Evolution and Immune Function of Fish Lectins

Abstract

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An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

“…Nevertheless, their roles in aquatic animals (i.e., reproduction, defense against pathogenic microbes (immunity), polyspermy block, morphogenesis and embryogenesis) are well studied [ 15 , 16 , 17 ]. The major classes of lectins identified in marine animals are C-type lectins (CTLs), F-type lectins (FTLs), X-type lectins (XTL), galectins (formerly S-type lectins), and pentraxins (P-type lectins) [ 6 , 18 ]. Typically, all lectins mentioned above present similar CRD sequences, the position of disulfide bonds, and calcium ion (Ca 2+ ) binding sites.…”

“…They act as opsonins that facilitate agglutination of bacteria (typically Gram-negative) and phagocytotic activity of peritoneal macrophages against pathogens (i.e., E. coli , among others). In summary, RBLs are involved in the detection and phagocytic elimination of microbial pathogens in blood by binding the pathogens to the leukocyte surface [ 6 ]. Multiple l -rhamnose-binding isolectins with various molecular and configurational features have previously been reported in fish eggs and serum.…”

“…Extraction of lectins under reducing and non-reducing conditions yielded proteins with different molecular weights, 34 kDa and 30 kDa, respectively, which may be ascribed to the shrinkage effect induced by the interchain disulfide bridges [ 52 ]. FBLs exert potent antibacterial activity and trigger immune defense in response to pathogens in the intestinal mucus and blood of fish [ 6 , 51 ]. Additionally, they can express phagocytic activity against E. coli , for example, and the FBLs isolated from hepatocytes and intestinal cells of European eel ( Anguilla anguilla ) and striped bass ( Morone saxatilis ), respectively [ 57 ].…”

“…In addition, lectins are classified based on their amino acid sequences, structural homology, and cation requirements. For instance, lectins from marine organisms are generally classified as C-type lectins (CTLs), galectins (formerly called S-type lectins), F-type lectins (FTLs), X-type lectins (XTLs), I-type lectins (ITL), P-type lectins, pentraxins, ricin-type, lily-type lectins, and mannan-binding lectins [ 5 , 6 ]. They are further categorized according to their sugar-binding preferences, into rhamnose-binding lectins (RBL), fucose-binding lectins (FBL), galactose-binding lectins (GBL), GlcNAc-specific lectins, mannan-binding lectins (MBL), and GalNAc-specific lectins.…”

F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity

“…Although teleost fish express most components of typical mammalian adaptive immune responses, it is well-established that a significant portion of their immediate response against infectious challenges is carried out by innate immune defence mechanisms. Accordingly, during the past few years, interest in the structural-functional aspects of fish innate immune responses, particularly lectins, toll-like receptors and complements, has grown at an exponential rate (Magnadóttir, 2006;Vasta et al, 2011;Cammarata et al, 2016;Elumalai et al, 2019;Sahoo, 2020). Lectins are carbohydrate-binding proteins present in essentially all living organisms and are involved in immune responses as well as in other biological processes.…”