Impact of peptidoglycan O-acetylation on autolytic activities of the Enterococcus faecalis N-acetylglucosaminidase AtlA and N-acetylmuramidase AtlB.

Aurélie Emirian (1) , Sophie Fromentin (1) , Catherine Eckert (1) , Françoise Chau (2) , Lionel Dubost (3) , Muriel Delepierre (4) , Laurent Gutmann (1, 5) , Michel Arthur (1) , Stéphane Mesnage (1)

1 CRC (UMR_S 872) - Centre de Recherche des Cordeliers
2 EA3964 - Emergence de la résistance bactérienne in vivo
3 Plateforme de Spectrométrie de Masse et de Protéomique du Muséum
4 Résonance Magnétique Nucléaire des Biomolécules
5 HEGP - Hôpital Européen Georges Pompidou [APHP]

Autolysins are potentially lethal enzymes that partially hydrolyze peptidoglycan for incorporation of new precursors and septum cleavage after cell division. Here, we explored the impact of peptidoglycan O-acetylation on the enzymatic activities of Enterococcus faecalis major autolysins, the N-acetylglucosaminidase AtlA and the N-acetylmuramidase AtlB. We constructed isogenic strains with various O-acetylation levels and used them as substrates to assay E. faecalis autolysin activities. Peptidoglycan O-acetylation had a marginal inhibitory impact on the activities of these enzymes. In contrast, removal of cell wall glycopolymers increased the AtlB activity (37-fold), suggesting that these polymers negatively control the activity of this enzyme.

Domains: Life Sciences [q-bio]; Biochemistry, Molecular Biology

Aurélie Emirian, Sophie Fromentin, Catherine Eckert, Françoise Chau, Lionel Dubost, et al.. Impact of peptidoglycan O-acetylation on autolytic activities of the Enterococcus faecalis N-acetylglucosaminidase AtlA and N-acetylmuramidase AtlB.. FEBS Letters, 2009, 583 (18), pp.3033-8. ⟨10.1016/j.febslet.2009.08.010⟩. ⟨pasteur-00512062⟩