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The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.15.044073 doi: bioRxiv preprint The copyright holder for this preprint (which was not peer-reviewed) is the .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 1 Values and proline backbone analysis were obtained from the Ramachandran plot analysis web server (http://zlab.bu.edu/rama) (53) . Pre-Pro assessments correspond to pre-proline Ramachandran plot conformation for the backbone of the preceding residue. Unfavorable Pro or Pre-Pro conformations are noted with gray shaded cells. 2 Predicted binding energy change for proline epitope mutant to the HC84.26.5D HMAb, based on the X-ray structure of the complex (PDB code 4Z0X) and computational mutagenesis in Rosetta (54) . Predicted destabilizing values (> 0.5 in Rosetta energy units) are indicated with shaded cells.