Murein-hydrolyzing activity of flagellin FlaA of Listeria monocytogenes

In this preliminary report we show that a 29 kDa surface protein of Listeria monocytogenes EGD removed from cells with 4 M LiCl has peptidoglycan (murein) hydrolyzing activity, as revealed by zymographic analysis using Bacillus subtilis murein and heat-killed Micrococcus luteus cells casted in the g...

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Veröffentlicht in:	Polish journal of microbiology 2004, Vol.53 (4), p.237-241
Hauptverfasser:	Popowska, Magdalena, Markiewicz, Zdzislaw
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus subtilis Chromatography, Affinity Electrophoresis, Gel, Two-Dimensional Escherichia coli Escherichia coli - metabolism FlaA protein Flagellin Flagellin - chemistry Flagellin - isolation & purification Flagellin - metabolism Listeria Listeria monocytogenes Listeria monocytogenes - enzymology Micrococcus luteus N-Acetylmuramoyl-L-alanine Amidase - metabolism Peptidoglycan - metabolism Peptidoglycans
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Zusammenfassung:	In this preliminary report we show that a 29 kDa surface protein of Listeria monocytogenes EGD removed from cells with 4 M LiCl has peptidoglycan (murein) hydrolyzing activity, as revealed by zymographic analysis using Bacillus subtilis murein and heat-killed Micrococcus luteus cells casted in the gel. Following two-dimensional electrophoresis, the protein was electroblotted to PVDF membrane and its identity (FlaA) was revealed by sequencing. Peptidoglycan hydrolysing activity of FlaA purified by FPLC on Mono-S Sepharose against labelled Escherichia coli murein was demonstrated.
ISSN:	1733-1331 2544-4646