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_18
Snippet: The two candidate structure-based E2 designs H445P, Y632NS, as well as ΔHVR1, were expressed as soluble E2 (sE2) glycoproteins and tested for thermostability and binding affinity to a panel of HMAbs, as well as the CD81 receptor ( Table 3) . Pairwise combinations of these designs, and a "Triple" design with all three modifications, were also expressed and tested. As noted previously by others (27), wild-type sE2 was found to exhibit high thermos.....
Document: The two candidate structure-based E2 designs H445P, Y632NS, as well as ΔHVR1, were expressed as soluble E2 (sE2) glycoproteins and tested for thermostability and binding affinity to a panel of HMAbs, as well as the CD81 receptor ( Table 3) . Pairwise combinations of these designs, and a "Triple" design with all three modifications, were also expressed and tested. As noted previously by others (27), wild-type sE2 was found to exhibit high thermostability (Tm = 84.5 C in Table 3 ). All designs likewise showed high thermostability, with only minor reductions in Tm, with the exception of combined Triple which had the lowest measured thermostability among the tested E2 mutants (Tm = 76.5 C).
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