ArticleThe Journal of biological chemistry2013
Recognition of the Thomsen-Friedenreich pancarcinoma carbohydrate antigen by a lamprey variable lymphocyte receptor.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Editor's Choice Protein engineering strategies to develop lectins by design.Glycobiology · 2025Review
- Phage Display Reveals VLRB-Mediated Recognition of Minimal Tumor Glycan Antigen Sialyl-Tn.Current issues in molecular biology · 2025Article
- Article
- Identification of lamprey variable lymphocyte receptors that target the brain vasculature.Scientific reports · 2022Article
- Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Lamprey Variable Lymphocyte Receptor Monoclonal Antibodies for Whole-Cell Surface Antigens.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Strategies and Tactics for the Development of Selective Glycan-Binding Proteins.ACS chemical biology · 2021Review
- Novel lamprey antibody recognizes terminal sulfated galactose epitopes on mammalian glycoproteins.Communications biology · 2021Article
- The immune system of jawless vertebrates: insights into the prototype of the adaptive immune system.Immunogenetics · 2021Review
- Article
- Development of smart anti-glycan reagents using immunized lampreys.Communications biology · 2020Article
- Guidelines for the use of flow cytometry and cell sorting in immunological studies (second edition).European journal of immunology · 2019Article
- Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.Frontiers in chemistry · 2019Review
- The variable lymphocyte receptor as an antibody alternative.Current opinion in biotechnology · 2018Review
- VLR Recognition of TLR5 Expands the Molecular Characterization of Protein Antigen Binding by Non-Ig-based Antibodies.Journal of molecular biology · 2018Article
- Crystal structure of an anti-idiotype variable lymphocyte receptor.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Structural Insights into VLR Fine Specificity for Blood Group Carbohydrates.Structure (London, England : 1993) · 2017Article
- Biochemical Regulatory Features of Activation-Induced Cytidine Deaminase Remain Conserved from Lampreys to Humans.Molecular and cellular biology · 2017Article
- Leucine-rich-repeat-containing variable lymphocyte receptors as modules to target plant-expressed proteins.Plant methods · 2017Article
- Identification and characterisation of the immune response properties of Lampetra japonica BLNK.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 2 countries.
Funding
Abstract
Variable lymphocyte receptors (VLRs) are leucine-rich repeat proteins that mediate adaptive immunity in jawless vertebrates. VLRs were recently shown to recognize glycans, such as the tumor-associated Thomsen-Friedenreich antigen (TFα; Galβ1-3GalNAcα), with a selectivity rivaling or exceeding that of lectins and antibodies. To understand the basis for TFα recognition by one such VLR (VLRB.aGPA.23), we measured thermodynamic parameters for the binding interaction and determined the structure of the VLRB.aGPA.23-TFα complex to 2.2 Å resolution. In the structure, four tryptophan residues form a tight hydrophobic cage encasing the TFα disaccharide that completely excludes buried water molecules. This cage together with hydrogen bonding of sugar hydroxyls to polar side chains explains the exquisite selectivity of VLRB.aGPA.23. The topology of the glycan-binding site of VLRB.aGPA.23 differs markedly from those of lectins or antibodies, which typically consist of long, convex grooves for accommodating the oligosaccharide. Instead, the TFα disaccharide is sandwiched between a variable loop and the concave surface of the VLR formed by the β-strands of the leucine-rich repeat modules. Longer oligosaccharides are predicted to extend perpendicularly across the β-strands, requiring them to bend to match the concavity of the VLR solenoid.
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Registered trials
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.