Disease relevance of lectin

• Database searches revealed high levels of similarity with beta-galactoside-binding lectin-like proteins (Ga1BPs or galectins) from Caenorhabditis elegans and Onchocerca volvulus [1].
• The whole molecule (LEC-1), the N-terminal lectin domain (Nh), and the C-terminal lectin domain (Ch) were expressed in Escherichia coli, purified, and immobilized on HiTrap gel agarose columns, and the extent of retardation of various sugars by the columns was measured [2].
• Using the lectin wheat germ agglutinin as a probe, we show that the matrix on C. elegans contains carbohydrate produced by Yersinia [3].

High impact information on lectin

• Like latex beads, these new lectin receptors move continuously over the pseudopod surface to the cell body-pseudopod junction where they are probably internalized [4].
• Together with the observation that fluorescent phospholipids are cleared from the pseudopod of developing spermatozoa at the same rate as lectin receptors (25), these results show that there is bulk membrane flow over the pseudopod with assembly at the tip and apparent disassembly at the base [4].
• The approach, termed isotope-coded glycosylation-site-specific tagging (IGOT), is based on the lectin column-mediated affinity capture of a set of glycopeptides generated by tryptic digestion of protein mixtures, followed by peptide-N-glycosidase-mediated incorporation of a stable isotope tag, 18O, specifically into the N-glycosylation site [5].
• Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. Detailed analysis by an improved frontal affinity chromatography method [2].
• The purified 16-kDa lectin was found to exist as a dimer (approximately 30 kDa) and showed hemagglutinating activity toward trypsinized rabbit erythrocytes, which was inhibited by lactose [6].

Biological context of lectin

• Mutations in these genes fall into two phenotypic classes: srf-2, -3, -5 mutants are grossly wild-type, except for their lectin-binding phenotype; srf-4, -8, -9 mutants have a suite of defects, including uncoordinated movement, abnormal egg laying, and defective copulatory bursae morphogenesis [7].
• A recombinant form of this lectin induced symbiont aggregation in seawater and was able to compete with the native lectin for symbiont binding in vivo [8].
• Glycosylation differences were also detected by blotting nematode homogenates with the lectin wheat germ agglutinin (WGA), WGA was also able to differentiate between G. rostochiensis which gave 2 bands at 130 kDa and 110 kDa, and G. pallida which produced 2 bands present at 120 kDa and 110 kDa [9].
• Caenorhabditis elegans: lectin-mediated modification of chemotaxis [10].
• The protein is 72% identical in amino acid sequence and shares symmetrical two-domain structure with L-36, a lectin of unknown function from rat intestine, indicating that the 37-kDa protein is the porcine form of L-36 [11].

Anatomical context of lectin

• Galectin-3 is a member of a family of lectin-binding proteins produced by many different types of immune cells, including macrophages [12].
• The findings suggest that the lectin function may be involved in the assembly of adherens junctions [11].
• LL35 was initially isolated from membranes of the leech CNS; however, large amounts of this lectin were also extracted from the rest of the leech [13].
• The developmentally regulated distribution of LL35 in epithelial cells, neurons, and CNS muscles suggests a multifunctional role for this lectin with respect to these different cell types [13].
• Three surface polypeptides bound 125I-labeled WGA, and binding of WGA to hemocyte surface polypeptides was successfully inhibited by the incubation of cells with the lectin and its competing sugar [14].

Associations of lectin with chemical compounds

• Here, we identify a novel Ca(2+)-dependent mannose-specific lectin that was exclusively secreted onto the posterior, bacterium-associated region of L. oneistus cuticle [8].
• Staining of egg mixtures with fluorescein-labelled peanut agglutinin showed that the lectin correctly identified the percentage of H. contortus eggs present [15].
• Both TES-120 and TES-400 components are resistant to tryptic or peptic cleavage, bind to Helix pomatia lectin and stain with periodic acid-Schiff, yet unlike TES-120, TES-400 does not incorporate radioactive methionine nor can it be stained by silver stain techniques [16].
• Treatment of male T. colubriformis with the lectin Lens culinaris agglutinin (LcA) reduced the feeding by helminths that was stimulated by histamine and the male's response to their female's pheromone, based on in vitro assays [17].
• Expression of the C-terminal domain of the pig lectin in bacteria yields a lectin which binds lactosyl-Sepharose, and binding is inhibited by lactose [11].

Other interactions of lectin

• The subsequent study revealed that the 32-kDa lectin is a member of the galectin family [6].
• Western- and lectin-blotting of the shed coat material demonstrated 2 prominent entities; a 90 kDa glycoprotein, which bound Datura stramonium agglutinin and was resistant to N- and O-glycanase treatment and a 47-60 kDa set of protein(s) [18].

Analytical, diagnostic and therapeutic context of lectin

• Native TES-32 acted as a functional lectin in affinity chromatography [19].

References