AI Article Synopsis
- Peptidoglycan is a vital part of bacterial cell walls that protects against damage and is a target for antibiotics like β-lactams and glycopeptides.
- Class A penicillin-binding proteins (PBPs) help synthesize peptidoglycan by linking sugar chains and peptides, although their function in natural membranes is not fully understood.
- A new assay using Förster resonance energy transfer has been created to study the real-time activity of these PBPs in lipid environments, aiding in the understanding of peptidoglycan synthesis and potential development of new antibiotics.
Article Abstract
Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from and in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7943195 | PMC |
| http://dx.doi.org/10.7554/eLife.61525 | DOI Listing |
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