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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

This summary is machine-generated.

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.

Keywords:

cryo electron microscopy structural diversity structure virus‐like particles

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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.