Analysis of the murein of a Listeria monocytogenes EGD mutant lacking functional penicillin binding protein 5 (PBP5).
Cells of a mutant of Listeria monocytogenes lacking functional PBP5, an enzyme with DD-carboxypeptidase activity, make thicker cells walls. In this study we show that the muropeptide profile of the mutant, obtained after HPLC analysis of a muramidase digest of cell wall murein, differs from that for the wild type strain. The main differences embrace strongly reduced disaccharide-tripeptide content, strongly increased amounts of pentapeptide-containing muropeptides and a shift in profile from less cross-linked muropeptides (monomers, dimers) towards more highly cross-linked ones.
Korsak
Dorota
D
Department of General Microbiology, Faculty of Biology, Warsaw University, Poland. d.korsak@uw.edu.pl
Popowska
Magdalena
M
Markiewicz
Zdzisław
Z
D002473:Cell Wall / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D005798:Genes, Bacterial; D008089:Listeria monocytogenes / Q000235:genetics* / Q000378:metabolism*; D046912:Multiprotein Complexes; D009154:Mutation; D046915:Penicillin-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D010457:Peptidoglycan / Q000737:chemistry* / Q000235:genetics*
D046912:Multiprotein Complexes; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan