Brune, Karl D; Leneghan, Darren B; Brian, Iona J; Ishizuka, Andrew S; Bachmann, Martin; Draper, Simon J; Biswas, Sumi; Howarth, Mark (2016). Plug-and-Display: decoration of Virus-Like Particles via isopeptide bonds for modular immunization. Scientific Reports, 6(19234), p. 19234. Nature Publishing Group 10.1038/srep19234
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Virus-like particles (VLPs) are non-infectious self-assembling nanoparticles, useful in medicine and nanotechnology. Their repetitive molecularly-defined architecture is attractive for engineering multivalency, notably for vaccination. However, decorating VLPs with target-antigens by genetic fusion or chemical modification is time-consuming and often leads to capsid misassembly or antigen misfolding, hindering generation of protective immunity. Here we establish a platform for irreversibly decorating VLPs simply by mixing with protein antigen. SpyCatcher is a genetically-encoded protein designed to spontaneously form a covalent bond to its peptide-partner SpyTag. We expressed in E. coli VLPs from the bacteriophage AP205 genetically fused to SpyCatcher. We demonstrated quantitative covalent coupling to SpyCatcher-VLPs after mixing with SpyTag-linked to malaria antigens, including CIDR and Pfs25. In addition, we showed coupling to the VLPs for peptides relevant to cancer from epidermal growth factor receptor and telomerase. Injecting SpyCatcher-VLPs decorated with a malarial antigen efficiently induced antibody responses after only a single immunization. This simple, efficient and modular decoration of nanoparticles should accelerate vaccine development, as well as other applications of nanoparticle devices.
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
04 Faculty of Medicine > Department of Dermatology, Urology, Rheumatology, Nephrology, Osteoporosis (DURN) > Clinic of Rheumatology and Immunology |
UniBE Contributor: |
Bachmann, Martin (B) |
Subjects: |
600 Technology > 610 Medicine & health |
ISSN: |
2045-2322 |
Publisher: |
Nature Publishing Group |
Language: |
English |
Submitter: |
Nathalie Taiana |
Date Deposited: |
29 Feb 2016 16:18 |
Last Modified: |
29 Mar 2023 23:34 |
Publisher DOI: |
10.1038/srep19234 |
PubMed ID: |
26781591 |
BORIS DOI: |
10.7892/boris.76236 |
URI: |
https://boris.unibe.ch/id/eprint/76236 |
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