Affordable Access

Publisher Website

Carbohydrate microarrays reveal sulphation as a modulator of siglec binding

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
344
Issue
4
Identifiers
DOI: 10.1016/j.bbrc.2006.03.223
Keywords
  • Carbohydrate-Binding Proteins
  • Glycolipids
  • Carbohydrate–Protein Interactions
  • Immune System
  • Lectin-Type Receptors
  • Lewis X
  • Microarrays Of Oligosaccharide Probes
  • Neoglycolipids
  • Selectins
  • Siglecs
  • Sialylated Oligosaccharide Sequences
  • Sulphated Oligosaccharide Sequences

Abstract

Abstract Siglecs are receptors on cells of the immune, haemopoietic, and nervous systems that recognize sialyl-glycans with differing preferences for sialic acid linkage and oligosaccharide backbone sequence. We investigate here siglec binding using microarrays of Lewis x (Le x)- and 3′-sialyl-Le x-related probes with different sulphation patterns. These include sulphation at position 3 of the terminal galactose of Le x, position 6 of the galactose of Le x and sialyl-Le x, position 6 of N-acetylglucosamine of Le x and sialyl-Le x, or both positions of sialyl-Le x. Recombinant soluble forms of five siglecs have been investigated: human Siglec-7, -8, -9, and murine Siglec-F and CD22 (Siglec-2). Each siglec has a different binding pattern. Unlike two C-type lectins of leukocytes, L-selectin and Langerin, which also bind to sulphated analogues of sialyl-Le x, the siglecs do not give detectable binding signals with sulphated analogues that are lacking sialic acid. The sulphate groups modulate, however, positively or negatively the siglec binding intensities to the sialyl-Le x sequence.

There are no comments yet on this publication. Be the first to share your thoughts.