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      Sialic acid O-acetylation: From biosynthesis to roles in health and disease

      review-article
      1 , , 1 , , 1 , 1 , 1 , , 2 , 3 ,
      The Journal of Biological Chemistry
      American Society for Biochemistry and Molecular Biology
      sialic acids, O-acetylation, sialic acid O-acetyl transferases (SOATs), sialic acid O-acetyl esterases (SIAEs), influenza C/D virus, glycan modifications, glycobiology, Ac-CoA, acetyl-coenzyme A, ALL, acute lymphoblastic leukemia, BCoV, bovine coronavirus, CASD1, capsule structure1 domain containing 1, CMAH, CMP-Neu5Ac hydroxylase, CMP, cytidine 5′-monophosphate, CPS, capsular polysaccharides, EHEC, enterohemorrhagic Escherichia coli, GBP, glycan-binding protein, HA, hemagglutinin, HE, hemagglutinin esterase protein, HEF, hemagglutinin esterase fusion protein, IA/B/C/DV, Influenza A/B/C/D virus, KDN, 2-keto-3-deoxynononic acid, MERS-CoV, Middle East respiratory syndrome coronavirus, MHV-S, murine hepatitis virus strain S, MUC, mucin, NA, neuraminidase, Neu5Ac, N-acetylneuraminic acid, Neu5Gc, N-glycolylneuraminic acid, NPL, neuraminic acid pyruvate-lyase, O-Ac, O-acetyl, S protein, spike protein, SARS-CoV, severe acute respiratory syndrome coronavirus, SDAV, sialodacryoadenitis virus, Sia, sialic acid, SIAE, sialic acid O-acetyl esterase, Siglec, sialic acid-binding immunoglobulin-like lectin, sLex, sialyl-Lewisx antigen, SOAT, sialic acid O-acetyl transferase

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          Abstract

          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 O-acetylated sialic acids and inhibitors of SOATs and SIAEs that may enable therapeutic targeting of this versatile sialic acid modification.

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          Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

          Summary The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
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            Proteomics. Tissue-based map of the human proteome.

            Resolving the molecular details of proteome variation in the different tissues and organs of the human body will greatly increase our knowledge of human biology and disease. Here, we present a map of the human tissue proteome based on an integrated omics approach that involves quantitative transcriptomics at the tissue and organ level, combined with tissue microarray-based immunohistochemistry, to achieve spatial localization of proteins down to the single-cell level. Our tissue-based analysis detected more than 90% of the putative protein-coding genes. We used this approach to explore the human secretome, the membrane proteome, the druggable proteome, the cancer proteome, and the metabolic functions in 32 different tissues and organs. All the data are integrated in an interactive Web-based database that allows exploration of individual proteins, as well as navigation of global expression patterns, in all major tissues and organs in the human body. Copyright © 2015, American Association for the Advancement of Science.
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              Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

              Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells 1,2 . Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2) 3,4 , isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV. Supplementary information The online version of this article (doi:10.1038/nature02145) contains supplementary material, which is available to authorized users.
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                Author and article information

                Contributors
                Journal
                J Biol Chem
                J Biol Chem
                The Journal of Biological Chemistry
                American Society for Biochemistry and Molecular Biology
                0021-9258
                1083-351X
                19 June 2021
                August 2021
                19 June 2021
                : 297
                : 2
                : 100906
                Affiliations
                [1 ]Institute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen, Nijmegen, the Netherlands
                [2 ]Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark
                [3 ]Hubrecht Institute, Utrecht, the Netherlands
                Author notes
                []For correspondence: Christian Büll; Thomas J. Boltje t.boltje@ 123456ru.nl c.bull@ 123456sund.ku.dk
                [‡]

                These authors contributed equally to this work.

                Article
                S0021-9258(21)00706-7 100906
                10.1016/j.jbc.2021.100906
                8319020
                34157283
                68cef393-c9d4-46b8-876a-9fcae4fd6852
                © 2021 The Authors

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                : 5 April 2021
                : 16 June 2021
                Categories
                JBC Reviews

                Biochemistry
                sialic acids,o-acetylation,sialic acid o-acetyl transferases (soats),sialic acid o-acetyl esterases (siaes),influenza c/d virus,glycan modifications,glycobiology,ac-coa, acetyl-coenzyme a,all, acute lymphoblastic leukemia,bcov, bovine coronavirus,casd1, capsule structure1 domain containing 1,cmah, cmp-neu5ac hydroxylase,cmp, cytidine 5′-monophosphate,cps, capsular polysaccharides,ehec, enterohemorrhagic escherichia coli,gbp, glycan-binding protein,ha, hemagglutinin,he, hemagglutinin esterase protein,hef, hemagglutinin esterase fusion protein,ia/b/c/dv, influenza a/b/c/d virus,kdn, 2-keto-3-deoxynononic acid,mers-cov, middle east respiratory syndrome coronavirus,mhv-s, murine hepatitis virus strain s,muc, mucin,na, neuraminidase,neu5ac, n-acetylneuraminic acid,neu5gc, n-glycolylneuraminic acid,npl, neuraminic acid pyruvate-lyase,o-ac, o-acetyl,s protein, spike protein,sars-cov, severe acute respiratory syndrome coronavirus,sdav, sialodacryoadenitis virus,sia, sialic acid,siae, sialic acid o-acetyl esterase,siglec, sialic acid-binding immunoglobulin-like lectin,slex, sialyl-lewisx antigen,soat, sialic acid o-acetyl transferase

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