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_28
Snippet: To demonstrate native-like E2 and E1E2 assembly of the HCVpps in the context of the ELISA assay, purified HCVpps showed binding to monoclonal antibodies that target linear and conformational epitopes on E2 (HCV1, HC84.26.WH.5DL, AR3A) and conformational epitopes on E1E2 (AR4A, AR5A), and did not interact with negative control antibody (CA45) ( Figure S2 )......
Document: To demonstrate native-like E2 and E1E2 assembly of the HCVpps in the context of the ELISA assay, purified HCVpps showed binding to monoclonal antibodies that target linear and conformational epitopes on E2 (HCV1, HC84.26.WH.5DL, AR3A) and conformational epitopes on E1E2 (AR4A, AR5A), and did not interact with negative control antibody (CA45) ( Figure S2 ).
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