ArticleActa crystallographica. Section D, Biological crystallography2014
Bacterial periplasmic sialic acid-binding proteins exhibit a conserved binding site.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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.
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Who cites it
28 citing papers in PubMed, 60 citations in OpenAlex.
- Expanding salivary biomarker detection by creating a synthetic neuraminic acid sensor via chimeragenesis.Applied and environmental microbiology · 2026Article
- Structural Basis for Tetramerization ofJournal of microbiology and biotechnology · 2025Article
- Molecular determinants of Neu5Ac binding to a tripartite ATP independent periplasmic (TRAP) transporter.eLife · 2025Article
- On the function of TRAP substrate-binding proteins: the isethionate-specific binding protein IseP.The Biochemical journal · 2024Article
- Allosteric substrate release by a sialic acid TRAP transporter substrate binding protein.Communications biology · 2024Article
- On the function of TRAP substrate-binding proteins: Conformational variation of the sialic acid binding protein SiaP.The Journal of biological chemistry · 2024Article
- Review
- Structural and biophysical analysis of aeLife · 2024Article
- Conformational coupling of the sialic acid TRAP transporter HiSiaQM with its substrate binding protein HiSiaP.Nature communications · 2024Article
- Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter.Nature communications · 2023Article
- Sialic Acid 4-N-Piperazine and Piperidine Derivatives Bind with High Affinity to the P. mirabilis Sialic Acid Sodium Solute Symporter.ChemMedChem · 2022Article
- Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter.Nature communications · 2022Article
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- Biological functions of sialic acid as a component of bacterial endotoxin.Frontiers in microbiology · 2022Review
- Multiple evolutionary origins reflect the importance of sialic acid transporters in the colonization potential of bacterial pathogens and commensals.Microbial genomics · 2021Article
- Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme.Frontiers in molecular biosciences · 2021Review
- Uncovering a novel molecular mechanism for scavenging sialic acids in bacteria.The Journal of biological chemistry · 2020Article
- Glycan cross-feeding supports mutualism between Fusobacterium and the vaginal microbiota.PLoS biology · 2020Article
- Article
- Elucidation of a sialic acid metabolism pathway in mucus-foraging Ruminococcus gnavus unravels mechanisms of bacterial adaptation to the gut.Nature microbiology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Sialic acids are a family of related nine-carbon sugar acids that play important roles in both eukaryotes and prokaryotes. These sialic acids are incorporated/decorated onto lipooligosaccharides as terminal sugars in multiple bacteria to evade the host immune system. Many pathogenic bacteria scavenge sialic acids from their host and use them for molecular mimicry. The first step of this process is the transport of sialic acid to the cytoplasm, which often takes place using a tripartite ATP-independent transport system consisting of a periplasmic binding protein and a membrane transporter. In this paper, the structural characterization of periplasmic binding proteins from the pathogenic bacteria Fusobacterium nucleatum, Pasteurella multocida and Vibrio cholerae and their thermodynamic characterization are reported. The binding affinities of several mutations in the Neu5Ac binding site of the Haemophilus influenzae protein are also reported. The structure and the thermodynamics of the binding of sugars suggest that all of these proteins have a very well conserved binding pocket and similar binding affinities. A significant conformational change occurs when these proteins bind the sugar. While the C1 carboxylate has been identified as the primary binding site, a second conserved hydrogen-bonding network is involved in the initiation and stabilization of the conformational states.
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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.