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Molecular Insights into the Interaction between CD147 and the SARS-CoV‑2 Spike Protein
Milton S Gonzalez-Serrano1,2, Li-Yu Chen1, Hemi Desai3
1Institute for Bioprocessing and Analytical Measurement Techniques, Heiligenstadt 37308, Germany.
SARS-CoV-2 spike protein (SP) binds CD147 differently than ACE2, with binding strength increasing at fever temperatures. Heparin enhances SP-CD147 interactions, suggesting new COVID-19 therapeutic targets.
Area of Science:
- Virology and Molecular Biology
- Biophysics
Background:
- Cluster of differentiation 147 (CD147) is a potential auxiliary receptor for SARS-CoV-2 spike protein (SP).
- Detailed binding characteristics of the SP-CD147 interaction are not fully understood.
Purpose of the Study:
- To characterize the binding of SARS-CoV-2 SP to CD147.
- To investigate the influence of temperature and heparin on SP-CD147 binding.
Main Methods:
- Enzyme-Linked Immunosorbent Assay (ELISA)
- Single-molecule force spectroscopy (SMFS)
- Quartz Crystal Microbalance (QCM)
- Molecular dynamics simulations
Main Results:
- SP-CD147 binding force increases significantly at fever-like temperatures, unlike SP-ACE2 interactions.
- Heparin binds independently to both SP and CD147.
- Heparin enhances the binding force between SP and CD147, stabilizing the complex.
Conclusions:
- The CD147-SP interaction is temperature-dependent and modulated by heparin.
- Heparin's stabilizing effect on the SP-CD147 complex offers potential therapeutic strategies for COVID-19.
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