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Issue 21, 2015
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Heparan sulfate phage display antibodies recognise epitopes defined by a combination of sugar sequence and cation binding

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Abstract

Phage display antibodies are widely used to follow heparan sulfate (HS) expression in tissues and cells. We demonstrate by ELISA, that cations alter phage display antibody binding profiles to HS and this is mediated by changes in polysaccharide conformation, demonstrated by circular dichroism spectroscopy. Native HS structures, expressed on the cell surfaces of neuroblastoma and fibroblast cells, also exhibited altered antibody binding profiles following exposure to low mM concentrations of these cations. Phage display antibodies recognise conformationally-defined HS epitopes, rather than sequence alone, as has been assumed, and resemble proteins in being sensitive to changes in both charge distribution and conformation following binding of cations to HS polysaccharides.

Graphical abstract: Heparan sulfate phage display antibodies recognise epitopes defined by a combination of sugar sequence and cation binding

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Article information


Submitted
20 Mar 2015
Accepted
28 Apr 2015
First published
28 Apr 2015

Org. Biomol. Chem., 2015,13, 6066-6072
Article type
Paper
Author version available

Heparan sulfate phage display antibodies recognise epitopes defined by a combination of sugar sequence and cation binding

V. Solari, T. R. Rudd, S. E. Guimond, A. K. Powell, J. E. Turnbull and E. A. Yates, Org. Biomol. Chem., 2015, 13, 6066
DOI: 10.1039/C5OB00564G

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