Bacterial superglue enables easy development of efficient virus-like particle based vaccines

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Standard

Bacterial superglue enables easy development of efficient virus-like particle based vaccines. / Thrane, Susan; Janitzek, Christoph M; Matondo, Sungwa; dos Santos Marques Resende, Mafalda; Gustavsson, Tobias; De Jongh, Willem Adriaan; Clemmensen, Stine; Roeffen, Will; van de Vegte-Bolmer, Marga; van Gemert, Geert Jan; Sauerwein, Robert; Schiller, John T; Nielsen, Morten A; Theander, Thor G; Salanti, Ali; Pedersen, Adam Frederik Sander.

I: Journal of Nanobiotechnology, Bind 14, 30, 27.04.2016.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Thrane, S, Janitzek, CM, Matondo, S, dos Santos Marques Resende, M, Gustavsson, T, De Jongh, WA, Clemmensen, S, Roeffen, W, van de Vegte-Bolmer, M, van Gemert, GJ, Sauerwein, R, Schiller, JT, Nielsen, MA, Theander, TG, Salanti, A & Pedersen, AFS 2016, 'Bacterial superglue enables easy development of efficient virus-like particle based vaccines', Journal of Nanobiotechnology, bind 14, 30. https://doi.org/10.1186/s12951-016-0181-1

APA

Thrane, S., Janitzek, C. M., Matondo, S., dos Santos Marques Resende, M., Gustavsson, T., De Jongh, W. A., ... Pedersen, A. F. S. (2016). Bacterial superglue enables easy development of efficient virus-like particle based vaccines. Journal of Nanobiotechnology, 14, [30]. https://doi.org/10.1186/s12951-016-0181-1

Vancouver

Thrane S, Janitzek CM, Matondo S, dos Santos Marques Resende M, Gustavsson T, De Jongh WA o.a. Bacterial superglue enables easy development of efficient virus-like particle based vaccines. Journal of Nanobiotechnology. 2016 apr 27;14. 30. https://doi.org/10.1186/s12951-016-0181-1

Author

Thrane, Susan ; Janitzek, Christoph M ; Matondo, Sungwa ; dos Santos Marques Resende, Mafalda ; Gustavsson, Tobias ; De Jongh, Willem Adriaan ; Clemmensen, Stine ; Roeffen, Will ; van de Vegte-Bolmer, Marga ; van Gemert, Geert Jan ; Sauerwein, Robert ; Schiller, John T ; Nielsen, Morten A ; Theander, Thor G ; Salanti, Ali ; Pedersen, Adam Frederik Sander. / Bacterial superglue enables easy development of efficient virus-like particle based vaccines. I: Journal of Nanobiotechnology. 2016 ; Bind 14.

Bibtex

@article{e5ed035686244903b6f5ee1d2f2e7751,
title = "Bacterial superglue enables easy development of efficient virus-like particle based vaccines",
abstract = "BACKGROUND: Virus-like particles (VLPs) represent a significant advance in the development of subunit vaccines, combining high safety and efficacy. Their particulate nature and dense repetitive subunit organization makes them ideal scaffolds for display of vaccine antigens. Traditional approaches for VLP-based antigen display require labor-intensive trial-and-error optimization, and often fail to generate dense antigen display. Here we utilize the split-intein (SpyTag/SpyCatcher) conjugation system to generate stable isopeptide bound antigen-VLP complexes by simply mixing of the antigen and VLP components.RESULTS: Genetic fusion of SpyTag or SpyCatcher to the N-terminus and/or C-terminus of the Acinetobacter phage AP205 capsid protein resulted in formation of stable, nonaggregated VLPs expressing one SpyCatcher, one SpyTag or two SpyTags per capsid protein. Mixing of spy-VLPs with eleven different vaccine antigens fused to SpyCatcher or SpyTag resulted in formation of antigen-VLP complexes with coupling efficiencies ({\%} occupancy of total VLP binding sites) ranging from 22-88 {\%}. In mice, spy-VLP vaccines presenting the malaria proteins Pfs25 or VAR2CSA markedly increased antibody titer, affinity, longevity and functional efficacy compared to corresponding vaccines employing monomeric proteins. The spy-VLP vaccines also effectively broke B cell self-tolerance and induced potent and durable antibody responses upon vaccination with cancer or allergy-associated self-antigens (PD-L1, CTLA-4 and IL-5).CONCLUSIONS: The spy-VLP system constitutes a versatile and rapid method to develop highly immunogenic VLP-based vaccines. Our data provide proof-of-concept for the technology's ability to present complex vaccine antigens to the immune system and elicit robust functional antibody responses as well as to efficiently break B cell self-tolerance. The spy-VLP-system may serve as a generic tool for the cost-effective development of effective VLP-vaccines against both infectious- and non-communicable diseases and could facilitate rapid and unbiased screening of vaccine candidate antigens.",
author = "Susan Thrane and Janitzek, {Christoph M} and Sungwa Matondo and {dos Santos Marques Resende}, Mafalda and Tobias Gustavsson and {De Jongh}, {Willem Adriaan} and Stine Clemmensen and Will Roeffen and {van de Vegte-Bolmer}, Marga and {van Gemert}, {Geert Jan} and Robert Sauerwein and Schiller, {John T} and Nielsen, {Morten A} and Theander, {Thor G} and Ali Salanti and Pedersen, {Adam Frederik Sander}",
year = "2016",
month = "4",
day = "27",
doi = "10.1186/s12951-016-0181-1",
language = "English",
volume = "14",
journal = "Journal of Nanobiotechnology",
issn = "1477-3155",
publisher = "BioMed Central",

