Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display. / Singh, Susheel K; Thrane, Susan; Janitzek, Christoph M; Nielsen, Morten A; Theander, Thor G; Theisen, Michael; Salanti, Ali; Sander, Adam F.

In: Vaccine, Vol. 35, No. 30, 2017, p. 3726-3732.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Singh, SK, Thrane, S, Janitzek, CM, Nielsen, MA, Theander, TG, Theisen, M, Salanti, A & Sander, AF 2017, 'Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display', Vaccine, vol. 35, no. 30, pp. 3726-3732. https://doi.org/10.1016/j.vaccine.2017.05.054

APA

Singh, S. K., Thrane, S., Janitzek, C. M., Nielsen, M. A., Theander, T. G., Theisen, M., Salanti, A., & Sander, A. F. (2017). Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display. Vaccine, 35(30), 3726-3732. https://doi.org/10.1016/j.vaccine.2017.05.054

Vancouver

Singh SK, Thrane S, Janitzek CM, Nielsen MA, Theander TG, Theisen M et al. Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display. Vaccine. 2017;35(30):3726-3732. https://doi.org/10.1016/j.vaccine.2017.05.054

Author

Singh, Susheel K ; Thrane, Susan ; Janitzek, Christoph M ; Nielsen, Morten A ; Theander, Thor G ; Theisen, Michael ; Salanti, Ali ; Sander, Adam F. / Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display. In: Vaccine. 2017 ; Vol. 35, No. 30. pp. 3726-3732.

Bibtex

@article{fac17c67d3b84ddc93b6d423aa42b1a8,
title = "Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display",
abstract = "Malaria is a devastating disease caused by Plasmodium parasites, resulting in almost 0.5 million deaths per year. The Pfs48/45 protein exposed on the P. falciparum sexual stages is one of the most advanced antigen candidates for a transmission-blocking (TB) vaccine in the clinical pipeline. However, it remains essential to identify an optimal vaccine formulation that can facilitate induction of a long-lasting TB anti-Pfs48/45 response. Here we report on the development and evaluation of two Pfs48/45-based virus-like particle (VLP) vaccines generated using the AP205 SpyTag/Catcher VLP system. Two different recombinant proteins (SpyCatcher-R0.6C and SpyCatcher-6C), comprising the Pfs48/45-6C region, were covalently attached to the surface of Spy-tagged Acinetobacter phage AP205 VLPs. Resulting Pfs48/45-VLP complexes appeared as non-aggregated particles of ∼30nm, each displaying an average of 216 (R0.6C) or 291 (6C) copies of the antigens. Both R0.6C and 6C VLP conjugates were strongly reactive with a monoclonal antibody (mAb45.1) targeting a conformational TB Pfs48/45 epitope, suggesting that the TB epitope is accessible for immune recognition on the particles. To select the most suitable vaccine formulation for downstream clinical studies the two VLP vaccines were tested in CD1 mice using different adjuvant formulations. The study demonstrates that VLP-display of R0.6C and 6C significantly increases antigen immunogenicity when using Montanide ISA 720 VG as extrinsic adjuvant.",
author = "Singh, {Susheel K} and Susan Thrane and Janitzek, {Christoph M} and Nielsen, {Morten A} and Theander, {Thor G} and Michael Theisen and Ali Salanti and Sander, {Adam F}",
note = "Copyright {\textcopyright} 2017 Elsevier Ltd. All rights reserved.",
year = "2017",
doi = "10.1016/j.vaccine.2017.05.054",
language = "English",
volume = "35",
pages = "3726--3732",
journal = "Vaccine",
issn = "0264-410X",
publisher = "Elsevier",
number = "30",

}

RIS

TY - JOUR

T1 - Improving the malaria transmission-blocking activity of a Plasmodium falciparum 48/45 based vaccine antigen by SpyTag/SpyCatcher mediated virus-like display

AU - Singh, Susheel K

AU - Thrane, Susan

AU - Janitzek, Christoph M

AU - Nielsen, Morten A

AU - Theander, Thor G

AU - Theisen, Michael

AU - Salanti, Ali

AU - Sander, Adam F

N1 - Copyright © 2017 Elsevier Ltd. All rights reserved.

PY - 2017

Y1 - 2017

N2 - Malaria is a devastating disease caused by Plasmodium parasites, resulting in almost 0.5 million deaths per year. The Pfs48/45 protein exposed on the P. falciparum sexual stages is one of the most advanced antigen candidates for a transmission-blocking (TB) vaccine in the clinical pipeline. However, it remains essential to identify an optimal vaccine formulation that can facilitate induction of a long-lasting TB anti-Pfs48/45 response. Here we report on the development and evaluation of two Pfs48/45-based virus-like particle (VLP) vaccines generated using the AP205 SpyTag/Catcher VLP system. Two different recombinant proteins (SpyCatcher-R0.6C and SpyCatcher-6C), comprising the Pfs48/45-6C region, were covalently attached to the surface of Spy-tagged Acinetobacter phage AP205 VLPs. Resulting Pfs48/45-VLP complexes appeared as non-aggregated particles of ∼30nm, each displaying an average of 216 (R0.6C) or 291 (6C) copies of the antigens. Both R0.6C and 6C VLP conjugates were strongly reactive with a monoclonal antibody (mAb45.1) targeting a conformational TB Pfs48/45 epitope, suggesting that the TB epitope is accessible for immune recognition on the particles. To select the most suitable vaccine formulation for downstream clinical studies the two VLP vaccines were tested in CD1 mice using different adjuvant formulations. The study demonstrates that VLP-display of R0.6C and 6C significantly increases antigen immunogenicity when using Montanide ISA 720 VG as extrinsic adjuvant.

AB - Malaria is a devastating disease caused by Plasmodium parasites, resulting in almost 0.5 million deaths per year. The Pfs48/45 protein exposed on the P. falciparum sexual stages is one of the most advanced antigen candidates for a transmission-blocking (TB) vaccine in the clinical pipeline. However, it remains essential to identify an optimal vaccine formulation that can facilitate induction of a long-lasting TB anti-Pfs48/45 response. Here we report on the development and evaluation of two Pfs48/45-based virus-like particle (VLP) vaccines generated using the AP205 SpyTag/Catcher VLP system. Two different recombinant proteins (SpyCatcher-R0.6C and SpyCatcher-6C), comprising the Pfs48/45-6C region, were covalently attached to the surface of Spy-tagged Acinetobacter phage AP205 VLPs. Resulting Pfs48/45-VLP complexes appeared as non-aggregated particles of ∼30nm, each displaying an average of 216 (R0.6C) or 291 (6C) copies of the antigens. Both R0.6C and 6C VLP conjugates were strongly reactive with a monoclonal antibody (mAb45.1) targeting a conformational TB Pfs48/45 epitope, suggesting that the TB epitope is accessible for immune recognition on the particles. To select the most suitable vaccine formulation for downstream clinical studies the two VLP vaccines were tested in CD1 mice using different adjuvant formulations. The study demonstrates that VLP-display of R0.6C and 6C significantly increases antigen immunogenicity when using Montanide ISA 720 VG as extrinsic adjuvant.

U2 - 10.1016/j.vaccine.2017.05.054

DO - 10.1016/j.vaccine.2017.05.054

M3 - Journal article

C2 - 28578824

VL - 35

SP - 3726

EP - 3732

JO - Vaccine

JF - Vaccine

SN - 0264-410X

IS - 30

ER -

ID: 179521892