ArticleMolecular bioSystems2011
Identifying selective inhibitors against the human cytosolic sialidase NEU2 by substrate specificity studies.
Article in Molecular bioSystems, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 62 citations in OpenAlex.
- Improved C5-Amide Bioisosteres for Human Neuraminidase 1 Inhibitors Based on 2-Deoxy-2,3-Didehydro-N-Acetyl Neuraminic Acid.ChemMedChem · 2025Article
- Catch, Cut, or Block? Versatile 4-N-Derivatized Sialyl Glycosides for Influenza Virus Neuraminidase Detection and Purification.Angewandte Chemie (International ed. in English) · 2025Article
- Synthetic Sialosides Terminated with 8-N-Substituted Sialic Acid as Selective Substrates for Sialidases from Bacteria and Influenza Viruses.Angewandte Chemie (International ed. in English) · 2024Article
- The role of sialidase Neu1 in respiratory diseases.Respiratory research · 2024Review
- Sialosides Containing 7-ACS infectious diseases · 2023Article
- Microscale Quantification of the Inhibition of Neuraminidase Using Capillary Nanogel Electrophoresis.Analytical chemistry · 2022Article
- Desialylation of Atg5 by sialidase (Neu2) enhances autophagosome formation to induce anchorage-dependent cell death in ovarian cancer cells.Cell death discovery · 2021Article
- GBA3: a polymorphic pseudogene in humans that experienced repeated gene loss during mammalian evolution.Scientific reports · 2020Article
- Gut bacteria responding to dietary change encode sialidases that exhibit preference for red meat-associated carbohydrates.Nature microbiology · 2019Article
- 9-Azido-9-deoxy-2,3-difluorosialic Acid as a Subnanomolar Inhibitor against Bacterial Sialidases.The Journal of organic chemistry · 2019Article
- SnClBeilstein journal of organic chemistry · 2019Article
- Synthesis ofFrontiers in immunology · 2019Review
- Triazole-linked transition state analogs as selective inhibitors against V. cholerae sialidase.Bioorganic & medicinal chemistry · 2018Article
- Streptococcus pneumoniae Sialidase SpNanB-Catalyzed One-Pot Multienzyme (OPME) Synthesis of 2,7-Anhydro-Sialic Acids as Selective Sialidase Inhibitors.The Journal of organic chemistry · 2018Article
- α2-6-Neosialidase: A Sialyltransferase Mutant as a Sialyl Linkage-Specific Sialidase.ACS chemical biology · 2018Article
- A Diazido Mannose Analogue as a Chemoenzymatic Synthon for Synthesizing Di-N-acetyllegionaminic Acid-Containing Glycosides.Angewandte Chemie (International ed. in English) · 2018Article
- Sialidase-catalyzed one-pot multienzyme (OPME) synthesis of sialidase transition-state analogue inhibitors.ACS catalysis · 2018Article
- Chemoenzymatic synthesis of Neu5Ac9NAc-containing α2-3- and α2-6-linked sialosides and their use for sialidase substrate specificity studies.Carbohydrate research · 2017Article
- Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged α2-8-sialosides and high-throughput substrate specificity studies of α2-8-sialidases.Organic & biomolecular chemistry · 2016Article
- Pneumococcal Neuraminidase Substrates Identified through Comparative Proteomics Enabled by Chemoselective Labeling.Bioconjugate chemistry · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Aberrant expression of human sialidases has been shown to associate with various pathological conditions. Despite the effort in the sialidase inhibitor design, less attention has been paid to designing specific inhibitors against human sialidases and characterizing the substrate specificity of different sialidases regarding diverse terminal sialic acid forms and sialyl linkages. This is mainly due to the lack of sialoside probes and efficient screening methods, as well as limited access to human sialidases. A low cellular expression level of the human sialidase NEU2 hampers its functional and inhibitory studies. Here we report the successful cloning and expression of the human sialidase NEU2 in E. coli. About 11 mg of soluble active NEU2 was routinely obtained from 1 L of E. coli cell culture. Substrate specificity studies of the recombinant human NEU2 using twenty p-nitrophenol (pNP)-tagged α2-3- or α2-6-linked sialyl galactosides containing different terminal sialic acid forms including common N-acetylneuraminic acid (Neu5Ac), non-human N-glycolylneuraminic acid (Neu5Gc), 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid (Kdn), or their C5-derivatives in a microtiter plate-based high-throughput colorimetric assay identified a unique structural feature specifically recognized by the human NEU2 but not two bacterial sialidases. The results obtained from substrate specificity studies were used to guide the design of a sialidase inhibitor that was selective against human NEU2. The selectivity of the inhibitor was revealed by the comparison of sialidase crystal structures and inhibitor docking studies.
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