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- W3113995279 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." @default.
- W3113995279 created "2021-01-05" @default.
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- W3113995279 date "2020-12-24" @default.
- W3113995279 modified "2023-10-06" @default.
- W3113995279 title "N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles" @default.
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- W3113995279 doi "https://doi.org/10.3390/vaccines9010008" @default.
- W3113995279 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7824077" @default.
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