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A glycosaminoglycan microarray identifies the binding of SARS‐CoV‐2 spike protein to chondroitin sulfate E

Tomoko Watanabe, Ko Takeda, Keiko Hiemori, Toshikazu Minamisawa, Hiroaki Tateno

2021FEBS Letters16 citationsDOIOpen Access PDF

Abstract

Heparan sulfate (HS), a sulfated glycosaminoglycan (GAG), was reported to be a necessary host attachment factor that promotes SARS-CoV-2 infection. In this study, we developed GAG microarrays based on fluorescence detection for high-sensitivity screening of the GAG-binding specificity of proteins and applied it for the analysis of SARS-CoV-2 spike (S) protein. Among the 20 distinct GAGs, the S protein bound not only to heparin (HEP)/HS but also to chondroitin sulfate E (CSE) in a concentration-dependent manner. We then analyzed the specificity of each subunit of the S protein. While the S1 subunit showed exclusive binding to HEP, the S2 subunit also bound to CSE and HEP/HS. CSE might act as an alternative attachment factor for HS in SARS-CoV-2 infection.

Topics & Concepts

Heparan sulfateGlycosaminoglycanProtein subunitChondroitin sulfateChemistryHeparinSulfationMolecular biologyChondroitinGroup-specific antigenProteoglycanBiochemistryKeratan sulfateBiologyGeneExtracellular matrixAnimal Virus Infections StudiesSARS-CoV-2 and COVID-19 ResearchVirus-based gene therapy research
A glycosaminoglycan microarray identifies the binding of SARS‐CoV‐2 spike protein to chondroitin sulfate E | Litcius