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Updated: Sep 17, 2025
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Expression and Purification of Virus-like Particles for Vaccination
Published on: June 2, 2016
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Speed Matters: Directed Assembly of Icosahedral HPV Virus-Like Particles.
Shelby M Klein1, Angela Patterson2, Kim Young2
1Chemistry Department, Indiana University, Bloomington, Indiana 47405, United States.
Journal of the American Chemical Society
|July 1, 2025
Summary
Accelerating human papillomavirus (HPV) virus-like particle (VLP) assembly produces uniform, stable T=7 structures. This method overcomes off-target shapes, enhancing VLP vaccine potential.
Area of Science:
- Biotechnology
- Structural Biology
- Vaccine Development
Background:
- Virus-like particles (VLPs) are crucial vaccine platforms, mimicking native virions for optimal immunogenicity.
- Controlling VLP assembly to achieve native structures is challenging due to off-target formations.
Purpose of the Study:
- To redirect human papillomavirus (HPV) VLP assembly towards the native T=7 icosahedral structure.
- To understand the mechanism of VLP assembly and identify strategies for producing uniform, stable VLPs.
Main Methods:
- Charge detection mass spectrometry and resistive pulse sensing were used to analyze VLP assembly products.
- Computational simulations were employed to identify stable VLP structures.
Main Results:
- Standard HPV VLP assembly conditions result in heterogeneous particle sizes, stalling before the T=7 structure formation.
- Accelerated assembly conditions yield almost exclusively the desired 21 MDa T=7 icosahedral particles.
- Accelerated assembly produces VLPs with increased resistance to dissociation.
Conclusions:
- VLP assembly is influenced by kinetic traps and error-correction mechanisms.
- Accelerating assembly can bypass these traps, leading to the exclusive formation of native, stable T=7 HPV VLPs.
- Uniform, stable VLPs are beneficial for vaccine applications.
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