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• W3119184445 abstract "ABSTRACT Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) is causing an unprecedented global pandemic demanding the urgent development of therapeutic strategies. Microarray binding experiments using an extensive heparan sulfate (HS) oligosaccharide library showed that the receptor binding domain (RBD) of the spike of SARS-CoV-2 can bind HS in a length-and sequence-dependent manner. Hexa- and octa-saccharides composed of IdoA2S-GlcNS6S repeating units were identified as optimal ligands. Surface plasma resonance (SPR) showed the SARS-CoV-2 spike protein binds with much higher affinity to heparin (K D = 55 nM) compared to the RBD (K D = 1 μM) alone. We also found that heparin does not interfere in angiotensin-converting enzyme 2 (ACE2) binding or proteolytic processing of the spike. Our data supports a model in which HS functions as the point of initial attachment for SARS-CoV-2 infection. Tissue staining studies using biologically relevant tissues indicate that heparan sulfate proteoglycan (HSPG) is a critical attachment factor for the virus. Collectively, our results highlight the potential of using HS oligosaccharides as a therapeutic agent by inhibiting SARS-CoV-2 binding to target cells." @default.
• W3119184445 created "2021-01-18" @default.
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• W3119184445 date "2020-05-10" @default.
• W3119184445 modified "2023-09-29" @default.
• W3119184445 title "Heparan sulfate proteoglycans as attachment factor for SARS-CoV-2" @default.
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• W3119184445 doi "https://doi.org/10.1101/2020.05.10.087288" @default.
• W3119184445 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7263551" @default.
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