Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy
2024

How SARS-CoV-2 Spike Protein Binds to Cell Membranes

Sample size: 23 publication 10 minutes Evidence: high

Author Information

Author(s): Zhang Qingrong, Rosa Raissa S. L., Ray Ankita, Durlet Kimberley, Dorrazehi Gol Mohammad, Bernardi Rafael C., Alsteens David

Primary Institution: Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain

Hypothesis

How does the SARS-CoV-2 spike protein interact with host cell membranes, particularly the membrane-binding peptide (MBP)?

Conclusion

The study reveals that the MBP of SARS-CoV-2 preferentially binds to cholesterol-rich membranes, which enhances viral infectivity.

Supporting Evidence

  • The MBP binds five times faster to cholesterol-containing membranes than to sphingomyelin-containing membranes.
  • Cholesterol depletion significantly reduces viral infectivity.
  • The presence of an internal disulfide bond in the MBP enhances its binding to host membranes.
  • Binding events were observed to be longer in cholesterol-rich environments.
  • Cholesterol levels in host cells influence the efficiency of SARS-CoV-2 infection.

Takeaway

The spike protein of the virus that causes COVID-19 sticks to certain parts of our cells better when there's cholesterol around, helping the virus get inside.

Methodology

The study used biolayer interferometry and atomic force microscopy to analyze the binding of the SARS-CoV-2 MBP to lipid membranes.

Digital Object Identifier (DOI)

10.1038/s41467-024-55358-9

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