ArticleBMC structural biology2015
Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor.
Article in BMC structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Impedimetric Characterization of NanA Structural Domains Activity on Sialoside-Containing Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Recent advances in the discovery of plant-derived antimicrobial natural products to combat antimicrobial resistant pathogens: insights from 2018-2022.Natural product reports · 2023Review
- Co-infection of the respiratory epithelium, scene of complex functional interactions between viral, bacterial, and human neuraminidases.Frontiers in microbiology · 2023Review
- Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Efficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells.Acta biochimica et biophysica Sinica · 2022Article
- Structural and functional characterisation of a stable, broad-specificity multimeric sialidase from the oral pathogen Tannerella forsythia.The Biochemical journal · 2022Article
- The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing.Proteins · 2022Article
- Activity of a Carbohydrate-Binding Module Therapy, Neumifil, against SARS-CoV-2 Disease in a Hamster Model of Infection.Viruses · 2022Article
- The assessment of Pseudomonas aeruginosa lectin LecA binding characteristics of divalent galactosides using multiple techniques.Glycobiology · 2021Article
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Molecular Characterization of Hemorrhagic Enteritis Virus (HEV) Obtained from Clinical Samples in Western Canada 2017-2018.Viruses · 2020Article
- Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.Nature communications · 2019Article
- Streptococcus oralis subsp.Infection and immunity · 2019Article
- Design, synthesis, and evaluation of curcumin analogues as potential inhibitors of bacterial sialidase.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- The study of multivalent carbohydrate-protein interactions by bio-layer interferometry.Organic & biomolecular chemistry · 2018Article
- Article
- Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus.Nature communications · 2017Article
- Erratum to: Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor.BMC structural biology · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundStreptococcus pneumoniae Neuraminidase A (NanA) is a multi-domain protein anchored to the bacterial surface. Upstream of the catalytic domain of NanA is a domain that conforms to the sialic acid-recognising CBM40 family of the CAZY (carbohydrate-active enzymes) database. This domain has been identified to play a critical role in allowing the bacterium to promote adhesion and invasion of human brain microvascular endothelial cells, and hence may play a key role in promoting bacterial meningitis. In addition, the CBM40 domain has also been reported to activate host chemokines and neutrophil recruitment during infection.
resultsCrystal structures of both apo- and holo- forms of the NanA CBM40 domain (residues 121 to 305), have been determined to 1.8 Å resolution. The domain shares the fold of other CBM40 domains that are associated with sialidases. When in complex with α2,3- or α2,6-sialyllactose, the domain is shown to interact only with the terminal sialic acid. Significantly, a deep acidic pocket adjacent to the sialic acid-binding site is identified, which is occupied by a lysine from a symmetry-related molecule in the crystal. This pocket is adjacent to a region that is predicted to be involved in protein-protein interactions.
conclusionsThe structural data provide the details of linkage-independent sialyllactose binding by NanA CBM40 and reveal striking surface features that may hold the key to recognition of binding partners on the host cell surface. The structure also suggests that small molecules or sialic acid analogues could be developed to fill the acidic pocket and hence provide a new therapeutic avenue against meningitis caused by S. pneumoniae.
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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.