Author: Boyington, Jeffrey C.; Joyce, M. Gordon; Sastry, Mallika; Stewart-Jones, Guillaume B. E.; Chen, Man; Kong, Wing-Pui; Ngwuta, Joan O.; Thomas, Paul V.; Tsybovsky, Yaroslav; Yang, Yongping; Zhang, Baoshan; Chen, Lei; Druz, Aliaksandr; Georgiev, Ivelin S.; Ko, Kiyoon; Zhou, Tongqing; Mascola, John R.; Graham, Barney S.; Kwong, Peter D.
Title: Structure-Based Design of Head-Only Fusion Glycoprotein Immunogens for Respiratory Syncytial Virus Document date: 2016_7_27
ID: 1nbocmux_54
Snippet: The low neutralization titers for i-273 and i-210 were unexpected in light of the nanomolar affinity observed for the antigenic site Ø antibodies D25 and AM22 (Table 1 and S3 Fig). With the i-273 monomer, its relatively small size of 31 kDa may have hindered its immunogenicity [41] and its 13 hydrophilic surface mutations covering approximately 9% of the surface area (S2 Fig) may have distracted the antibody response from neutralizing epitopes. .....
Document: The low neutralization titers for i-273 and i-210 were unexpected in light of the nanomolar affinity observed for the antigenic site Ø antibodies D25 and AM22 (Table 1 and S3 Fig). With the i-273 monomer, its relatively small size of 31 kDa may have hindered its immunogenicity [41] and its 13 hydrophilic surface mutations covering approximately 9% of the surface area (S2 Fig) may have distracted the antibody response from neutralizing epitopes. With the i-210 trimer, the quaternary heterogeneity observed by negative-stain EM suggested that unexpected neoepitopes may also be present, potentially diluting the B cell response to epitopes for neutralizing antibodies.
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