Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines

Abstract Vaccine development efforts have recently focused on enabling strong immune responses to poorly immunogenic antigens, via display on multimerisation scaffolds or virus like particles (VLPs). Typically such studies demonstrate improved antibody titer comparing monomeric and nano-arrayed anti...

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Autores principales:	Darren B. Leneghan, Kazutoyo Miura, Iona J. Taylor, Yuanyuan Li, Jing Jin, Karl D. Brune, Martin F. Bachmann, Mark Howarth, Carole A. Long, Sumi Biswas
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/af545a6db3a5422c9c7b0870d3c2cf54
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spelling	oai:doaj.org-article:af545a6db3a5422c9c7b0870d3c2cf542021-12-02T16:06:17ZNanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines10.1038/s41598-017-03798-32045-2322https://doaj.org/article/af545a6db3a5422c9c7b0870d3c2cf542017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03798-3https://doaj.org/toc/2045-2322Abstract Vaccine development efforts have recently focused on enabling strong immune responses to poorly immunogenic antigens, via display on multimerisation scaffolds or virus like particles (VLPs). Typically such studies demonstrate improved antibody titer comparing monomeric and nano-arrayed antigen. There are many such studies and scaffold technologies, but minimal side-by-side evaluation of platforms for both the amount and efficacy of antibodies induced. Here we present direct comparison of three leading platforms displaying the promising malaria transmission-blocking vaccine (TBV) target Pfs25. These platforms encompass the three important routes to antigen-scaffold linkage: genetic fusion, chemical cross-linking and plug-and-display SpyTag/SpyCatcher conjugation. We demonstrate that chemically-conjugated Qβ VLPs elicited the highest quantity of antibodies, while SpyCatcher-AP205-VLPs elicited the highest quality anti-Pfs25 antibodies for transmission blocking upon mosquito feeding. These quantative and qualitative features will guide future nanoassembly optimisation, as well as the development of the new generation of malaria vaccines targeting transmission.Darren B. LeneghanKazutoyo MiuraIona J. TaylorYuanyuan LiJing JinKarl D. BruneMartin F. BachmannMark HowarthCarole A. LongSumi BiswasNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Darren B. Leneghan Kazutoyo Miura Iona J. Taylor Yuanyuan Li Jing Jin Karl D. Brune Martin F. Bachmann Mark Howarth Carole A. Long Sumi Biswas Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
description	Abstract Vaccine development efforts have recently focused on enabling strong immune responses to poorly immunogenic antigens, via display on multimerisation scaffolds or virus like particles (VLPs). Typically such studies demonstrate improved antibody titer comparing monomeric and nano-arrayed antigen. There are many such studies and scaffold technologies, but minimal side-by-side evaluation of platforms for both the amount and efficacy of antibodies induced. Here we present direct comparison of three leading platforms displaying the promising malaria transmission-blocking vaccine (TBV) target Pfs25. These platforms encompass the three important routes to antigen-scaffold linkage: genetic fusion, chemical cross-linking and plug-and-display SpyTag/SpyCatcher conjugation. We demonstrate that chemically-conjugated Qβ VLPs elicited the highest quantity of antibodies, while SpyCatcher-AP205-VLPs elicited the highest quality anti-Pfs25 antibodies for transmission blocking upon mosquito feeding. These quantative and qualitative features will guide future nanoassembly optimisation, as well as the development of the new generation of malaria vaccines targeting transmission.
format	article
author	Darren B. Leneghan Kazutoyo Miura Iona J. Taylor Yuanyuan Li Jing Jin Karl D. Brune Martin F. Bachmann Mark Howarth Carole A. Long Sumi Biswas
author_facet	Darren B. Leneghan Kazutoyo Miura Iona J. Taylor Yuanyuan Li Jing Jin Karl D. Brune Martin F. Bachmann Mark Howarth Carole A. Long Sumi Biswas
author_sort	Darren B. Leneghan
title	Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
title_short	Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
title_full	Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
title_fullStr	Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
title_full_unstemmed	Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
title_sort	nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/af545a6db3a5422c9c7b0870d3c2cf54
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Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines

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