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Journal of Bacteriology, June 2009, p. 3752-3757, Vol. 191, No. 11
0021-9193/09/$08.00+0 doi:10.1128/JB.00126-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Michael Erkelenz,1,2,
Elvis Bernard,2
Pascal Courtin,2
Saulius Kulakauskas,1 and
Marie-Pierre Chapot-Chartier2*
INRA, UR888 Bactéries Lactiques et Pathogènes Opportunistes, F-78350 Jouy-en-Josas, France,1 INRA, UR477 Biochimie Bactérienne, F-78350 Jouy-en-Josas, France2
Received 30 January 2009/ Accepted 20 March 2009
We show that in Lactococcus lactis, the gene asnH encodes the asparagine synthase involved in amidation of D-Asp present in peptidoglycan side chains and crossbridges. The level of D-Asp amidation in peptidoglycan has a strong effect on the sensitivity of bacteria to endogenous autolysins and to the cationic antimicrobials nisin and lysozyme.
Published ahead of print on 27 March 2009.
Present address: Danone Research, Centre Daniel Carasso, RD 128, Avenue de la Vauve, 91767 Palaiseau Cedex, France.
Present address: Universität Dortmund, FB Chemie Biologisch-Chemische Mikrostrukturtechnik, Otto-Hahn-Str. 6, D-44227 Dortmund, Germany.
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