Peptide-controlled access to the interior surface of empty virus nanoparticles

Area of Science:

• Virology and Bionanotechnology
• Biophysical Chemistry

Background:

• High-resolution structure of Cowpea mosaic virus (CPMV) enables applications in vaccine design and nanotechnology.
• Production of empty virus-like particles (eVLPs) expands possibilities for CPMV capsid-based technologies, including internal mineralization.

Purpose of the Study:

• Investigate the role of the small coat (S) protein's carboxyl (C) terminus in controlling CPMV eVLP interior access.
• Determine the efficiency of internal mineralization in relation to the C-terminal peptide.

Main Methods:

• Assessed internal mineralization efficiency of CPMV eVLPs.
• Utilized enzymatic removal of the C-terminal 24-amino acid peptide.
• Genetically modified the C terminus, introducing a six-histidine residue substitution.

Main Results:

• The C-terminal 24-amino acid peptide of the S protein inhibited internal mineralization.
• Enzymatic removal of this peptide eliminated the inhibitory effect.
• Histidine substitution at the C terminus yielded stable particles and enabled external cobalt mineralization.

Conclusions:

• Demonstrated consistent internal and external mineralization of CPMV eVLPs.
• Findings support the development of CPMV eVLPs for bionanotechnological and medical applications.