Comparison of Two Major Classes of Glycan-Binding Proteins

Maureen E Taylor; Kurt Drickamer; Anne Imberty; Yvette van Kooyk; Ronald L Schnaar; Marilynn E Etzler; Ajit Varki

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Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology [Internet]. 4th edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022.

Essentials of Glycobiology [Internet]. 4th edition.

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Online Appendix 28AComparison of Two Major Classes of Glycan-Binding Proteins

Maureen E Taylor, Kurt Drickamer, Anne Imberty, Yvette van Kooyk, Ronald L Schnaar, Marilynn E Etzler, and Ajit Varki.

Table 1

Features	Lectins^a	Glycosaminoglycan-binding proteins^b
Shared evolutionary origins	yes (within each group)	no
Shared structural features	yes (within each group)	no
Defining amino acid residues involved in binding	often typical for each group	patch of basic amino acid residues
Type of glycans recognized	N-glycans, O-glycans, glycosphingolipids (a few also recognize sulfated glycosaminoglycans)	different types of sulfated glycosaminoglycans
Location of cognate residues within glycans	typically in sequences at outer ends of glycan chains	typically in sequences internal to an extended sulfated glycosaminoglycan chain
Specificity for glycans recognized	stereospecificity high for specific glycan structures	often recognize a range of related sulfated glycosaminoglycan structures
Single-site binding affinity	often low; high avidity generated by multivalency	often moderate to high
Valency of binding sites	multivalency common (either within native structure or by clustering)	often monovalent
Subgroups	C-type lectins, galectins, P-type lectins, I-type lectins, L-type lectins, R-type lectins, etc.	heparan sulfate–binding proteins, chondroitin sulfate–binding proteins, dermatan sulfate–binding proteins
Types of glycans recognized within each group	can be similar (e.g., galectins) or variable (e.g., C-type lectins)	classification itself is based on type of glycosaminoglycan chain recognized

: Modified from Varki A, Angata T. 2006. Glycobiology 16: 1R–27R.
^a: There are other animal proteins that recognize glycans in a lectin-like manner and do not appear to fall into one of the well-recognized classes (e.g., various cytokines).
^b: Hyaluronan (HA)-binding proteins (hyaloadherins) fall in between these two classes. On the one hand, some (but not all) of the hyaloadherins have shared evolutionary origins. On the other hand, recognition involves internal regions of HA, which is a nonsulfated glycosaminoglycan.

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Taylor ME, Drickamer K, Imberty A, et al. Comparison of Two Major Classes of Glycan-Binding Proteins. In: Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology [Internet]. 4th edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022. Online Appendix 28A.