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Article

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

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)
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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