Structure, biochemistry and mechanism of action of glycopeptide antibiotics

Reynolds, P. E.

doi:10.1007/bf01967563

Cited by 699Antimicrobial Resistance in StaphylococcusBacterial Genetics and BiotechnologyAntimicrobial Peptides and Activities

Structure, biochemistry and mechanism of action of glycopeptide antibiotics

Reynolds, P. E.·1989·European Journal of Clinical Microbiology & Infectious Diseases

DOI 10.1007/bf01967563

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Abstract

Glycopeptide antibiotics, including vancomycin and teicoplanin, are large, rigid molecules that inhibit a late stage in bacterial cell wall peptidoglycan synthesis. The three-dimensional structure contains a cleft into which peptides of highly specific configuration (L-aa-D-aa-D-aa) can fit: such sequences are found only in bacterial cell walls, hence glycopeptides are selectively toxic. Glycopeptides interact with peptides of this conformation by hydrogen bonding, forming stable complexes. As a result of binding to L-aa-D-Ala-D-Ala groups in wall intermediates, glycopeptides inhibit, apparently by steric hindrance, the formation of the backbone glycan chains (catalysed by peptidoglycan polymerase) from the simple wall subunits as they are extruded through the cytoplasmic membrane. The subsequent transpeptidation reaction that imparts rigidity to the cell wall is also thus inhibited. This unique mechanism of action, involving binding of the bulky inhibitor to the substrate outside the membrane so that the active sites of two enzymes cannot align themselves correctly, renders the acquisition of resistance to the glycopeptide antibiotics more difficult than that to the majority of the other antibiotic groups.

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It has been postulated that the main effect of vancomycin binding to D-Ala-D-Ala-ending precursors is alteration of transglycosylation, presumably by steric hindrance, preventing further processing of the cell wall and leading to bacterial death.
“It has been postulated that the main effect of the binding of vancomycin to D-Ala-D-Ala-ending precursors emerging from the cytoplasm is alteration of transglycosylation (presumably due to steric hindrance) preventing further processing of the cell wall and leading to bacterial death (72).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [72]

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Authors: Reynolds, P. E.
Affiliations: University of Cambridge (GB)
Corresponding author: Reynolds, P. E.
Venue: European Journal of Clinical Microbiology & Infectious Diseases
Publisher: Springer Science and Business Media LLC
Published: 1989-11
Volume: 8
Issue: 11
Pages: 943-950
ISSN: 0934-9723 (ISSN-L)
1435-4373
DOI: 10.1007/bf01967563
OpenAlex: W2020612301
Cited by: 699
References: 24
Citations by year: 2026: 17 · 2025: 20 · 2024: 21 · 2023: 27 · 2022: 28 · 2021: 36 · 2020: 28 · 2019: 29 · 2018: 31 · 2017: 23 · 2016: 33 · 2015: 35 · 2014: 32 · 2013: 25 · 2012: 22
FWCI: 7.77
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: European Journal of Clinical Microbiology & Infectious Diseases (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Keywords: glycopeptides, vancomycin, teicoplanin, peptidoglycan synthesis inhibition, cell wall biosynthesis, antibiotic mechanism of action, antibiotic resistance, transpeptidation, hydrogen bonding, selective toxicity, three-dimensional structure
MeSH terms: Amino Acid Sequence, Anti-Bacterial Agents, Bacteria, Cell Wall, Drug Resistance, Microbial, Glycopeptides, Humans, Models, Molecular, Molecular Sequence Data, Peptidoglycan, Vancomycin, Molecular Structure, Teicoplanin

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Structure, biochemistry and mechanism of action of glycopeptide antibiotics

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