| dc.description.abstract | Glycoconjugates are very important compounds found in all domains of life. They are
not primary products of genetic code like other structural biomolecules such as proteins
and nucleic acids. They are product of glycosylation, i.e. addition of sugars to target
molecules like proteins and lipids. Sialylated glycoconjugates are synthesized when
sialic acids from donor molecules are transferred to the target molecules by
sialyltransferase. These sialylated glycoconjugates are involved primarily in mediating
the cell-cell interaction. Due to their prominent position on cell surface they act as a
recognition site for various receptors as well as pathogens. Until now, most of the
research about sialic acids and their functions is limited to deuterostomes. The
information about the biosynthesis of sialic acid is incomplete and not well studied in
protostomes. In Drosophila, the GNE enzyme that catalyzes the first two steps of sialic
acid synthesis in vertebrates, is absent but the sialylated products can be detected in
small quantities. I studied if an isozyme of GNE is present in Drosophila which catalyzes
the rate limiting reaction of the glycosylation pathway.
iv
The results from immunoassay and western blot suggest that recombinant protein is
being synthesized in the cytosol. At this moment, I am balancing the transgenic flies
which will be tested for in vivo expression of GNE enzyme. I will perform physical tests
to check for ectopic expression in these transgenic flies. | en |
