title: The Inactivation of a New Peptidoglycan Hydrolase Pmp23 Leads to Abnormal Septum Formation in Streptococcus pneumoniae.
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 beta-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.
authors.affiliation: Laboratoire d'Ingénierie des Macromolécules.
authors.forename: Pagliero
authors.initials: P
authors.lastname: E
authors.forename: Dublet
authors.initials: D
authors.lastname: B
authors.forename: Frehel
authors.initials: F
authors.lastname: C
authors.forename: Dideberg
authors.initials: D
authors.lastname: O
authors.forename: Vernet
authors.initials: V
authors.lastname: T
authors.forename: Di Guilmi
authors.initials: DG
authors.lastname: Am