Journal Article

Induction of β-Lactamase in <i>Enterobacter cloacae</i>

Bernd Wiedemann, Helgard Dietz and Dieter Pfeifle

in Clinical Infectious Diseases

Published on behalf of Infectious Diseases Society of America

Volume 27, issue Supplement_1, pages S42-S47
Published in print August 1998 | ISSN: 1058-4838
Published online August 1998 | e-ISSN: 1537-6591 | DOI:
Induction of β-Lactamase in Enterobacter cloacae

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β-lactamase induction in Enterobacter cloacae, which is linked to peptidoglycan recycling, was investigated with use of high-performance liquid chromatography of cell wall fragments in genetically defined cells of Escherichia coli. After treatment of cells with β-lactams, we detected in the periplasm an increase of D-tripeptide (N-acetylglucosaminyl-1,6 anhydro N-acetylmuramyl-l-alanyl- d-glutamyl-meso-diaminopimelic acid), D-tetrapeptide (N-acetylglucosaminyl-1,6 anhydro N-acetylmuramyl-l-alanyl-d-glutamyl-meso-diaminopimelic acid-d-alanine), and a yet-unknown anhydromuropeptide. We identified this anhydromuramylpeptide by fast atom bombardment-mass spectrometry as anhydromuramyl-pentapeptide. The amount of these molecules did not alter after treatment with cell wall-active non β-lactams. The transmembrane protein AmpG transports not only D-tripeptide but also D-pentapeptide into the cell. In the cytoplasm these molecules are degraded into the corresponding monosaccharide peptides M-tripeptide (N-acetylmuramyl-l-alanyl- d-glutamyl-meso-diaminopimelic acid) and M-pentapeptide (N-acetylmuramyl-l-alanyl-d-glutamyl- meso-diaminopimelic acid-d-alanine-d-alanine). These findings indicate that besides M-tripeptide and D-tripeptide, probably M-tetrapeptide, D-tetrapeptide, M-pentapeptide, and D-pentapeptide are also signal muropeptides for β-lactamase induction.

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Subjects: Infectious Diseases ; Immunology ; Public Health and Epidemiology ; Microbiology

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