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Mueller-Guhl, J.

Publications and source records attributed to Mueller-Guhl, J..

2 recordsLinked to original sources

Applying distinct CDMS strategies to observe non-classical virus capsid assembly

In conventional native mass spectrometry (MS), one faces severe limitations when challenged with heterogenous, high mass samples, commonly failing to resolve clear peak distributions and thus mass determination. Charge detection MS (CDMS) has emerged as a premier method to analyze these samples by determining mass-to-charge ratio (m/z) and charge (z) simultaneously. Here, the two currently available commercialized CDMS systems, the Orbitrap-based Direct Mass Technology (DMT) and the electrostatic linear ion trap (ELIT)-based Xevo CDMS are applied to human norovirus capsids from two different strains, GI.1 Norwalk and GII.17 Kawasaki. The norovirus capsid is highly heterogenous due to N-terminal processing on the repeating subunits that it is built from and commonly forms T = 3 and sometimes T = 4 particles. Both CDMS approaches were able to determine similar masses in both strains. GII.17 Kawasaki exhibits both T = 3 and T = 4 particles, though the Xevo CDMS measurements were closer to the theoretical mass than the DMT instrument. Interestingly, GII.17 Kawasaki also displayed non-classical mass distributions with high abundance in-between T = 3 and T = 4 which was then confirmed by cryogenic electron microscopy (cryo-EM), demonstrating an oval capsid shape. GI.1 Norwalk displays a wide mass distribution in both instruments that exceeds the theoretical T = 3 mass by 8-10 %. Proteomics and native MS experiments suggest possible interactions with a protein from the expression system. This study demonstrates the capabilities of two distinct CDMS methodologies on two viral capsids and presents the first non-classical capsid assembly in a GII.17 noroviral capsid.

biochemistry↗

N-terminal VP1 truncations favor T=1 norovirus-like particles

Noroviruses cause immense sporadic gastroenteritis outbreaks worldwide. Emerging genotypes, which are divided based on VP1 sequence, 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 are characterized in detail using a set of biophysical and structural tools. We are using native mass spectrometry, gas-phase electrophoretic mobility molecular analysis and proteomics to get clear insights into particle size, structure, composition as well as stability. Generally, noroviruses have been known to form mainly T=3 particles. Importantly, we identify a major truncation in the capsid proteins as a likely cause for the formation of merely 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.

biophysics↗