ArticleBiomolecules2015
Mammalian Cell Surface Display as a Novel Method for Developing Engineered Lectins with Novel Characteristics.
Article in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 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
- Engineering glycosyltransferases into glycan binding proteins using a mammalian surface display platform.Nature communications · 2025Article
- Construction of mouse cochlin mutants with different GAG-binding specificities and their use for immunohistochemistry.The Biochemical journal · 2023Article
- Article
- Strategies and Tactics for the Development of Selective Glycan-Binding Proteins.ACS chemical biology · 2021Review
- Lectin engineering: the possible and the actual.Interface focus · 2019Review
- Expression of Lectins in Heterologous Systems.International journal of molecular sciences · 2018Review
- Brief introduction of current technologies in isolation of broadly neutralizing HIV-1 antibodies.Virus research · 2018Review
- Biomolecular engineering for nanobio/bionanotechnology.Nano convergence · 2017Review
- Golgb1 regulates protein glycosylation and is crucial for mammalian palate development.Development (Cambridge, England) · 2016Article
- Mutated Leguminous Lectin Containing a Heparin-Binding like Motif in a Carbohydrate-Binding Loop Specifically Binds to Heparin.PloS one · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leguminous lectins have a conserved carbohydrate recognition site comprising four loops (A-D). Here, we randomly mutated the sequence and length of loops C and D of peanut agglutinin (PNA) and expressed the proteins on the surface of mouse green fluorescent protein (GFP)-reporter cells. Flow cytometry, limiting dilution, and cDNA cloning were used to screen for several mutated PNAs with distinct properties. The mutated PNA clones obtained using NeuAcα2-6(Galβ1-3)GalNAc as a ligand showed preference for NeuAcα2-6(Galβ1-3)GalNAc rather than non-sialylated Galβ1-3GlcNAc, whereas wild-type PNA binds to Galβ1-3GlcNAc but not sialylated Galβ1-3GalNAc. Sequence analyses revealed that for all of the glycan-reactive mutated PNA clones, (i) loop C was eight amino acids in length, (ii) loop D was identical to that of wild-type PNA, (iii) residue 127 was asparagine, (iv) residue 125 was tryptophan, and (v) residue 130 was hydrophobic tyrosine, phenylalanine, or histidine. The sugar-binding ability of wild-type PNA was increased nine-fold when Tyr125 was mutated to tryptophan, and that of mutated clone C was increased more than 30-fold after His130 was changed to tyrosine. These results provide an insight into the relationship between the amino acid sequences of the carbohydrate recognition site and sugar-binding abilities of leguminous lectins.
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Registered trials
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