 2003 , and in revised form, June 10, 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.: 33-1-45688438; Fax: 33-1-45688338; E-mail: mktaha{at}pasteur.fr.

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