| Identification of a second catalytically active trans-sialidase in Trypanosoma brucei. | |
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MedLine Citation:
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PMID: 22040733 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Fumiki Nakatani; Yasu S Morita; Hisashi Ashida; Kisaburo Nagamune; Yusuke Maeda; Taroh Kinoshita |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-21 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: - ISSN: 1090-2104 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-11-1 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
Affiliation:
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Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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