ArticleFrontiers in immunology2013
Peptidoglycan glycosyltransferase substrate mimics as templates for the design of new antibacterial drugs.
Article in Frontiers in immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- Recent advances in enzymatic synthesis of β-glucan and cellulose.Carbohydrate research · 2021Review
- Rational structural modification of the isatin scaffold to develop new and potent antimicrobial agents targeting bacterial peptidoglycan glycosyltransferase.RSC advances · 2021Article
- Regulated cleavage of glycan strands by the murein hydrolase SagB inJournal of bacteriology · 2021Article
- Competing Substrates for the Bifunctional Diaminopimelic Acid Epimerase/Glutamate Racemase Modulate Peptidoglycan Synthesis in Chlamydia trachomatis.Infection and immunity · 2020Article
- Squalamine and Aminosterol Mimics Inhibit the Peptidoglycan Glycosyltransferase Activity of PBP1b.Antibiotics (Basel, Switzerland) · 2020Article
- Article
- Peptidoglycan pathways: there are still more!RSC advances · 2019Review
- Identification of glucosyl transferase inhibitors fromJournal of traditional and complementary medicine · 2019Article
- Network-Based Metabolism-Centered Screening of Potential Drug Targets inFrontiers in cellular and infection microbiology · 2019Article
- Selective Inhibition ofAntimicrobial agents and chemotherapy · 2018Article
- Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018Review
- Towards new antibiotics targeting bacterial transglycosylase: Synthesis of a Lipid II analog as stable transition-state mimic inhibitor.Bioorganic & medicinal chemistry letters · 2018Article
- The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization.Cell surface (Amsterdam, Netherlands) · 2018Article
- Glycosyltransferases and Transpeptidases/Penicillin-Binding Proteins: Valuable Targets for New Antibacterials.Antibiotics (Basel, Switzerland) · 2016Review
- Carbohydrate scaffolds as glycosyltransferase inhibitors with in vivo antibacterial activity.Nature communications · 2015Article
- Prospects for novel inhibitors of peptidoglycan transglycosylases.Bioorganic chemistry · 2014Review
- Reversing resistance: The next generation antibacterials.Indian journal of pharmacologyReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptidoglycan (PG) is an essential net-like macromolecule that surrounds bacteria, gives them their shape, and protects them against their own high osmotic pressure. PG synthesis inhibition leads to bacterial cell lysis, making it an important target for many antibiotics. The final two reactions in PG synthesis are performed by penicillin-binding proteins (PBPs). Their glycosyltransferase (GT) activity uses the lipid II precursor to synthesize glycan chains and their transpeptidase (TP) activity catalyzes the cross-linking of two glycan chains via the peptide side chains. Inhibition of either of these two reactions leads to bacterial cell death. β-lactam antibiotics target the transpeptidation reaction while antibiotic therapy based on inhibition of the GTs remains to be developed. Ongoing research is trying to fill this gap by studying the interactions of GTs with inhibitors and substrate mimics and utilizing the latter as templates for the design of new antibiotics. In this review we present an updated overview on the GTs and describe the structure-activity relationship of recently developed synthetic ligands.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.