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Single-Point Mutations in Qβ Virus-like Particles Change Binding to Cells
Marisa L Martino1, Stephen N Crooke2, Marianne Manchester3
1Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
Biomacromolecules
|July 12, 2021
Summary
Modifying virus-like particles (VLPs) by altering lysine residues reduces unwanted cell binding. This research enables the development of safer VLPs for targeted delivery applications.
Area of Science:
- Biotechnology
- Molecular Biology
- Biochemistry
Background:
- Virus-like particles (VLPs) are versatile platforms for functionalization.
- Nonspecific cell association can limit VLP applications in biological systems.
- Lysine residues are implicated in mediating these nonspecific interactions.
Purpose of the Study:
- To investigate the role of lysine residues in VLP-cell interactions.
- To engineer VLPs with reduced nonspecific binding for improved targeted delivery.
Main Methods:
- Chemical acylation of surface-exposed amines on Qβ VLPs.
- Site-directed mutagenesis of lysine residues on Qβ VLPs.
- Assessing VLP association with mammalian cells.
Main Results:
- Chemical acylation significantly reduced nonspecific VLP association with cells.
- Single-point mutations were generally well-tolerated, while multiple mutations affected capsid integrity.
- Specific mutations (K13E, K46Q) dramatically altered cellular binding.
- Qβ VLPs interact with plasma membrane components independently of surface charge.
Conclusions:
- Lysine residues play a critical role in mediating nonspecific VLP-cell interactions.
- Mutational strategies can be employed to control VLP cellular binding.
- Engineered VLPs with reduced nonspecificity offer potential for enhanced targeted delivery applications.
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