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Resistance to β-Lactam Antibiotics Mediated by Alterations of Penicillin-Binding Proteins

  • Chapter
Microbial Resistance to Drugs

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 91))

Abstract

Beta-lactam antibiotics interfere with the biosynthesis of the bacterial cell wall by acting as analogues of the acyl-d-alanyl-d-alanine moiety of the lipid-linked disaccharide-pentapeptide substrate of the enzymes that catalyse the synthesis of crosslinked peptidoglycan (Waxman and Strominger 1983). These enzymes can be detected and studied as penicillin-binding proteins (PBPs) as they are essentially irreversibly acylated by penicillin, and other β-lactam antibiotics, resulting in an inactive penicilloyl-enzyme that is analogous to the acyl-enzyme formed during the processing of their normal peptide substrate (Spratt and Pardee 1975; Spratt 1983).

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  1. B. G. Spratt
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  1. Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Health Sciences Centre, 3330 Hospital Drive N.W., T2N 4N1, Calgary, Alberta, Canada

    Lawrence E. Bryan M.D., Ph. D., F.R.C.P. (C.) (Head) (Head)

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Spratt, B.G. (1989). Resistance to β-Lactam Antibiotics Mediated by Alterations of Penicillin-Binding Proteins. In: Bryan, L.E. (eds) Microbial Resistance to Drugs. Handbook of Experimental Pharmacology, vol 91. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74095-4_4

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  • DOI: https://doi.org/10.1007/978-3-642-74095-4_4

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