The diverse role of heparan sulfate and other GAGs in SARS-CoV-2 infections and therapeutics. (1st January 2023)

• Record Type: Journal Article
• Authors: Eilts, Friederike; Bauer, Sarah; Fraser, Keith; Dordick, Jonathan S.; Wolff, Michael W.; Linhardt, Robert J.; Zhang, Fuming
• Is Part Of: Carbohydrate polymers. Volume 299(2023)
• Publication Date: 2023-01-01
• Subjects: Ac acetate -- ACE2 angiotensin-converting enzyme 2 -- ASGR-1 asialoglycoprotein receptor 1 -- CS chondroitin sulfate -- CD4 cluster of differentiation 4 -- COVID-19 coronavirus disease 2019 -- hCoVs coronavirus strains are infectious to humans -- CP cytoplasm domain -- dp degree of polymerization -- DS dermatan sulfate -- E envelope -- EXT1 exostosin glycosyltransferase 1 -- GalN galactosamine -- GlcN glucosamine -- GlcA glucuronic acid -- GAGs glycosaminoglycans -- HS heparan sulfate -- HP heparin -- HP-1 heptad repeating domain-1 -- HP-2 heptad repeating domain-2 -- HSase heparin lyases -- HIV human immunodeficiency viruses -- HA hyaluronic acid -- IdoA iduronic acid -- IL-6 interleukin 6 -- KS keratan sulfate -- LMWH low molecular weight heparin -- MS mass spectrometry -- M membrane -- MERS Middle East respiratory syndrome -- MD molecular dynamic -- NDST1 N-deacetylase/N-sulfotransferase 1 -- NACH non-anticoagulant low molecular weight heparin -- TRiS non-anticoagulant trisulfated heparin -- NTD N-terminal domain -- NMR nuclear magnetic resonance -- N nucleocapsid -- PAMP pathogen-associated molecular pattern -- PGs proteoglycans -- RBD receptor binding domain -- RBM receptor binding motif -- RAHMM receptor for hyaluronan-mediated motility -- SARS-CoV-1 severe acute respiratory syndrome coronavirus 1 -- SARS-CoV-2 severe acute respiratory syndrome coronavirus 2 -- ss single stranded -- S-protein spike protein -- S sulfate -- SPR surface plasmon resonance -- TM transmembrane domain -- TMPRSS-2 transmembrane protease serine protease-2 -- AXL tyrosine-protein kinase receptor -- UFH unfractionated heparin -- VOCs variants of concern -- VLP virus like particle; Glycosaminoglycans -- Heparan sulfate co-receptor -- Receptor binding domain -- Spike protein -- SARS-CoV-2; Polysaccharides -- Periodicals; Polysaccharides -- Periodicals; Polysaccharides -- Périodiques; Electronic journals; 547.78
• DOI: 10.1016/j.carbpol.2022.120167
• Languages: English
• ISSNs: 0144-8617

Abstract

Abstract: In December 2019, the global coronavirus disease 2019 (COVID-19) pandemic began in Wuhan, China. COVID-19 is caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which infects host cells primarily through the angiotensin-converting enzyme 2 (ACE2) receptor. In addition to ACE2, several studies have shown the importance of heparan sulfate (HS) on the host cell surface as a co-receptor for SARS-CoV-2-binding. This insight has driven research into antiviral therapies, aimed at inhibiting the HS co-receptor-binding, e.g., by glycosaminoglycans (GAGs), a family of sulfated polysaccharides that includes HS. Several GAGs, such as heparin (a highly sulfated analog of HS), are used to treat various health indications, including COVID-19. This review is focused on current research on the involvement of HS in SARS-CoV-2 infection, implications of viral mutations, as well as the use of GAGs and other sulfated polysaccharides as antiviral agents. Graphical abstract: Unlabelled Image