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Vaccines
Volume 9
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10.3390/vaccines9010008
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Article

N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles

by
Ronja Pogan
1,2,
Victor U. Weiss
3,
Kevin Bond
4,
Jasmin Dülfer
1,
Christoph Krisp
5,
Nicholas Lyktey
4,
Jürgen Müller-Guhl
1,6,
Samuele Zoratto
3,
Günter Allmaier
3,
Martin F. Jarrold
4,
Cesar Muñoz-Fontela
6,
Hartmut Schlüter
5 and
Charlotte Uetrecht
1,2,*
1
Heinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany
2
European XFEL GmbH, 22869 Schenefeld, Germany
3
Institute of Chemical Technologies and Analytics, TU Wien, 1060 Vienna, Austria
4
Department of Chemistry, Indiana University, Bloomington, IN 47405, USA
5
Mass Spectrometric Proteomics Group, Institute of Clinical Chemistry and Laboratory Medicine, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany
6
Partner Site Hamburg-Lübeck-Borstel-Riems, Bernhard Nocht Institute for Tropical Medicine and German Center for Infection Research (DZIF), 20359 Hamburg, Germany
*
Author to whom correspondence should be addressed.
Vaccines 2021, 9(1), 8; https://doi.org/10.3390/vaccines9010008
Received: 25 November 2020 / Revised: 18 December 2020 / Accepted: 21 December 2020 / Published: 24 December 2020
(This article belongs to the Special Issue Research on Development of Norovirus Vaccines)
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Abstract

Noroviruses cause immense sporadic gastroenteritis outbreaks worldwide. Emerging genotypes, which are divided based on the sequence of the major capsid protein VP1, further enhance this public threat. Self-assembling properties of the human norovirus major capsid protein VP1 are crucial for using virus-like particles (VLPs) for vaccine development. However, there is no vaccine available yet. Here, VLPs from different variants produced in insect cells were characterized in detail using a set of biophysical and structural tools. We used native mass spectrometry, gas-phase electrophoretic mobility molecular analysis, and proteomics to get clear insights into particle size, structure, and composition, as well as stability. Generally, noroviruses have been known to form mainly T = 3 particles. Importantly, we identified a major truncation in the capsid proteins as a likely cause for the formation of T = 1 particles. For vaccine development, particle production needs to be a reproducible, reliable process. Understanding the underlying processes in capsid size variation will help to produce particles of a defined capsid size presenting antigens consistent with intact virions. Next to vaccine production itself, this would be immensely beneficial for bio-/nano-technological approaches using viral particles as carriers or triggers for immunological reactions. View Full-Text
Keywords: norovirus; capsid assembly; native mass spectrometry; nES GEMMA; differential mobility analysis; CDMS norovirus; capsid assembly; native mass spectrometry; nES GEMMA; differential mobility analysis; CDMS
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MDPI and ACS Style

Pogan, R.; Weiss, V.U.; Bond, K.; Dülfer, J.; Krisp, C.; Lyktey, N.; Müller-Guhl, J.; Zoratto, S.; Allmaier, G.; Jarrold, M.F.; Muñoz-Fontela, C.; Schlüter, H.; Uetrecht, C. N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles. Vaccines 2021, 9, 8. https://doi.org/10.3390/vaccines9010008

AMA Style

Pogan R, Weiss VU, Bond K, Dülfer J, Krisp C, Lyktey N, Müller-Guhl J, Zoratto S, Allmaier G, Jarrold MF, Muñoz-Fontela C, Schlüter H, Uetrecht C. N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles. Vaccines. 2021; 9(1):8. https://doi.org/10.3390/vaccines9010008

Chicago/Turabian Style

Pogan, Ronja, Victor U. Weiss, Kevin Bond, Jasmin Dülfer, Christoph Krisp, Nicholas Lyktey, Jürgen Müller-Guhl, Samuele Zoratto, Günter Allmaier, Martin F. Jarrold, Cesar Muñoz-Fontela, Hartmut Schlüter, and Charlotte Uetrecht. 2021. "N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles" Vaccines 9, no. 1: 8. https://doi.org/10.3390/vaccines9010008

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