analysis of the peptidoglycan hydrolase complement of lactobacillus casei and characterization of the major γ-d-glutamyl-l-lysyl-endopeptidase分析的肽聚糖水解酶补干酪乳杆菌和表征主要γ-d-glutamyl-l-lysyl-endopeptidase.pdfVIP

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analysis of the peptidoglycan hydrolase complement of lactobacillus casei and characterization of the major γ-d-glutamyl-l-lysyl-endopeptidase分析的肽聚糖水解酶补干酪乳杆菌和表征主要γ-d-glutamyl-l-lysyl-endopeptidase.pdf

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analysis of the peptidoglycan hydrolase complement of lactobacillus casei and characterization of the major γ-d-glutamyl-l-lysyl-endopeptidase分析的肽聚糖水解酶补干酪乳杆菌和表征主要γ-d-glutamyl-l-lysyl-endopeptidase

Analysis of the Peptidoglycan Hydrolase Complement of Lactobacillus casei and Characterization of the Major c-D-Glutamyl-L-Lysyl-Endopeptidase 1,2 1,2 1,2 3 3¤ Krzysztof Regulski , Pascal Courtin , Mickael Meyrand , Ingmar J. J. Claes , Sarah Lebeer , 3 4 1,2 1,2 Jos Vanderleyden , Pascal Hols , Alain Guillot , Marie-Pierre Chapot-Chartier * 1 Institut National de la Recherche Agronomique, UMR1319 Micalis, Jouy-en-Josas, France, 2 AgroParisTech, UMR Micalis, Jouy-en-Josas, France, 3 Centre of Microbial and ´ ´ ´ ´ ´ Plant Genetics, K.U. Leuven, Leuven, Belgium, 4 Biochimie et Genetique Moleculaire Bacterienne, Institut des Sciences de la Vie, Universite Catholique de Louvain, Louvain- la-Neuve, Belgium Abstract Peptidoglycan (PG) is the major component of Gram positive bacteria cell wall and is essential for bacterial integrity and shape. Bacteria synthesize PG hydrolases (PGHs) which are able to cleave bonds in their own PG and play major roles in PG remodelling required for bacterial growth and division. Our aim was to identify the main PGHs in Lactobacillus casei BL23, a lactic acid bacterium with probiotic properties. The PGH complement was first identified in silico by amino acid sequence similarity searches of the BL23 genome sequence. Thirteen PGHs were detected with different predicted hydrolytic specificities. Transcription of the genes was confirmed by RT-PCR. A