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Journal of Bacteriology, March 2006, p. 1875-1881, Vol. 188, No. 5
0021-9193/06/$08.00+0     doi:10.1128/JB.188.5.1875-1881.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of the Bifunctional Glycosyltransferase/Acyltransferase Penicillin-Binding Protein 4 of Listeria monocytogenes

Joanna Zawadzka-Skomia,¹ Zdzislaw Markiewicz,¹ Martine Nguyen-Distèche,² Bart Devreese,³ Jean-Marie Frère,² and Mohammed Terrak^2*

Institute of Microbiology, Warsaw University, Miecznikowa 1, 02-096 Warsaw, Poland,¹ Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman, Belgium,² Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, KL Ledeganckstraat 35, B-9000 Gent, Belgium³

Received 12 October 2005/ Accepted 12 December 2005

Multimodular penicillin-binding proteins (PBPs) are essential enzymes responsible for bacterial cell wall peptidoglycan (PG) assembly. Their glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate (undecaprenyl-pyrophosphoryl-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide), and their transpeptidase activity catalyzes cross-linking between peptides carried by two adjacent glycan chains. Listeria monocytogenes is a food-borne pathogen which exerts its virulence through secreted and cell wall PG-associated virulence factors. This bacterium has five PBPs, including two bifunctional glycosyltransferase/transpeptidase class A PBPs, namely, PBP1 and PBP4. We have expressed and purified the latter and have shown that it binds penicillin and catalyzes in vitro glycan chain polymerization with an efficiency of 1,400 M^–1 s^–1 from Escherichia coli lipid II substrate. PBP4 also catalyzes the aminolysis (D-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxypeptidase activities. Disruption of the gene lmo2229 encoding PBP4 in L. monocytogenes EGD did not have any significant effect on growth rate, peptidoglycan composition, cell morphology, or sensitivity to ß-lactam antibiotics but did increase the resistance of the mutant to moenomycin.

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