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Cited by 11Bacteriophages and microbial interactionsEvolution and Genetic DynamicsSupramolecular Self-Assembly in Materials

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Systematic engineering of virus-like particles to identify self-assembly rules for shifting particle size

Open access
Ikwuagwu, Bon, Hartman, Emily, Mills, Carolyn E., Tullman-Ercek, Danielle·2023·Virology
DOI 10.1016/j.virol.2023.01.002PMC PMC10776172

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Abstract

Virus-like particles (VLPs) are promising scaffolds for biomaterials as well as diagnostic and therapeutic applications. However, there are some key challenges to be solved, such as the ability to engineer alternate sizes for varied use cases. To this end, we created a library of MS2 VLP variants at two key residues in the coat protein which have been implicated as important to controlling VLP size and geometry. By adapting a method for systematic mutagenesis coupled with size-based selections and high-throughput sequencing as a readout, we developed a quantitative assessment of two residues in MS2 coat protein that govern the size shift in MS2 VLPs. We then applied the strategy to the equivalent residues in Qβ VLPs, an MS2 homolog, and demonstrate that the analogous pair of residues are also able to impact Qβ VLP size and shape. These results underscore the power of fitness landscapes in identifying critical features for assembly.

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Research works printed but not linked: 26

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Metadata

Authors
Ikwuagwu, B., Hartman, E., Mills, C. E., & Tullman-Ercek, D.
Affiliations
  • Northwestern University (US)
  • University of California, Berkeley (US)
ORCID
Venue
Virology
Publisher
Elsevier BV
Published
2023-02
Volume
579
Pages
137-147
ISSN
0042-6822 (ISSN-L)
DOI
10.1016/j.virol.2023.01.002
PMC
PMC10776172
OpenAlex
W4313560633
Cited by
11
References
1
Citations by year
2026: 3 · 2025: 3 · 2024: 4 · 2023: 1
FWCI
1.67
Type
journal article
Language
en
Open access
Licence
Locations
  • Virology (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Air Force Office of Scientific Research
  • National Defense Science and Engineering Graduate (32 CFR 168a)
  • National Science Foundation (CBET-2043973)
  • U.S. Department of Defense
Topics
  • Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
  • Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
Keywords
virus-like particles, MS2 coat protein, self-assembly, fitness landscape, next-generation sequencing, protein engineering
MeSH terms
Particle Size, Gene Library, Vaccines, Virus-Like Particle

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