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_6
Snippet: Here we report the generation, characterization, and in vivo immunogenicity of novel structurebased designs of the HCV E2 glycoprotein, which is the primary target of the antibody response to HCV and a major vaccine target. Designs were focused on antigenic domain D, which is a key region of E2 targeted by broadly neutralizing antibodies (bNAbs) that are resistant to viral escape (24), as well as antigenic domain A, which is targeted by non-neutr.....
Document: Here we report the generation, characterization, and in vivo immunogenicity of novel structurebased designs of the HCV E2 glycoprotein, which is the primary target of the antibody response to HCV and a major vaccine target. Designs were focused on antigenic domain D, which is a key region of E2 targeted by broadly neutralizing antibodies (bNAbs) that are resistant to viral escape (24), as well as antigenic domain A, which is targeted by non-neutralizing antibodies (25, 26).
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