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Pesticin displays muramidase activity

Lookup NU author(s): Professor Waldemar Vollmer


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Pesticin of Yersinia pestis is the only bacteriocin that converts sensitive cells to stable spheroplasts. The amino acid sequence of pesticin as derived from the nucleotide sequence shows no similarity to those of any of the bacteriocins. The unique properties of pesticin prompted an investigation of its mode of action. Since the pesticin plasmid does not encode a lysis protein for release of pesticin into the culture medium, pesticin was isolated from cells and purified to electrophoretic homogeneity. Highly purified pesticin degraded murein and murein glycan strands lacking the peptide side chains to products that were similar to those obtained by lysozyme, as revealed by high- resolution high-pressure liquid chromatography. After reduction of the murein degradation products with tritium-labeled sodium borohydride, acid hydrolysis, and separation of the products by thin-layer chromatography, radiolabeled muraminitol was identified. This indicates that pesticin is a muramidase, and not an N-acetyl-glucosaminidase, that converts cells into stable spheroplasts by slowly degrading murein.

Publication metadata

Author(s): Vollmer W, Pilsl H, Hantke K, Höltje J-V, Braun V

Publication type: Article

Publication status: Published

Journal: Journal of Bacteriology

Year: 1997

Volume: 179

Issue: 5

Pages: 1580-1583

Print publication date: 01/03/1997

ISSN (print): 0021-9193

ISSN (electronic): 1067-8832

Publisher: American Society for Microbiology