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Infection and Immunity, November 2007, p. 5390-5398, Vol. 75, No. 11
0019-9567/07/$08.00+0     doi:10.1128/IAI.00571-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Enterococcus faecalis Constitutes an Unusual Bacterial Model in Lysozyme Resistance{triangledown}

Laurent Hébert,1 Pascal Courtin,2 Riccardo Torelli,3 Maurizio Sanguinetti,3 Marie-Pierre Chapot-Chartier,2 Yanick Auffray,1 and Abdellah Benachour1*

Laboratoire de Microbiologie de l'Environnement, USC INRA 2017, EA956, Université de Caen, 14032 Caen Cedex, France,1 Unité de Biochimie Bactérienne, UR477, INRA, 78350 Jouy-en-Josas, France,2 Institute of Microbiology, Catholic University of Sacred Heart, L. go F. Vito 1, 00168 Rome, Italy3

Received 19 April 2007/ Returned for modification 15 June 2007/ Accepted 14 August 2007

Lysozyme is an important and widespread compound of the host constitutive defense system, and it is assumed that Enterococcus faecalis is one of the few bacteria that are almost completely lysozyme resistant. On the basis of the sequence analysis of the whole genome of E. faecalis V583 strain, we identified two genes that are potentially involved in lysozyme resistance, EF_0783 and EF_1843. Protein products of these two genes share significant homology with Staphylococcus aureus peptidoglycan O-acetyltransferase (OatA) and Streptococcus pneumoniae N-acetylglucosamine deacetylase (PgdA), respectively. In order to determine whether EF_0783 and EF_1843 are involved in lysozyme resistance, we constructed their corresponding mutants and a double mutant. The {Delta}EF_0783 mutant and {Delta}EF_0783 {Delta}EF_1843 double mutant were shown to be more sensitive to lysozyme than the parental E. faecalis JH2-2 strain and {Delta}EF_1843 mutant were. However, compared to other bacteria, such as Listeria monocytogenes or S. pneumoniae, the tolerance of {Delta}EF_0783 and {Delta}EF_0783 {Delta}EF_1843 mutants towards lysozyme remains very high. Peptidoglycan structure analysis showed that EF_0783 modifies the peptidoglycan by O acetylation of N-acetyl muramic acid, while the EF_1843 deletion has no obvious effect on peptidoglycan structure under the same conditions. Moreover, the EF_0783 and EF_1843 deletions seem to significantly affect the ability of E. faecalis to survive within murine macrophages. In all, while EF_0783 is currently involved in the lysozyme resistance of E. faecalis, peptidoglycan O acetylation and de-N-acetylation are not the main mechanisms conferring high levels of lysozyme resistance to E. faecalis.

* Corresponding author. Mailing address: Laboratoire de Microbiologie de l'Environnement, USC INRA 2017, EA956, Université de Caen, 14032 Caen Cedex, France. Phone: 33 (0)2 31 56 66 18. Fax: 33 (0)2 31 56 53 11. E-mail: abdellah.benachour{at}unicaen.fr

{triangledown} Published ahead of print on 4 September 2007.

Editor: F. C. Fang

Infection and Immunity, November 2007, p. 5390-5398, Vol. 75, No. 11
0019-9567/07/$08.00+0     doi:10.1128/IAI.00571-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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