However, an analysis of cell morphology of L. monocytogenes pAKB-lmo1438 and the control strain in the Selleck GSK3235025 stationary phase of growth showed that the cells of both strains had the same diameter, but those of the former strain were significantly shorter (Figure 3B). The reduced growth rate of L. monocytogenes pAKB-lmo1438 cannot solely be attributed to the overexpression of PBP3, since an elevated level

of PBP4 expression was also found in the recombinant strain, and disruption of the lmo2229 gene indicates that PBP4 is essential for the growth of L. monocytogenes [18]. Therefore, the observed growth retardation may be the result of the overexpression of PBP3, PBP4 or of both these proteins. The clear reduction mTOR inhibitor in the cell length of L. monocytogenes pAKB-lmo1438, with no change in Selleck HMPL-504 cell diameter, suggests a role for PBP3 in cell division. Current models of bacterial cell wall synthesis suggest that distinct wall-synthetic complexes

act in an alternating fashion during the life cycle, to first drive cell elongation by the insertion of peptidoglycan into the cylindrical wall, followed by the switching of most wall-synthetic activity to septum production [20]. In E. coli, the genes required for septation have been identified and most are designated fts (filamentation, temperature sensitive), of which FtsI (a PBP with monofunctional transpeptidase activity) is a major protein of the cell division complex or divisome [21]. Bioinformatic analysis of the L. monocytogenes PBP3 showed that this protein could potentially act as an FtsI cell division transpeptidase [8]. We hypothesize that an excess of PBP3 disturbs the balance between the activities of Rapamycin the cell elongation and cell division complexes, and the majority of peptidoglycan synthesis might be carried out by the septum synthetic machinery. This would explain the production of shorter cells by L. monocytogenes pAKB-lmo1438. We assume that

the formation of short cells is triggered by PBP3 overexpression, rather than increased PBP4 abundance, since transglycosylases are part of the general peptidoglycan synthetic machinery and are not specific for cell division. However, a number of less specialized enzymes are also required for lateral expansion [22]. The postulated participation of PBP3 in cell division is evidently limited to the stationary phase of growth which may result from the presence of a second protein with FtsI activity in L. monocytogenes. Indeed, Lmo2039 is also a potential FtsI cell division transpeptidase and it is suggested that the lmo2039 mutation is lethal for L. monocytogenes [8]. It seems therefore, that Lmo2039 is the main protein involved in division of L. monocytogenes.