F-type lectin from the sea bass (Dicentrarchus labrax): purification, cDNA cloning, tissue expression and localization, and opsonic activity.

6533b834fe1ef96bd129dff9

RESEARCH PRODUCT

F-type lectin from the sea bass (Dicentrarchus labrax): purification, cDNA cloning, tissue expression and localization, and opsonic activity.

Daniela Parrinello Gerardo R. Vasta Maria Giovanna Parisi Aiti Vizzini Giuseppina Salerno Gigliola Benenati Matteo Cammarata Mirella Vazzana

subject

food.ingredient DNA Complementary Immunoblotting Aquatic Science Chromatography Affinity Bass (fish)F-type lectin; Dicentrarchus labrax;teleost;emaggluthinins opsonin food Phagocytosis Opsonin Proteins Complementary DNA Lectins Environmental Chemistry Animals Dicentrarchus labrax RNA Messenger Sea bass Cloning Molecular Opsonin emaggluthinins opsonin Phylogeny teleost biology Base Sequence Lectin General Medicine Opsonin Proteins biology.organism_classification Molecular biology Gene Expression Regulation Immunology biology.protein Macrophages Peritoneal F lectin sea bass inflammation Dicentrarchus Bass Electrophoresis Polyacrylamide Gel Sequence motif F-type lectin

description

Recently described biochemical and structural aspects of fucose-binding lectins from the European eel (Anguilla anguilla) and striped bass (Morone saxatilis) led to the identification of a novel lectin family ("F-type" lectins) characterized by a unique sequence motif and a characteristic structural fold. The F-type fold is shared not only with other members of this lectin family, but also with apparently unrelated proteins ranging from prokaryotes to vertebrates. Here we describe the purification, biochemical and molecular properties, and the opsonic activity of an F-type lectin (DlFBL) isolated from sea bass (Dicentrarchus labrax) serum. DlFBL exhibits two tandemly arranged carbohydrate-recognition domains that display the F-type sequence motif. In situ hybridization and immunohistochemical analysis revealed that DlFBL is specifically expressed and localized in hepatocytes and intestinal cells. Exposure of formalin-killed Escherichia coli to DlFBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls, suggesting that DlFBL may function as an opsonin in plasma and intestinal mucus.

year	journal	country	edition	language
2009-08-01	Fishshellfish immunology

10.1016/j.fsi.2009.01.004 https://pubmed.ncbi.nlm.nih.gov/19162197