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Biochem Biophys Res Commun. 2011 Nov 18;415(2):421-5. doi: 10.1016/j.bbrc.2011.10.085. Epub 2011 Oct 21.

Identification of a second catalytically active trans-sialidase in Trypanosoma brucei.

Author information

1
Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.

Abstract

The procyclic stage of Trypanosoma brucei is covered by glycosylphosphatidylinositol (GPI)-anchored surface proteins called procyclins. The procyclin GPI anchor contains a side chain of N-acetyllactosamine repeats terminated by sialic acids. Sialic acid modification is mediated by trans-sialidases expressed on the parasite's cell surface. Previous studies suggested the presence of more than one active trans-sialidases, but only one has so far been reported. Here we cloned and examined enzyme activities of four additional trans-sialidase homologs, and show that one of them, Tb927.8.7350, encodes another active trans-sialidase, designated as TbSA C2. In an in vitro assay, TbSA C2 utilized α2-3 sialyllactose as a donor, and produced an α2-3-sialylated product, suggesting that it is an α2-3 trans-sialidase. We suggest that TbSA C2 plays a role in the sialic acid modification of the trypanosome cell surface.

PMID:
22040733
DOI:
10.1016/j.bbrc.2011.10.085
[Indexed for MEDLINE]

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