6V0R
BG505 SOSIP.664 Trimer
6V0R の概要
エントリーDOI | 10.2210/pdb6v0r/pdb |
EMDBエントリー | 20396 |
分子名称 | BG505 SOSIPv5.2 gp120, BG505 SOSIPv5.2 gp41, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
機能のキーワード | antibody, hiv, glycoprotein, viral protein, polyclonal, non-human primate, rhesus macaque |
由来する生物種 | Human immunodeficiency virus 1 (HIV-1) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 233285.05 |
構造登録者 | |
主引用文献 | Nogal, B.,Bianchi, M.,Cottrell, C.A.,Kirchdoerfer, R.N.,Sewall, L.M.,Turner, H.L.,Zhao, F.,Sok, D.,Burton, D.R.,Hangartner, L.,Ward, A.B. Mapping Polyclonal Antibody Responses in Non-human Primates Vaccinated with HIV Env Trimer Subunit Vaccines. Cell Rep, 30:3755-3765.e7, 2020 Cited by PubMed Abstract: Rational immunogen design aims to focus antibody responses to vulnerable sites on primary antigens. Given the size of these antigens, there is, however, potential for eliciting unwanted, off-target responses. Here, we use our electron microscopy polyclonal epitope mapping approach to describe the antibody specificities elicited by immunization of non-human primates with soluble HIV envelope trimers and subsequent repeated viral challenge. An increased diversity of epitopes recognized and the approach angle by which these antibodies bind constitute a hallmark of the humoral response in most protected animals. We also show that fusion peptide-specific antibodies are likely responsible for some neutralization breadth. Moreover, cryoelectron microscopy (cryo-EM) analysis of a fully protected animal reveals a high degree of clonality within a subset of putatively neutralizing antibodies, enabling a detailed molecular description of the antibody paratope. Our results provide important insights into the immune response against a vaccine candidate that entered into clinical trials in 2019. PubMed: 32187547DOI: 10.1016/j.celrep.2020.02.061 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.87 Å) |
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