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The Enigmatic Conserved Q134-F135-N137 Triad in SARS-CoV-2 Spike Protein: A Conformational Transducer?
Marine Lefebvre1,2, Henri Chahinian3, Nouara Yahi3
1IHU Méditerranée Infection, 19-21 Boulevard Jean Moulin, 13005 Marseille, France.
Biomolecules
|January 28, 2026
Summary
Lipid raft gangliosides trigger SARS-CoV-2 spike protein unmasking via a conformational wave initiated by a conserved amino acid triad in the N-terminal domain. This interaction reveals the receptor-binding domain, offering a potential therapeutic target.
Area of Science:
- Virology
- Structural Biology
- Biophysics
Background:
- SARS-CoV-2 entry relies on spike protein conformational changes.
- Lipid rafts and gangliosides are implicated in viral entry.
- The spike protein's receptor-binding domain (RBD) is initially hidden.
Purpose of the Study:
- To investigate the mechanism of ganglioside-induced spike protein conformational change.
- To elucidate the role of the N-terminal domain (NTD) and a conserved amino acid triad in RBD exposure.
- To explore potential therapeutic targets for disrupting SARS-CoV-2 entry.
Main Methods:
- In silico analysis
- Cryoelectron microscopy
- Physicochemical approaches
- Integration of structural and experimental data
Main Results:
- Gangliosides induce conformational changes in the spike protein's NTD, propagating to the RBD.
- A conserved Q134-F135-N137 triad in the NTD acts as a conformational transducer.
- A dual conformational/quantum wave mechanism is hypothesized, involving electron transfer in the NTD.
Conclusions:
- The conserved NTD triad is critical for SARS-CoV-2 entry by mediating RBD unmasking.
- This triad represents a potential Achilles' heel for therapeutic and vaccinal interventions.
- Targeting this conserved element could disrupt viral infection by preventing conformational changes.
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