ArticleThe Journal of biological chemistry2014
Structural basis for multiple sugar recognition of Jacalin-related human ZG16p lectin.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- ZG16B: A key regulator of tumor progression and immune microenvironment modulation in cancer (Review).International journal of molecular medicine · 2026Review
- Comprehensive bioinformatics analysis was used to identify and verify differentially expressed genes in targeted therapy of colon cancer.Scientific reports · 2025Article
- Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024Review
- Glycosaminoglycan microarrays for studying glycosaminoglycan-protein systems.Carbohydrate polymers · 2024Review
- A jacalin-related lectin domain-containing lipase from chestnut (Current research in food science · 2022Article
- Conformational switches and redox properties of the colon cancer-associated human lectin ZG16.The FEBS journal · 2021Article
- The role of Jacalin-related lectin gene AOL_s00083g511 in the development and pathogenicity of the nematophagous fungus Arthrobotrys oligospora.Journal of microbiology (Seoul, Korea) · 2021Article
- 3D Structural View of Pathogen Recognition by Mammalian Lectin Receptors.Frontiers in molecular biosciences · 2021Review
- A molecularly engineered antiviral banana lectin inhibits fusion and is efficacious against influenza virus infection in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Substrate-Dependent Fermentation of Bamboo in Giant Panda Gut Microbiomes: Leaf Primarily to Ethanol and Pith to Lactate.Frontiers in microbiology · 2020Article
- Crystal structure of a cytocidal protein from lamprey and its mechanism of action in the selective killing of cancer cells.Cell communication and signaling : CCS · 2019Article
- Structure-function characterization of an insecticidal protein GNIP1Aa, a member of an MACPF and β-tripod families.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Messages From the Past: New Insights in Plant Lectin Evolution.Frontiers in plant science · 2019Article
- Recognition of microbial glycans by soluble human lectins.Current opinion in structural biology · 2017Review
- The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Structure (London, England : 1993) · 2017Article
- A pore-forming protein implements VLR-activated complement cytotoxicity in lamprey.Cell discovery · 2017Article
- Gram-positive bacteria are held at a distance in the colon mucus by the lectin-like protein ZG16.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.EMBO reports · 2016Article
- Defining the Interaction of Human Soluble Lectin ZG16p and Mycobacterial Phosphatidylinositol Mannosides.Chembiochem : a European journal of chemical biology · 2015Article
- Protein-carbohydrate interactions as part of plant defense and animal immunity.Molecules (Basel, Switzerland) · 2015Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
ZG16p is a soluble mammalian lectin, the first to be described with a Jacalin-related β-prism-fold. ZG16p has been reported to bind both to glycosaminoglycans and mannose. To determine the structural basis of the multiple sugar-binding properties, we conducted glycan microarray analyses of human ZG16p. We observed that ZG16p preferentially binds to α-mannose-terminating short glycans such as Ser/Thr-linked O-mannose, but not to high mannose-type N-glycans. Among sulfated glycosaminoglycan oligomers examined, chondroitin sulfate B and heparin oligosaccharides showed significant binding. Crystallographic studies of human ZG16p lectin in the presence of selected ligands revealed the mechanism of multiple sugar recognition. Manα1-3Man and Glcβ1-3Glc bound in different orientations: the nonreducing end of the former and the reducing end of the latter fitted in the canonical shallow mannose binding pocket. Solution NMR analysis using (15)N-labeled ZG16p defined the heparin-binding region, which is on an adjacent flat surface of the protein. On-array competitive binding assays suggest that it is possible for ZG16p to bind simultaneously to both types of ligands. Recognition of a broad spectrum of ligands by ZG16p may account for the multiple functions of this lectin in the formation of zymogen granules via glycosaminoglycan binding, and in the recognition of pathogens in the digestive system through α-mannose-related recognition.
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