Saccharide binding by intelectins
•Human intelectin-1 binds to saccharides lacking an acyclic 1,2-diol and it binds to Sepharose CL-6B with high affinity.•Intelectin-1 binds to 2-C-hydroxymethyl-D-ribose, talose, idose, altrose, and sorbitol.•Halocynthia roretzii intelectin binds to melibiose, sialic acid and glycerol.•Xenopus laevi...
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Published in | International journal of biological macromolecules Vol. 108; pp. 1010 - 1016 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.03.2018
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Subjects | |
Online Access | Get full text |
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Summary: | •Human intelectin-1 binds to saccharides lacking an acyclic 1,2-diol and it binds to Sepharose CL-6B with high affinity.•Intelectin-1 binds to 2-C-hydroxymethyl-D-ribose, talose, idose, altrose, and sorbitol.•Halocynthia roretzii intelectin binds to melibiose, sialic acid and glycerol.•Xenopus laevis intelectin binds to altrose, melibiose and sialic acid.•Saccharide binding modulates binding of Intelectin-1 to lactoferrin and vice versa.
This communication probes ligand binding by human Intelectin-1 with several saccharides. Human Intelectin-1 was previously reported to bind to microbial glycans via ribofuranoside or galactofuranoside residues, whereas subsequently, a crystal structure of ligand bound hITLN1 indicated that hITLN1 does not bind to ribofuranoside but distinguishes between microbial and human glycans through a glycan motif – a terminal, acyclic 1,2-diol, which is present on galactofuranose and other microbial saccharides. Here, we demonstrate that besides glycerol and glycerol derivatives (which have an acyclic 1,2-diol), and 2-deoxy-d-galactose, d-ribose and 2-deoxy-d-ribose, which have been previously reported as human Intelectin-1 ligands, 2-C-hydroxymethyl-d-ribose, d-talose, d-idose, d-altrose and sorbitol also elute human Intelectin-1 from Sepharose CL-6B. Interestingly, Sepharose, 2-deoxy-d-galactose (in its pyranose form), 2-C-hydroxymethyl-d-ribose, d-ribose and 2-deoxy d-ribose lack a terminal, acyclic 1,2-diol. We discuss the implications of these observations and rationalize the discrepancies in the apparent affinity of saccharide ligands for hITLN1 with different assay formats. We also report the distinct saccharide binding profiles of the hITLN1 homologues, HaloITLN and XL35ITLN, and demonstrate that hITLN1 binding to a saccharide ligand may modulate binding to its protein ligand, lactoferrin and vice versa. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0141-8130 1879-0003 |
DOI: | 10.1016/j.ijbiomac.2017.11.007 |