Self-assembling amyloid-like nanostructures from SARS-CoV-2 S1, S2, RBD and N recombinant proteins

Area of Science:

• Biophysics
• Nanotechnology
• Virology

Background:

• Recombinant proteins of SARS-CoV-2 (S1, S2, RBD, N) were investigated for self-assembly.
• Understanding the structural properties of viral proteins is crucial for vaccine development and disease pathogenesis.

Purpose of the Study:

• To characterize self-assembling nanoparticles (saNP) formed by SARS-CoV-2 proteins.
• To investigate the stability, structure, and cellular interactions of these saNP.
• To explore the potential implications of these amyloid-like nanostructures in disease and diagnostics.

Main Methods:

• Protein purification via affinity chromatography.
• Nanostructure characterization using Scanning Electron Microscopy (SEM), Atomic Force Microscopy (AFM), and Dynamic Light Scattering (DLS).
• Stability assessment under various conditions and cell penetration studies.

Main Results:

• SARS-CoV-2 proteins spontaneously formed solid, amyloid-like saNP and nanofibers.
• AFM revealed distinct mean heights for S1, S2, N, and RBD saNP.
• saNP demonstrated stability over time and through freeze-thaw cycles, with efficient receptor-mediated entry into specific cells.

Conclusions:

• Spontaneous formation of amyloid-like saNP from SARS-CoV-2 proteins is confirmed.
• These nanostructures may contribute to proteinopathy, including neurodegenerative diseases.
• The findings suggest potential impacts on vaccine stability and diagnostic systems.