Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry

Mol Cell Proteomics. 2015 Apr;14(4):974-88. doi: 10.1074/mcp.M115.048272. Epub 2015 Feb 10.

Abstract

Glucans are polymers of d-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes, including immunomodulation, anticancer activities, pathogen virulence, and plant cell-wall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a "glucome" microarray, the first sequence-defined glycome-scale microarray, using a "designer" approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. Negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear "homo" and "hetero" and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signaling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies / metabolism
  • Carbohydrate Sequence
  • Cell Adhesion Molecules / metabolism
  • Glucans / metabolism*
  • Immune System / metabolism
  • Lectins, C-Type / metabolism
  • Ligands
  • Mice
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism
  • Protein Array Analysis / methods*
  • Protein Binding
  • Proteome / metabolism*
  • Receptors, Cell Surface / metabolism
  • Reproducibility of Results
  • Signal Transduction
  • Spectrometry, Mass, Electrospray Ionization / methods*
  • Vaccines / immunology

Substances

  • Antibodies
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Glucans
  • Lectins, C-Type
  • Ligands
  • Oligosaccharides
  • Proteome
  • Receptors, Cell Surface
  • Vaccines
  • saccharide-binding proteins