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Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

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Programmable polymorphism of a virus-like particle.

Artur P Biela¹, Antonina Naskalska¹, Farzad Fatehi^2,3

¹Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, 30-392 Krakow, Poland.

Communications Materials

|March 14, 2022

Summary

This summary is machine-generated.

Researchers engineered larger virus-like particles (VLPs) by inserting amino acid sequences into MS2 bacteriophage capsid proteins. This method controls VLP size and morphology for potential vaccine and drug delivery applications.

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Area of Science:

Biotechnology
Structural Biology
Biophysics

Background:

Virus-like particles (VLPs) show promise as artificial vaccines and drug delivery vehicles.
Controlling VLP size and polymorphism is crucial for their utility but challenging with single protein subunits.
Altering VLP geometry is key to achieving size control.

Purpose of the Study:

To achieve size control of MS2 bacteriophage VLPs through protein subunit modification.
To investigate the impact of inserted amino acid sequences on VLP size and morphology.
To understand the assembly dynamics and structural basis of altered VLP formation.

Main Methods:

Insertion of variable amino acid sequences into an external loop of the MS2 bacteriophage coat protein.
Cryo-electron microscopy to determine the structure of engineered VLPs.
Development of a kinetic model to analyze VLP assembly and polymorphism.

Main Results:

Successfully generated larger MS2 VLPs by altering external loop sequences.
Demonstrated that insert length and type control VLP size and geometry.
Observed biased abundance of different VLP symmetries (T=3, T=4, D3, D5) based on insert modifications.
Cryo-EM structures revealed the impact of inserts on VLP architecture.

Conclusions:

Engineered MS2 VLPs with controlled size and morphology via amino acid insertions.
Proposed a mechanism involving altered capsid protein dimer dynamics and conformer interconversion.
This approach offers a method for tailoring VLPs for specific applications in vaccinology and drug delivery.