ArticleThe Journal of biological chemistry2012
Directed evolution of lectins with sugar-binding specificity for 6-sulfo-galactose.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Engineered OAA lectins as selective and sensitive high mannose glycan targeting tools.bioRxiv : the preprint server for biology · 2026Article
- Editor's Choice Protein engineering strategies to develop lectins by design.Glycobiology · 2025Review
- Computationally guided conversion of the specificity of E-selectin to mimic that of Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Glioblastoma Extracellular Vesicle-Specific Peptides Inhibit EV-Induced Neuronal Cytotoxicity.International journal of molecular sciences · 2022Article
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- LectinOracle: A Generalizable Deep Learning Model for Lectin-Glycan Binding Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Evaluation of Glycan-Binding Specificity by Glycoconjugate Microarray with an Evanescent-Field Fluorescence Detection System.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Strategies and Tactics for the Development of Selective Glycan-Binding Proteins.ACS chemical biology · 2021Review
- Comprehensive analysis of glycosphingolipid glycans by lectin microarrays and MALDI-TOF mass spectrometry.Nature protocols · 2021Article
- Directed evolution in mammalian cells.Nature methods · 2021Review
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- Functional reprogramming ofThe Journal of biological chemistry · 2020Article
- Application of Lectin Microarrays for Biomarker Discovery.ChemistryOpen · 2020Review
- Lectin engineering: the possible and the actual.Interface focus · 2019Review
- Microscopy examination of red blood and yeast cell agglutination induced by bacterial lectins.PloS one · 2019Article
- Deciphering Protein Glycosylation by Computational Integration of On-chip Profiling, Glycan-array Data, and Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- Computational and biological characterization of fusion proteins of two insecticidal proteins for control of insect pests.Scientific reports · 2018Article
- Ribosome Inactivating Proteins from Rosaceae.Molecules (Basel, Switzerland) · 2016Article
- Mammalian Cell Surface Display as a Novel Method for Developing Engineered Lectins with Novel Characteristics.Biomolecules · 2015Article
- Lectin engineering, a molecular evolutionary approach to expanding the lectin utilities.Molecules (Basel, Switzerland) · 2015Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
6-sulfo-galactose (6S-Gal) is a prevalent motif observed in highly sulfated keratan sulfate, which is closely associated with the glioblastoma malignancy while acting as a critical determinant for endogenous lectins. However, facile detection of this unique glycoepitope is greatly hampered because of a lack of appropriate probes. We have previously reported tailoring an α2-6-linked sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein, EW29Ch, by a reinforced ribosome display system following an error-prone PCR. In this study, we challenged the creation of novel lectins to recognize 6S-Gal-terminated glycans by incorporating a high-throughput screening system with a glycoconjugate microarray. After two rounds of selection procedures, 20 mutants were obtained and 12 were then successfully expressed in Escherichia coli, 8 of which showed a significant affinity for 6'-Sulfo-LN (6-O-sulfo-Galβ1-4GlcNAc), which the parental EW29Ch lacked. Analysis of two representative mutants by frontal affinity chromatography revealed a substantial affinity (K(d) ∼3 μm) for a 6S-Gal-terminated glycan. On the basis of the observation that all eight mutants have a common mutation at Glu-20 to Lys, site-directed mutagenesis experiments were performed focusing on this aspect. The results clearly indicated that the E20K mutation is necessary and sufficient to acquire the specificity for 6S-Gal. We also confirmed a difference in binding between E20K and EW29Ch to CHO cells, in which enzymes to catalyze the synthesis of 6S-Gal were overexpressed. The results clearly demonstrate that these mutants have potential to distinguish between cells containing different amounts of 6S-Gal-terminated glycans. This new technology will be used to provide novel tools essential for sulfoglycomics.
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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.