ArticlePLoS pathogens2020
The role of 9-O-acetylated glycan receptor moieties in the typhoid toxin binding and intoxication.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 35 citations in OpenAlex.
- Editorial Note: The role of 9-O-acetylated glycan receptor moieties in the typhoid toxin binding and intoxication.PLoS pathogens · 2026Article
- Functional synergy of heteropentameric B subunits underlies virulence in a Salmonella A2B5 toxin.PLoS pathogens · 2025Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Molecular basis of the hepatobiliary tropism of typhoid toxin promotingScience advances · 2025Article
- Typhoid toxin causes neuropathology by disrupting the blood-brain barrier.Nature microbiology · 2025Article
- The diverse landscape of AB5-type toxins.Engineering microbiology · 2023Review
- Application of the Nicoya OpenSPR to Studies of Biomolecular Binding: A Review of the Literature from 2016 to 2022.Sensors (Basel, Switzerland) · 2023Review
- Delivery, structure, and function of bacterial genotoxins.Virulence · 2022Review
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Malnutrition and maternal vaccination against typhoid toxin.PLoS pathogens · 2022Article
- Sulfation of sialic acid is ubiquitous and essential for vertebrate development.Scientific reports · 2022Article
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- Glycan-mediated molecular interactions in bacterial pathogenesis.Trends in microbiology · 2022Review
- Article
- Neutralization of Typhoid Toxin by Alpaca-Derived, Single-Domain Antibodies Targeting the PltB and CdtB Subunits.Infection and immunity · 2022Article
- Bacterial AB toxins and host-microbe interactions.Advances in microbial physiology · 2022Review
- Diversity of sialic acids and sialoglycoproteins in gametes and at fertilization.Frontiers in cell and developmental biology · 2022Review
- The evolutionary diversification of theFrontiers in microbiology · 2022Article
- Article
- The structural basis of Salmonella ACell reports · 2021Article
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12 authors at 2 institutions in 1 country.
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Abstract
Typhoid toxin is an A2B5 toxin secreted from Salmonella Typhi-infected cells during human infection and is suggested to contribute to typhoid disease progression and the establishment of chronic infection. To deliver the enzymatic 'A' subunits of the toxin to the site of action in host cells, the receptor-binding 'B' subunit PltB binds to the trisaccharide glycan receptor moieties terminated in N-acetylneuraminic acid (Neu5Ac) that is α2-3 or α2-6 linked to the underlying disaccharide, galactose (Gal) and N-acetylglucosamine (GlcNAc). Neu5Ac is present in both unmodified and modified forms, with 9-O-acetylated Neu5Ac being the most common modification in humans. Here we show that host cells associated with typhoid toxin-mediated clinical signs express both unmodified and 9-O-acetylated glycan receptor moieties. We found that PltB binds to 9-O-acetylated α2-3 glycan receptor moieties with a markedly increased affinity, while the binding affinity to 9-O-acetylated α2-6 glycans is only slightly higher, as compared to the affinities of PltB to the unmodified counterparts, respectively. We also present X-ray co-crystal structures of PltB bound to related glycan moieties, which supports the different effects of 9-O-acetylated α2-3 and α2-6 glycan receptor moieties on the toxin binding. Lastly, we demonstrate that the cells exclusively expressing unmodified glycan receptor moieties are less susceptible to typhoid toxin than the cells expressing 9-O-acetylated counterparts, although typhoid toxin intoxicates both cells. These results reveal a fine-tuning mechanism of a bacterial toxin that exploits specific chemical modifications of its glycan receptor moieties for virulence and provide useful insights into the development of therapeutics against typhoid fever.
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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.