The Inactivation of a New Peptidoglycan Hydrolase Pmp23 Leads to Abnormal Septum Formation in Streptococcus pneumoniae
| Autor: | Dublet B, Pagliero E, Dideberg O, Vernet T, Di Guilmi Am, Frehel C |
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| Rok vydání: | 2008 |
| Předmět: |
chemistry.chemical_classification
General Immunology and Microbiology Biology medicine.disease_cause Article Microbiology law.invention Cell wall chemistry.chemical_compound Enzyme Membrane protein chemistry Biochemistry law Streptococcus pneumoniae Hydrolase medicine Recombinant DNA Peptidoglycan Cell envelope |
| Zdroj: | The Open Microbiology Journal |
| ISSN: | 1874-2858 |
| DOI: | 10.2174/1874285800802010107 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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