PMID: 7541399Jul 1, 1995Paper

Localization of penicillin-binding proteins to the splitting system of Staphylococcus aureus septa by using a mercury-penicillin V derivative

Journal of Bacteriology
T R PaulT J Beveridge

Abstract

Precise localization of penicillin-binding protein (PBP)-antibiotic complexes in a methicillin-sensitive Staphylococcus aureus strain (BB255), its isogenic heterogeneous methicillin-resistant transductant (BB270), and a homogeneous methicillin-resistant strain (Col) was investigated by high-resolution electron microscopy. A mercury-penicillin V (Hg-pen V) derivative was used as a heavy metal-labeled, electron-dense probe for accurately localizing PBPs in situ in single bacterial cells during growth. The most striking feature of thin sections was the presence of an abnormally large (17 to 24 nm in width) splitting system within the thick cross walls or septa of Hg-pen V-treated bacteria of all strains. Untreated control cells possessed a thin, condensed splitting system, 7 to 9 nm in width. A thick splitting system was also distinguishable in unstained thin sections, thereby confirming that the electron contrast of this structure was not attributed to binding of bulky heavy metal stains usually used for electron microscopy. Biochemical analyses demonstrated that Hg-pen V bound to isolated plasma membranes as well as sodium dodecyl sulfate-treated cell walls and that two or more PBPs in each strain bound to this antibiotic. In co...Continue Reading

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Citations

Apr 1, 1997·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·O G Brakstad, J A Maeland
Mar 23, 2007·Molecular Microbiology·Valério R F Matias, Terry J Beveridge
Jan 31, 2009·Nature Reviews. Drug Discovery·Jia JiaYu Zong Chen
May 20, 2004·Journal of Bacteriology·Ahmed TouhamiTerry J Beveridge
Jan 28, 2012·Environmental Research·Christina S HölzelJohann Bauer
Dec 5, 1998·Microbiology and Molecular Biology Reviews : MMBR·P GiesbrechtJ Wecke
Mar 12, 2020·ACS Infectious Diseases·Declan Alan Gray, Michaela Wenzel

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