ArticleNature chemical biology2019
Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 41 citations in OpenAlex.
- A geroprotective probiotic and its functional metabolite counteract inflammaging to extend healthspan.Nature aging · 2026Article
- In silico typing maps the natural diversity of Escherichia coli transporter-dependent capsules.Nature microbiology · 2026Article
- Phage-steering permits antibody-mediated clearance of E. coli K1 from the gut.Nature communications · 2026Article
- Mechanisms governing bacterial capsular polysaccharide attachment and chain length.Annals of the New York Academy of Sciences · 2025Review
- Transition transferases prime bacterial capsule polymerization.Nature chemical biology · 2025Article
- Article
- Modeling and Simulation of Bacterial Outer Membranes with Lipopolysaccharides and Capsular Polysaccharides.Journal of chemical information and modeling · 2023Article
- Bioengineered materials with selective antimicrobial toxicity in biomedicine.Military Medical Research · 2023Review
- LPS O Antigen Plays a Key Role in Klebsiella pneumoniae Capsule Retention.Microbiology spectrum · 2022Article
- Article
- Infant gut strain persistence is associated with maternal origin, phylogeny, and traits including surface adhesion and iron acquisition.Cell reports. Medicine · 2021Article
- A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family.Nature chemical biology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several important Gram-negative bacterial pathogens possess surface capsular layers composed of hypervariable long-chain polysaccharides linked via a conserved 3-deoxy-β-D-manno-oct-2-ulosonic acid (β-Kdo) oligosaccharide to a phosphatidylglycerol residue. The pathway for synthesis of the terminal glycolipid was elucidated by determining the structures of reaction intermediates. In Escherichia coli, KpsS transfers a single Kdo residue to phosphatidylglycerol; this primer is extended using a single enzyme (KpsC), possessing two cytidine 5'-monophosphate (CMP)-Kdo-dependent glycosyltransferase catalytic centers with different linkage specificities. The structure of the N-terminal β-(2→4) Kdo transferase from KpsC reveals two α/β domains, supplemented by several helices. The N-terminal Rossmann-like domain, typically responsible for acceptor binding, is severely reduced in size compared with canonical GT-B folds in glycosyltransferases. The similar structure of the C-terminal β-(2→7) Kdo transferase indicates a past gene duplication event. Both Kdo transferases have a narrow active site tunnel, lined with key residues shared with GT99 β-Kdo transferases. This enzyme provides the prototype for the GT107 family.
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