Crystallization and Preliminary X-Ray Crystallographic Analysis of Galectin LEC-1 from Caenorhabditis elegans

Abstract

Galectin LEC-1 isolated from the nematode Caenorhabditis elegans was the first galectin found in invertebrates and also the first tandem-repeat-type galectin identified, containing two homologous carbohydrate-binding sites. This galectin is localized most abundantly in the adult cuticle and possibly plays a role in the formation of epidermal layers. We succeeded in crystallizing LEC-1 composed of 279 amino acids with a calculated molecular weight of 31,809 Da under two independent sets of conditions as a result of extensive screening. The crystals grown under one set of conditions belong to the triclinic space group P1, with unit-cell parameters a = 48.44, b = 52.13, c = 64.24 A, alpha = 108.73, beta= 91.39, and gamma = 98.45 degrees and two protein molecules per unit cell. The crystals grown under the other set of conditions which included lactose belong to the monoclinic space group P2(1), with unit-cell parameters a = 52.90, b = 47.01, c = 66.16 A, and beta= 113.30 degrees and one protein molecule per asymmetric unit.

Identification of Immunodominant Peptides from Gnathostoma binucleatum

“…This molecule has been identified in a free-living nematode (Caenorhabditis elegans). 30 Moreover, this molecule was also found in an array of parasitic nematodes such as B. malayi, 31 D. immitis, A. caninum, T. colubriformis, A. cantonensis, and Teladorsagia circumcincta. 8,[32][33][34] Galectin proteins show β-galactoside affinity, and they are structurally characterized by a carbohydrate recognition domain, which codes information for cell-to-cell and cell-to-extracellular matrix interactions; 35 they also mediate the invasion into host, and participate in maintaining infection and modulating the host immune response.…”