ArticlePLoS pathogens2016
Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 65 citations in OpenAlex.
- Characterization ofInfection and immunity · 2026Article
- Bacteriophage Challenge Drives Genomic and Proteomic Remodeling and Alters Antibiotic Resistance in a Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2026Article
- Structure-based computational investigation of potential TarA inhibitors in Staphylococcus aureus.Molecular diversity · 2026Article
- Phage Intolerance Impacts Antibiotic Susceptibility and Virulence in Staphylococcus aureus.Current microbiology · 2026Article
- A teichoic acid-like wall modification associated with immune suppression is socially regulated inmBio · 2026Article
- Article
- A teichoic acid-like wall modification associated with immune suppression is socially regulated inbioRxiv : the preprint server for biology · 2026Article
- WrtF fromProceedings of the National Academy of Sciences of the United States of America · 2025Article
- In Vivo Emergence of Podovirus Resistance viaViruses · 2025Article
- Article
- Molecular properties of the RmlT wall teichoic acid rhamnosyltransferase that modulates virulence in Listeria monocytogenes.Nature communications · 2025Article
- Chitin Translocation Is Functionally Coupled with Synthesis in Chitin Synthase.International journal of molecular sciences · 2024Article
- Klebsiella pneumoniae O-polysaccharide biosynthesis highlights the diverse organization of catalytic modules in ABC transporter-dependent glycan assembly.The Journal of biological chemistry · 2024Article
- Unveiling the Multifaceted Capabilities of EndophyticPharmaceuticals (Basel, Switzerland) · 2024Article
- Cryo-EM analysis ofScience advances · 2024Article
- InvasiveScience advances · 2023Article
- Article
- Genetic diversity ofMicrobial genomics · 2022Article
- A dZnONPs Enhanced Hybrid Injectable Photocrosslinked Hydrogel for Infected Wounds Treatment.Gels (Basel, Switzerland) · 2022Article
- Structural and mechanistic investigations of protein S-glycosyltransferases.Cell chemical biology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, there has been a growing interest in teichoic acids as targets for antibiotic drug design against major clinical pathogens such as Staphylococcus aureus, reflecting the disquieting increase in antibiotic resistance and the historical success of bacterial cell wall components as drug targets. It is now becoming clear that β-O-GlcNAcylation of S. aureus wall teichoic acids plays a major role in both pathogenicity and antibiotic resistance. Here we present the first structure of S. aureus TarS, the enzyme responsible for polyribitol phosphate β-O-GlcNAcylation. Using a divide and conquer strategy, we obtained crystal structures of various TarS constructs, mapping high resolution overlapping N-terminal and C-terminal structures onto a lower resolution full-length structure that resulted in a high resolution view of the entire enzyme. Using the N-terminal structure that encapsulates the catalytic domain, we furthermore captured several snapshots of TarS, including the native structure, the UDP-GlcNAc donor complex, and the UDP product complex. These structures along with structure-guided mutants allowed us to elucidate various catalytic features and identify key active site residues and catalytic loop rearrangements that provide a valuable platform for anti-MRSA drug design. We furthermore observed for the first time the presence of a trimerization domain composed of stacked carbohydrate binding modules, commonly observed in starch active enzymes, but adapted here for a poly sugar-phosphate glycosyltransferase.
Indexed as
Identifiers
What OpenQuestion holds
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.