RESEARCH ARTICLE


The Inactivation of a New Peptidoglycan Hydrolase Pmp23 Leads to Abnormal Septum Formation in Streptococcus pneumoniae



Pagliero E1, Dublet B2, Frehel C3, Dideberg O4, Vernet T1, *, Di Guilmi AM1
1 Laboratoire d'Ingénierie des Macromolécules
2 Laboratoire de Spectrométrie de Masse des Protéines
3 INSERM U570, Faculté de Médecine Necker-Enfants Malades, 156 rue de Vaugirard, 75730 Paris cedex 15, France
1,2,4 Institut de Biologie Structurale Jean-Pierre Ebel (CEA-CNRS UMR 5075-UJF), 41 Rue Jules Horowitz 38027 Grenoble cedex 1, France


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© Pagliero et al.; Licensee Bentham Open.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.

* Address correspondence to this author at the Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz 38027 Grenoble cedex 1, France; Tel: 33-04 38 78 96 81; Fax: 33-04 38 78 54 94; E-mail: vernet@ibs.fr.


Abstract

The bacterial peptidoglycan is the major component of the cell wall which integrity is essential to cell survival. In a previous work, we identified, in the positive-Gram pathogen Streptococcus pneumoniae , a unique protein containing a new putative peptidoglycan hydrolytic domain named PECACE (PEptidoglycan CArbohydrate Cleavage Enzyme). In this study, we characterise the physiological function of this protein called Pmp23 (Pneumococcal Membrane Protein of 23 kDa). A cell wall hydrolytic activity is observed with the recombinant protein. Inactivation of the pmp23 gene in the pneumococcus led to a decreased flocculation, an increased sensitivity to β-lactam antibiotics and morphological alterations affecting the formation and localisation of the division septa. Taken together these observations indicate that Pmp23 is a hydrolase whose function is linked to peptidoglycan metabolism at the septum site.