ArticleDevelopmental and comparative immunology2014
A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria.
Article in Developmental and comparative immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 35 citations in OpenAlex.
- Vitamin DFish physiology and biochemistry · 2017Trial
- Novel Lectins fromACS omega · 2025Article
- New l-Rhamnose-Binding Lectin from the BivalveMarine drugs · 2023Article
- New Data on the Rhamnose-Binding Lectin from the Colonial AscidianMarine drugs · 2023Article
- An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications.Marine drugs · 2022Review
- Bacterial glycobiology: rhamnose-containing cell wall polysaccharides in Gram-positive bacteria.FEMS microbiology reviews · 2016Review
- Comprehensive Analysis of a Vibrio parahaemolyticus Strain Extracellular Serine Protease VpSP37.PloS one · 2015Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is present as a physiological homotetramer. DlRBL subunit transcripts revealed an open reading frame encoding 212 amino acid residues that included two tandemly-arrayed carbohydrate-recognition domains, and an 18-residue signal sequence at the N-terminus. The deduced size of 24.1 kDa for the mature protein was in good agreement with the subunit size of the isolated lectin. Binding activity of DlRBL for rabbit erythrocytes could be inhibited in the presence of rhamnose or galactose, did not require calcium, and was optimal at around 20°C and within the pH 6.5-8.0 range. DlRBL agglutinated Gram positive and Gram negative bacteria, and exposure of formalin-killed Escherichia coli to DlRBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls. Taken together, the results suggest that plasma DlRBL may play a role in immune recognition of microbial pathogens and facilitate their clearance by phagocytosis.
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