Structure-based design of hepatitis C virus E2 glycoprotein improves serum binding and cross-neutralization

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

The copyright holder for this preprint (which was not peer-reviewed) is the .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 (Figure 8 ). The heterologous isolates collectively diverge substantially in sequence from H77C and represent neutralization phenotypes ranging from moderately to highly resistant ( Table 5) . As we found previously, there was relatively large intra-group variability in neutralization of H77C (19) , and no statistically significant differences between groups were observed. However, heterologous isolates showed much less intra-group variability, with some cases of designs yielding significantly higher neutralization than wild-type sE2. Notably, two resistant isolates had significantly higher neutralization for H445P-immunized sera than wild-type sE2-immunized sera (UKNP1.18.1, J6).