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TitleSynthetic Rewiring of Virus-like Particles via Circular Permutation Enables Modular Peptide Display and Protein Encapsulation.
Journal, issue, pagesACS Nano, Vol. 19, Issue 45, Page 39168-39180, Year 2025
Publish dateNov 18, 2025
AuthorsShiqi Liang / Kaavya Butaney / Daniel de Castro Assumpção / James Jung / Nolan W Kennedy / Danielle Tullman-Ercek /
PubMed AbstractVirus-like particles (VLPs) are self-assembling nanoparticles derived from viruses with the potential as scaffolds for myriad applications. They are also excellent testbeds for engineering protein ...Virus-like particles (VLPs) are self-assembling nanoparticles derived from viruses with the potential as scaffolds for myriad applications. They are also excellent testbeds for engineering protein superstructures. Engineers often employ techniques such as amino acid substitutions and insertions/deletions. Yet evolution also utilizes circular permutation, a powerful natural strategy that has not been fully explored in engineering self-assembling protein nanoparticles. Here, we demonstrate this technique using the MS2 VLP as a model self-assembling proteinaceous nanoparticle. We constructed a comprehensive circular permutation library of the fused MS2 coat protein dimer construct. The strategy revealed terminal locations, validated via cryo-electron microscopy, that enabled C-terminal peptide tagging and led to a protein encapsulation strategy via covalent bonding - a feature the native coat protein does not permit. Our systematic study demonstrates the power of circular permutation for engineering features as well as quantitatively and systematically exploring VLP structural determinants.
External linksACS Nano / PubMed:41159643
MethodsEM (single particle)
Resolution2.62 Å
Structure data

70484

9oh5

EMDB-70484, PDB-9oh5:
Cryo-EM structure of the assembled MS2 CPM58 VLP
Method: EM (single particle) / Resolution: 2.62 Å

Source
  • escherichia phage ms2 (virus)
KeywordsVIRUS LIKE PARTICLE / bacteriophage / circular permutation

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