Sweet spots in functional glycomics.
Information contained in the mammalian glycome is decoded by glycan-binding proteins (GBPs) that mediate diverse functions including host-pathogen interactions, cell trafficking and transmembrane signaling. Although information on the biological roles of GBPs is rapidly expanding, challenges remain in identifying the glycan ligands and their impact on GBP function. Protein-glycan interactions are typically low affinity, requiring multivalent interactions to achieve a biological effect. Though many glycoproteins can carry the glycan structure recognized by the GBP, other factors, such as recognition of protein epitopes and microdomain localization, may restrict which glycoproteins are functional ligands in situ. Recent advances in development of glycan arrays, synthesis of multivalent glycan ligands, bioengineering of cell-surface glycans and glycomics databases are providing new tools to identify the ligands of GBPs and to elucidate the mechanisms by which they participate in GBP function.
Paulson
James C
JC
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA. jpaulson@scripps.edu
Blixt
Ola
O
Collins
Brian E
BE
D001698:Biomedical Engineering; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D016208:Databases, Factual; D000939:Epitopes / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D008024:Ligands; D021962:Membrane Microdomains / Q000378:metabolism*; D046228:Microarray Analysis; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020543:Proteome; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology
D000939:Epitopes; D008024:Ligands; D011134:Polysaccharides; D020543:Proteome