}

RIS

TY - JOUR

T1 - Bacterial superglue enables easy development of efficient virus-like particle based vaccines

AU - Thrane, Susan

AU - Janitzek, Christoph M

AU - Matondo, Sungwa

AU - dos Santos Marques Resende, Mafalda

AU - Gustavsson, Tobias

AU - De Jongh, Willem Adriaan

AU - Clemmensen, Stine

AU - Roeffen, Will

AU - van de Vegte-Bolmer, Marga

AU - van Gemert, Geert Jan

AU - Sauerwein, Robert

AU - Schiller, John T

AU - Nielsen, Morten A

AU - Theander, Thor G

AU - Salanti, Ali

AU - Pedersen, Adam Frederik Sander

PY - 2016/4/27

Y1 - 2016/4/27

N2 - BACKGROUND: Virus-like particles (VLPs) represent a significant advance in the development of subunit vaccines, combining high safety and efficacy. Their particulate nature and dense repetitive subunit organization makes them ideal scaffolds for display of vaccine antigens. Traditional approaches for VLP-based antigen display require labor-intensive trial-and-error optimization, and often fail to generate dense antigen display. Here we utilize the split-intein (SpyTag/SpyCatcher) conjugation system to generate stable isopeptide bound antigen-VLP complexes by simply mixing of the antigen and VLP components.RESULTS: Genetic fusion of SpyTag or SpyCatcher to the N-terminus and/or C-terminus of the Acinetobacter phage AP205 capsid protein resulted in formation of stable, nonaggregated VLPs expressing one SpyCatcher, one SpyTag or two SpyTags per capsid protein. Mixing of spy-VLPs with eleven different vaccine antigens fused to SpyCatcher or SpyTag resulted in formation of antigen-VLP complexes with coupling efficiencies (% occupancy of total VLP binding sites) ranging from 22-88 %. In mice, spy-VLP vaccines presenting the malaria proteins Pfs25 or VAR2CSA markedly increased antibody titer, affinity, longevity and functional efficacy compared to corresponding vaccines employing monomeric proteins. The spy-VLP vaccines also effectively broke B cell self-tolerance and induced potent and durable antibody responses upon vaccination with cancer or allergy-associated self-antigens (PD-L1, CTLA-4 and IL-5).CONCLUSIONS: The spy-VLP system constitutes a versatile and rapid method to develop highly immunogenic VLP-based vaccines. Our data provide proof-of-concept for the technology's ability to present complex vaccine antigens to the immune system and elicit robust functional antibody responses as well as to efficiently break B cell self-tolerance. The spy-VLP-system may serve as a generic tool for the cost-effective development of effective VLP-vaccines against both infectious- and non-communicable diseases and could facilitate rapid and unbiased screening of vaccine candidate antigens.

AB - BACKGROUND: Virus-like particles (VLPs) represent a significant advance in the development of subunit vaccines, combining high safety and efficacy. Their particulate nature and dense repetitive subunit organization makes them ideal scaffolds for display of vaccine antigens. Traditional approaches for VLP-based antigen display require labor-intensive trial-and-error optimization, and often fail to generate dense antigen display. Here we utilize the split-intein (SpyTag/SpyCatcher) conjugation system to generate stable isopeptide bound antigen-VLP complexes by simply mixing of the antigen and VLP components.RESULTS: Genetic fusion of SpyTag or SpyCatcher to the N-terminus and/or C-terminus of the Acinetobacter phage AP205 capsid protein resulted in formation of stable, nonaggregated VLPs expressing one SpyCatcher, one SpyTag or two SpyTags per capsid protein. Mixing of spy-VLPs with eleven different vaccine antigens fused to SpyCatcher or SpyTag resulted in formation of antigen-VLP complexes with coupling efficiencies (% occupancy of total VLP binding sites) ranging from 22-88 %. In mice, spy-VLP vaccines presenting the malaria proteins Pfs25 or VAR2CSA markedly increased antibody titer, affinity, longevity and functional efficacy compared to corresponding vaccines employing monomeric proteins. The spy-VLP vaccines also effectively broke B cell self-tolerance and induced potent and durable antibody responses upon vaccination with cancer or allergy-associated self-antigens (PD-L1, CTLA-4 and IL-5).CONCLUSIONS: The spy-VLP system constitutes a versatile and rapid method to develop highly immunogenic VLP-based vaccines. Our data provide proof-of-concept for the technology's ability to present complex vaccine antigens to the immune system and elicit robust functional antibody responses as well as to efficiently break B cell self-tolerance. The spy-VLP-system may serve as a generic tool for the cost-effective development of effective VLP-vaccines against both infectious- and non-communicable diseases and could facilitate rapid and unbiased screening of vaccine candidate antigens.

U2 - 10.1186/s12951-016-0181-1

DO - 10.1186/s12951-016-0181-1

M3 - Journal article

VL - 14

JO - Journal of Nanobiotechnology

JF - Journal of Nanobiotechnology

SN - 1477-3155

M1 - 30

ER -

ID: 160866258