Author: Brian G. Pierce; Zhen-Yong Keck; Ruixue Wang; Patrick Lau; Kyle Garagusi; Khadija Elkholy; Eric A. Toth; Richard A. Urbanowicz; Johnathan D. Guest; Pragati Agnihotri; Melissa C. Kerzic; Alexander Marin; Alexander K. Andrianov; Jonathan K. Ball; Roy A. Mariuzza; Thomas R. Fuerst; Steven K.H. Foung
Title: Structure-based design of hepatitis C virus E2 glycoprotein improves serum binding and cross-neutralization Document date: 2020_4_17
ID: b6to1v4u_35
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.15.044073 doi: bioRxiv preprint increased nAb sensitivity and CD81 receptor binding, while a recent study has indicated that HVR1 may modulate viral dynamics and open and closed conformations during envelope breathing (41) . Despite its importance in the context of the virion and its dynamics, its removal appears to have a neutral or mini.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.15.044073 doi: bioRxiv preprint increased nAb sensitivity and CD81 receptor binding, while a recent study has indicated that HVR1 may modulate viral dynamics and open and closed conformations during envelope breathing (41) . Despite its importance in the context of the virion and its dynamics, its removal appears to have a neutral or minimal effect on the immunogenicity of recombinant envelope glycoproteins.
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