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_36
Snippet: Another design strategy tested in this study was hyperglycosylation, through structure-based addition of N-glycan sequons to mask antigenic domain A, which is associated with nonneutralizing antibodies (25, 26, 28, 42). The concept of down-modulating immunity to this region was based on the observation that this region is highly immunogenic and may divert antibody However, its combination with ΔHVR1 did lead to modest improvement in nAb titers a.....
Document: Another design strategy tested in this study was hyperglycosylation, through structure-based addition of N-glycan sequons to mask antigenic domain A, which is associated with nonneutralizing antibodies (25, 26, 28, 42). The concept of down-modulating immunity to this region was based on the observation that this region is highly immunogenic and may divert antibody However, its combination with ΔHVR1 did lead to modest improvement in nAb titers against one resistant isolate (UKNP2.4.1; p-value < 0.05), compared with wild-type sE2. Previously we used insect cell expression to alter the N-glycan profile of sE2 versus mammalian cell expressed sE2 author/funder. All rights reserved. No reuse allowed without permission.
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