Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.
Parisa Keshavarz-Joud1, Matthew C Jenkins1, Tahiti Dutta1
1School of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30306, USA.
Small (Weinheim an Der Bergstrasse, Germany)
|September 30, 2025
Summary
Virus-like particles (VLPs) exhibit diverse morphologies due to self-assembly sensitivity. Coat protein alterations reveal structural plasticity as a potential general property of these biomolecular structures.
Area of Science:
- Biochemistry and structural biology
- Biophysics
- Virology
Background:
- Virus-like particles (VLPs) are valuable for applications due to stability and homogeneity.
- Their structural uniformity arises from efficient self-assembly, driven by evolutionary viral pressures.
Purpose of the Study:
- To investigate the assembly properties of Leviphage PP7 VLPs.
- To determine if structural plasticity is a common characteristic of self-assembling viral structures.
Main Methods:
- Studied self-assembly of Leviphage PP7 VLPs.
- Analyzed the impact of coat protein sequence variations on VLP morphology.
Main Results:
- Leviphage PP7 VLPs assembled into a broad spectrum of morphologies.
- VLP structure abundance showed sensitivity to minor coat protein sequence modifications.
Conclusions:
- Structural plasticity may be a general feature of virus-like particle self-assembly.
- This finding has implications for VLP design and application development.
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