| dc.description.abstract | Galectins represent a group of proteins that bind β-galactosyl-containing glycoconjugates and share primary structural homology in their carbohydrate recognition domains. In mammals, galectins contribute to cell-cell interactions, cell surface signaling, regulation in immune responses, and embryo development. With little still known about the lectin-ligand associations concerning galectin, the Galectin-1 and galectin homologue in Drosophila melanogaster would make Drosophila a good model system for studying gelectin interactions. A novel Drosophila mutant with a deletion of both Galectin-1 and its homologue may serve to be important in analyzing phenotypes in the study of galectin functions. Several crosses were carried out using FLP mediated mutagenesis while following curly wings and bristle phenotypic markers. DNA extraction, PCR purification, and genomic sequencing were carried out on the last cross’s final product. Further experiments to remove an unnecessary bristle marker and cross the novel mutant with an L14 balancer stock are underway in order to investigate the lethality of the galectin deletion through Drosophila development. | en |
