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Area of Science:

  • Biotechnology
  • Nanotechnology
  • Virology

Background:

  • Ferritin nanocages are versatile platforms for nanoreactors and nanocarriers.
  • The Spike (S) receptor-binding domain (RBD) of SARS-CoV-2 is a key target for neutralizing antibodies and viral entry.

Purpose of the Study:

  • To evaluate the interaction efficiency of H-ferritin nanocages displaying SARS-CoV-2 S RBDs with host cell receptors and monoclonal antibodies (mAbs).
  • To characterize the binding pharmacophore and dynamic responses of the S RBD on the ferritin scaffold.

Main Methods:

  • Molecular dynamics simulations were employed to analyze the binding interactions.
  • The study focused on H-ferritin displaying 24 S RBDs and their interactions with ACE2 receptor and mAbs B38 and VVH-72.

Main Results:

  • Ferritin-displayed S RBDs targeted receptor- and antibody-binding interfaces, showing enhanced binding affinity with mAbs.
  • Key interactions involved the variable heavy chain of mAbs, with divergent dynamic responses observed for ACE2 and B38 binding.
  • mAb VVH-72 binding affinity was increased by the receptor, maintaining its structural orientation.

Conclusions:

  • The ferritin-displayed S RBD maintains native binding profiles for receptors and antibodies.
  • This ferritin-S RBD construct is a promising scaffold for pre-fusion stabilization of the Spike protein.
  • It holds potential for the design of effective SARS-CoV-2 RBD vaccines.