Sialic acid O-acetylation: From biosynthesis to roles in health and disease
Autor: | Thomas J. Boltje, Heleen de Jong, Sam J. Moons, Eline A. Visser, Suzanne B. P. E. Timmermans, Christian Büll |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
SOAT sialic acid O-acetyl transferase Biochemistry GBP glycan-binding protein chemistry.chemical_compound IA/B/C/DV Influenza A/B/C/D virus KDN 2-keto-3-deoxynononic acid N-Glycolylneuraminic acid S protein spike protein Disease SIAE sialic acid O-acetyl esterase SDAV sialodacryoadenitis virus sialic acid O-acetyl transferases (SOATs) biology EHEC enterohemorrhagic Escherichia coli Glycobiology BCoV bovine coronavirus CMP cytidine 5′-monophosphate Acetylation MERS-CoV Middle East respiratory syndrome coronavirus MHV-S murine hepatitis virus strain S NA neuraminidase CPS capsular polysaccharides O-Ac O-acetyl Glycan HE hemagglutinin esterase protein O-acetylation SARS-CoV severe acute respiratory syndrome coronavirus Hemagglutinin (influenza) Synthetic Organic Chemistry Siglec sialic acid-binding immunoglobulin-like lectin 03 medical and health sciences glycan modifications SDG 3 - Good Health and Well-being glycobiology Acetyltransferases Polysaccharides Sia sialic acid NPL neuraminic acid pyruvate-lyase Animals Humans Molecular Biology Ac-CoA acetyl-coenzyme A Glycoproteins 030102 biochemistry & molecular biology MUC mucin JBC Reviews HEF hemagglutinin esterase fusion protein SIGLEC Cell Biology ALL acute lymphoblastic leukemia Neu5Gc N-glycolylneuraminic acid N-Acetylneuraminic Acid CASD1 capsule structure1 domain containing 1 Neu5Ac N-acetylneuraminic acid Sialic acid Biosynthetic Pathways carbohydrates (lipids) 030104 developmental biology chemistry influenza C/D virus biology.protein sialic acid O-acetyl esterases (SIAEs) CMAH CMP-Neu5Ac hydroxylase sLex sialyl-Lewisx antigen Neuraminidase N-Acetylneuraminic acid Carboxylic Ester Hydrolases sialic acids HA hemagglutinin |
Zdroj: | The Journal of Biological Chemistry Journal of Biological Chemistry, 297, 1-19 Journal of Biological Chemistry, 297, 2, pp. 1-19 Visser, E A, Moons, S J, Timmermans, S B P E, de Jong, H, Boltje, T J & Büll, C 2021, ' Sialic acid O-acetylation : From biosynthesis to roles in health and disease ', Journal of Biological Chemistry, vol. 297, no. 2, 100906, pp. 1-19 . https://doi.org/10.1016/j.jbc.2021.100906 |
ISSN: | 1083-351X 0021-9258 |
Popis: | Sialic acids are nine-carbon sugars that frequently cap glycans at the cell surface in cells of vertebrates as well as cells of certain types of invertebrates and bacteria. The nine-carbon backbone of sialic acids can undergo extensive enzymatic modification in nature and O-acetylation at the C-4/7/8/9 position in particular is widely observed. In recent years, the detection and analysis of O-acetylated sialic acids have advanced, and sialic acid-specific O-acetyltransferases (SOATs) and O-acetylesterases (SIAEs) that add and remove O-acetyl groups, respectively, have been identified and characterized in mammalian cells, invertebrates, bacteria, and viruses. These advances now allow us to draw a more complete picture of the biosynthetic pathway of the diverse O-acetylated sialic acids to drive the generation of genetically and biochemically engineered model cell lines and organisms with altered expression of O-acetylated sialic acids for dissection of their roles in glycoprotein stability, development, and immune recognition, as well as discovery of novel functions. Furthermore, a growing number of studies associate sialic acid O-acetylation with cancer, autoimmunity, and infection, providing rationale for the development of selective probes and inhibitors of SOATs and SIAEs. Here, we discuss the current insights into the biosynthesis and biological functions of O-acetylated sialic acids and review the evidence linking this modification to disease. Furthermore, we discuss emerging strategies for the design, synthesis, and potential application of unnatural Oacetylated sialic acids and inhibitors of SOATs and SIAEs that may enable therapeutic targeting of this versatile sialic acid modification. |
Databáze: | OpenAIRE |
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