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Open AccessArticle

The Dramatic Modulatory Role of the 2'N Substitution of the Terminal Amino Hexose of Globotetraosylceramide in Determining Binding by Members of the Verotoxin Family

1
Program in Molecular Structure and Function, Research Institute, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, 686 Bay Street, Toronto, Ontario M5G 0A4, Canada
2
Laboratory Medicine & Pathobiology, University of Toronto, Toronto M5S 1A8, Canada
3
Department of Cell and Systems Biology, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada
4
Department of Biochemistry, University of Toronto, Toronto, M5S 1A8, Canada
*
Author to whom correspondence should be addressed.
Academic Editor: Mark Devlin Maloney
Chromatography 2015, 2(3), 529-544; https://doi.org/10.3390/chromatography2030529
Received: 27 April 2015 / Revised: 8 July 2015 / Accepted: 5 August 2015 / Published: 14 August 2015
(This article belongs to the Special Issue New Trends in Thin-Layer Chromatography)
Although globotetraosylceramide (Gb4) is only recognized by a single member of the verotoxin family namely, the pig edema disease toxin (VT2e), removal of the acetyl group from the terminal N-acetyl hexosamine of Gb4 to generate the free amino sugar containing species (aminoGb4) results in the generation of a glycolipid preferentially recognized by all members of the verotoxin family (i.e., VT1, VT2, VT2c, and VT2e). GT3, a site-specific mutant of VT2e, in which Gb4 recognition is lost but Gb3 binding is retained, also binds aminoGb4. We have now compared the binding of VT1, VT2, VT2e, and GT3 to a series of aminoGb4 derivatives using a TLC overlay technique. DimethylaminoGb4 is bound by VT1 and VT2 but not VT2e or GT3; formylaminoGb4 binds all toxins but poorly to VT2 and preferentially VT2e; trifluoroacetylaminoGb4 binds only VT2e and GT3; isopropylaminoGb4 binds VT1 and poorly to VT2; benzylaminoGb4 binds all four toxins. Thus, there is a marked distinction between the permissible amino substitutions for VT1 and VT2e binding. GT3 is a hybrid between these in that, according to the substitution, it behaves similarly either to VT1 or to VT2e. For each species, GT3 does not however, show a hybrid binding between that of VT1 and VT2e. Analysis of the binding as a function of pH shows opposite effects for VT1 and VT2e: decreased pH increases VT1, but decreases VT2e receptor glycolipid binding. View Full-Text
Keywords: shiga toxin receptor; globotetraosylceramide; amino substitution shiga toxin receptor; globotetraosylceramide; amino substitution
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Mylvaganam, M.; Binnington, B.; Budani, M.; Soltyk, A.M.; Lingwood, C.A. The Dramatic Modulatory Role of the 2'N Substitution of the Terminal Amino Hexose of Globotetraosylceramide in Determining Binding by Members of the Verotoxin Family. Chromatography 2015, 2, 529-544.

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