Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective

• Published in: Molecular & cellular proteomics Vol. 20; p. 100024
• Main Authors: West, Christopher M., Malzl, Daniel, Hykollari, Alba, Wilson, Iain B.H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2021; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biological Evolution; Evolution; glycome; Glycomics; Glycoproteins - metabolism; Glycosylation; glycosyltransferase; Humans; invertebrate; Polysaccharides - metabolism; Protein Processing, Post-Translational; Proteomics; protist; Review; GPI; GlcA; MALDI-TOF-MS; EGF; Neu5Ac; LacdiNAc; Neu5Gc; GT; GalNAc; RP-HPLC; TSR; PC; LECA; Galf; PE; glycosyltransferase; protist; SCF; Evolution; GlcNAc; invertebrate; glycome; HILIC
• ISSN: 1535-9476; 1535-9484
• DOI: 10.1074/mcp.R120.002263

Glycosylation is a highly diverse set of co- and posttranslational modifications of proteins. For mammalian glycoproteins, glycosylation is often site-, tissue-, and species-specific and diversified by microheterogeneity. Multitudinous biochemical, cellular, physiological, and organismic effects of their glycans have been revealed, either intrinsic to the carrier proteins or mediated by endogenous reader proteins with carbohydrate recognition domains. Furthermore, glycans frequently form the first line of access by or defense from foreign invaders, and new roles for nucleocytoplasmic glycosylation are blossoming. We now know enough to conclude that the same general principles apply in invertebrate animals and unicellular eukaryotes—different branches of which spawned the plants or fungi and animals. The two major driving forces for exploring the glycomes of invertebrates and protists are (i) to understand the biochemical basis of glycan-driven biology in these organisms, especially of pathogens, and (ii) to uncover the evolutionary relationships between glycans, their biosynthetic enzyme genes, and biological functions for new glycobiological insights. With an emphasis on emerging areas of protist glycobiology, here we offer an overview of glycan diversity and evolution, to promote future access to this treasure trove of glycobiological processes. [Display omitted] •Emerging evidence for evolution of eukaryotic protein glycans is summarized•Six common glycan–protein linkages are predicted in the last eukaryotic common ancestor•Protists and invertebrates exhibit diverse peripheral glycan modifications•Cytoplasmic glycosylation frequently occurs in protists This review article i) assesses the utility of current glycomic, glycoproteomic, and glycogenomic methods to characterize protein glycosylation in less-well-studied eukaryotes; ii) assembles a plausible evolutionary lineage of eukaryotic glycan–protein linkages from the last eukaryotic common ancestor through protists to multicellular plants, invertebrates, and vertebrates; and iii) highlights the diversity of peripheral glycan specializations and modifications with an emphasis on available information from diverse protist kingdoms and invertebrate animals.