Glycobiology, 2002, Vol. 12, No. 2 73-83
© 2002 Oxford University Press
Expression of a functional Drosophila melanogaster N-acetylneuraminic acid (Neu5Ac) phosphate synthase gene: evidence for endogenous sialic acid biosynthetic ability in insects
3Department of Biology, Temple University, Philadelphia, PA 19122, USA; 4Department of Chemical Engineering, Johns Hopkins University, Baltimore, MD 21218, USA; and 5Laboratory of Bacterial Toxins and Laboratory of Bacterial Polysaccharides, Food and Drug Administration, Bethesda, MD 20892, USA
In this study, we report the first cloning and characterization of a N-acetylneuraminic acid phosphate synthase gene from Drosophila melanogaster, an insect in the protostome lineage. The gene is ubiquitously expressed at all stages of Drosophila development and in Schneider cells. Similar to the human homologue, the gene encodes an enzyme with dual substrate specificity that can use either N-acetylmannosamine 6-phosphate or mannose 6-phosphate to generate phosphorylated forms of both the sialic acids, N-acetylneuraminic acid and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid, respectively, when expressed in either bacterial or baculoviral expression systems. The identification of a functional sialic acid synthase in Drosophila indicates that insects have the biosynthetic capability to produce sialic acids endogenously. Although sialylation is widely distributed in organisms of the deuterstome lineage, genetic evidence concerning the presence or absence of sialic acid metabolism in organisms of the protostome lineage has been lacking. Homology searches of the Drosophila genome identified putative orthologues of other genes required for sialylation of glycoconjugates.
1 These two authors contributed equally to the work.
2 To whom correspondence should be addressed
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