AI Article Synopsis
- SARS-CoV-2 binds to ACE2 receptors and gangliosides like GD1a on cell membranes to enter cells effectively.
- The study used supported membrane bilayers to analyze how these interactions work in a lab setting.
- Inhibiting GD1a limits SARS-CoV-2's ability to attach to ACE2, suggesting that GD1a enhances the virus's binding efficiency.
Article Abstract
Viruses utilize cell surface glycans and plasma membrane receptors to attain an adequate attachment strength for initiating cellular entry. We show that SARS-CoV-2 particles bind to endogenous ACE2 receptors and added sialylated gangliosides in near-native membranes. This was explored using supported membrane bilayers (SMBs) that were formed using plasma membrane vesicles having endogenous ACE2 and GD1a gangliosides reconstituted in lipid vesicles. The virus binding rate to the SMBs is influenced by GD1a and inhibition of the ganglioside reduces the extent of virus binding to the membrane receptors. Using combinations of inhibition assays, we confirm that added GD1a in lipid membranes increases the availability of the endogenous ACE2 receptor and results in the synergistic binding of SARS-CoV-2 to the membrane receptors in SMBs.
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| http://dx.doi.org/10.1021/acsinfecdis.3c00519 | DOI Listing |
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