Significant role of host sialylated glycans in the infection and spread of severe acute respiratory syndrome coronavirus 2.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been transmitted across all over the world, in contrast to the limited epidemic of genetically- and virologically-related SARS-CoV. However, the molecular basis explaining the difference in the virological characteristics among SARS-CoV-2 and SARS-CoV has been poorly defined. Here we identified that host ... sialoglycans play a significant role in the efficient spread of SARS-CoV-2 infection, while this was not the case with SARS-CoV. SARS-CoV-2 infection was significantly inhibited by ?2-6-linked sialic acid-containing compounds, but not by ?2-3 analog, in VeroE6/TMPRSS2 cells. The ?2-6-linked compound bound to SARS-CoV-2 spike S1 subunit to competitively inhibit SARS-CoV-2 attachment to cells. Enzymatic removal of cell surface sialic acids impaired the interaction between SARS-CoV-2 spike and angiotensin-converting enzyme 2 (ACE2), and suppressed the efficient spread of SARS-CoV-2 infection over time, in contrast to its least effect on SARS-CoV spread. Our study provides a novel molecular basis of SARS-CoV-2 infection which illustrates the distinctive characteristics from SARS-CoV.
Mesh Terms:
COVID-19, Humans, Peptidyl-Dipeptidase A, Polysaccharides, Protein Binding, SARS-CoV-2, Spike Glycoprotein, Coronavirus
COVID-19, Humans, Peptidyl-Dipeptidase A, Polysaccharides, Protein Binding, SARS-CoV-2, Spike Glycoprotein, Coronavirus
PLoS Pathog
Date: Jun. 01, 2022
PubMed ID: 35700214
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