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Issue 45, 2014
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Sialylation of lactosyl lipids in membrane microdomains by T. cruzi trans-sialidase

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Abstract

A synthetic perfluoroalkyl-tagged lactosyl glycolipid has been shown to form lipid microdomains in fluid phospholipid bilayers. When embedded in the membranes of phospholipid vesicles, this glycolipid was trans-sialylated by soluble T. cruzi trans-sialidase (TcTS) to give a perfluoroalkyl-tagged glycolipid that displayed the ganglioside GM3 epitope, with up to 35% trans-sialylation from fetuin after 18 h. Following sialylation, vesicles bearing this Neu5Ac(α2-3)Gal(β1-4)Glc sequence in their “glycocalyx” were recognised and agglomerated by the lectin M. amurensis leukoagglutinin. Monitoring TcTS-mediated trans-sialylation by HPLC over the first 6 h revealed that enzymatic transformation of bilayer-embedded substrate was much slower than that of a soluble lactosyl substrate. Furthermore, clustering of the lactose-capped glycolipid into “acceptor” microdomains did not increase the rate of sialic acid transfer from fetuin by soluble TcTS, instead producing slight inhibition.

Graphical abstract: Sialylation of lactosyl lipids in membrane microdomains by T. cruzi trans-sialidase

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Supplementary files

Article information


Submitted
29 Aug 2014
Accepted
25 Sep 2014
First published
25 Sep 2014

This article is Open Access

Org. Biomol. Chem., 2014,12, 9272-9278
Article type
Paper
Author version available

Sialylation of lactosyl lipids in membrane microdomains by T. cruzi trans-sialidase

G. T. Noble, F. L. Craven, M. D. Segarra-Maset, J. E. R. Martínez, R. Šardzík, S. L. Flitsch and S. J. Webb, Org. Biomol. Chem., 2014, 12, 9272
DOI: 10.1039/C4OB01852D

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