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_15
Snippet: We first screened the structure-based designs described above to assess their effects on E2 glycoprotein antigenicity, to confirm that designs preserved the structure of key E2 epitopes, and to disrupt non-neutralizing antigenic domain A HMAb binding in the case of the N-glycan designs. These designs were cloned in E1E2 and assessed using ELISA with a panel of representative HMAbs to antigenic domains A-E (Figure 2) . The results indicated that m.....
Document: We first screened the structure-based designs described above to assess their effects on E2 glycoprotein antigenicity, to confirm that designs preserved the structure of key E2 epitopes, and to disrupt non-neutralizing antigenic domain A HMAb binding in the case of the N-glycan designs. These designs were cloned in E1E2 and assessed using ELISA with a panel of representative HMAbs to antigenic domains A-E (Figure 2) . The results indicated that mutant H445P maintained approximately wild-type levels of binding to antibodies, while truncations of HVR1 had varying effects. Binding of domain E HMAb HC33.4, and to a lesser extent HC33.1, was negatively affected by truncation of all of HVR1 (residues 384-410 removed; referred to here author/funder. All rights reserved. No reuse allowed without permission.
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