Modular vaccine platform based on the norovirus-like particle

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Abstract

Background

Virus-like particle (VLP) vaccines have recently emerged as a safe and effective alternative to conventional vaccine technologies. The strong immunogenic effects of VLPs can be harnessed for making vaccines against any pathogen by decorating VLPs with antigens from the pathogen. Producing the antigenic pathogen fragments and the VLP platform separately makes vaccine development rapid and convenient. Here we decorated the norovirus-like particle with two conserved influenza antigens and tested for the immunogenicity of the vaccine candidates in BALB/c mice.

Results

SpyTagged noro-VLP was expressed with high efficiency in insect cells and purified using industrially scalable methods. Like the native noro-VLP, SpyTagged noro-VLP is stable for months when refrigerated in a physiological buffer. The conserved influenza antigens were produced separately as SpyCatcher fusions in E. coli before covalent conjugation on the surface of noro-VLP. The noro-VLP had a high adjuvant effect, inducing high titers of antibody production against the antigens presented on its surface.

Conclusions

The modular noro-VLP vaccine platform presented here offers a rapid, convenient and safe method to present various soluble protein antigens to the immune system for vaccination and antibody production purposes.

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Most cited references 45

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Fiji: an open-source platform for biological-image analysis.

Johannes Schindelin, Ignacio Arganda-Carreras, Erwin Frise … (2019)

Fiji is a distribution of the popular open-source software ImageJ focused on biological-image analysis. Fiji uses modern software engineering practices to combine powerful software libraries with a broad range of scripting languages to enable rapid prototyping of image-processing algorithms. Fiji facilitates the transformation of new algorithms into ImageJ plugins that can be shared with end users through an integrated update system. We propose Fiji as a platform for productive collaboration between computer science and biology research communities.

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Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin.

B. Zakeri, J. O. Fierer, E Celik … (2012)

Protein interactions with peptides generally have low thermodynamic and mechanical stability. Streptococcus pyogenes fibronectin-binding protein FbaB contains a domain with a spontaneous isopeptide bond between Lys and Asp. By splitting this domain and rational engineering of the fragments, we obtained a peptide (SpyTag) which formed an amide bond to its protein partner (SpyCatcher) in minutes. Reaction occurred in high yield simply upon mixing and amidst diverse conditions of pH, temperature, and buffer. SpyTag could be fused at either terminus or internally and reacted specifically at the mammalian cell surface. Peptide binding was not reversed by boiling or competing peptide. Single-molecule dynamic force spectroscopy showed that SpyTag did not separate from SpyCatcher until the force exceeded 1 nN, where covalent bonds snap. The robust reaction conditions and irreversible linkage of SpyTag shed light on spontaneous isopeptide bond formation and should provide a targetable lock in cells and a stable module for new protein architectures.

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The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability.

Frank Niesen, Helena Berglund, Masoud Vedadi (2007)

Differential scanning fluorimetry (DSF) is a rapid and inexpensive screening method to identify low-molecular-weight ligands that bind and stabilize purified proteins. The temperature at which a protein unfolds is measured by an increase in the fluorescence of a dye with affinity for hydrophobic parts of the protein, which are exposed as the protein unfolds. A simple fitting procedure allows quick calculation of the transition midpoint; the difference in the temperature of this midpoint in the presence and absence of ligand is related to the binding affinity of the small molecule, which can be a low-molecular-weight compound, a peptide or a nucleic acid. DSF is best performed using a conventional real-time PCR instrument. Ligand solutions from a storage plate are added to a solution of protein and dye, distributed into the wells of the PCR plate and fluorescence intensity measured as the temperature is raised gradually. Results can be obtained in a single day.

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Author and article information

Contributors

Minna M. Hankaniemi: minna.hankaniemi@tuni.fi

Vesna Blazevic:

ORCID: http://orcid.org/0000-0002-9357-1480

vesna.blazevic@tuni.fi

Vesa P. Hytönen: vesa.hytonen@tuni.fi

Journal

Journal ID (nlm-ta): J Nanobiotechnology

Journal ID (iso-abbrev): J Nanobiotechnology

Title: Journal of Nanobiotechnology

Publisher: BioMed Central (London )

ISSN (Electronic): 1477-3155

Publication date (Electronic): 19 January 2021

Publication date PMC-release: 19 January 2021

Publication date Collection: 2021

Volume: 19

Electronic Location Identifier: 25

Affiliations

[1 ]GRID grid.502801.e, ISNI 0000 0001 2314 6254, Faculty of Medicine and Health Technology, , Tampere University, ; 33014 Tampere, Finland

[2 ]GRID grid.502801.e, ISNI 0000 0001 2314 6254, Vaccine Development and Immunology/Vaccine Research Center, Faculty of Medicine and Health Technology, , Tampere University, ; Tampere, Finland

[3 ]Fimlab Laboratories, Tampere, Finland

Author information

Vesna Blazevic http://orcid.org/0000-0002-9357-1480

Article

Publisher ID: 772

DOI: 10.1186/s12951-021-00772-0

PMC ID: 7815183

PubMed ID: 33468139

SO-VID: 6234845e-d8fc-4580-8554-af7b435a3015

License:

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

History

Date received : 27 August 2020

Date accepted : 8 January 2021

Funding

Funded by: Research on Viral disease Foundation

Funded by: V.A. Kotilainen foundation

Funded by: Onni and Hilja Tuovinen Foundation

Funded by: Academy of Finland

Award ID: 309455

Award ID: 295814

Award Recipient : Marko Pesu Minna M. Hankaniemi

Funded by: Tampere Tuberculosis Foundation

Funded by: Cancer Society Finland

Funded by: Competitive State Research Financing

Custom metadata

ScienceOpen disciplines: Biotechnology

Keywords: vlp,vaccine,influenza,spycatcher,virus

Data availability:

ScienceOpen disciplines: Biotechnology

Keywords: vlp, vaccine, influenza, spycatcher, virus

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Modular vaccine platform based on the norovirus-like particle

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Abstract

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Annual Reviews: Coronavirus Research

Most cited references 45

Fiji: an open-source platform for biological-image analysis.

Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin.

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability.

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Cited by 12

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