9NI9
BG505-CH505 Env glycoprotein in complex with NHP pAb Base-1 isolated from animal RUu18 at week 14
これはPDB形式変換不可エントリーです。
9NI9 の概要
エントリーDOI | 10.2210/pdb9ni9/pdb |
EMDBエントリー | 49457 |
分子名称 | RUu-Base-1 pAb heavy chain, RUu-Base-1 pAb light chain, BG505-CH505 Envelope glycoprotein gp120, ... (7 entities in total) |
機能のキーワード | hiv-1, polyclonal, cryoempem, structural protein |
由来する生物種 | Human immunodeficiency virus 1 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 252463.25 |
構造登録者 | |
主引用文献 | Pratap, P.P.,Cottrell, C.A.,Quinn, J.,Carnathan, D.G.,Bader, D.L.V.,Tran, A.S.,Enemuo, C.A.,Ngo, J.T.,Richey, S.T.,Gao, H.,Shen, X.,Greene, K.M.,Hurtado, J.,Michaels, K.K.,Ben-Akiva, E.,Allen, J.D.,Ozorowski, G.,Crispin, M.,Briney, B.,Montefiori, D.,Silvestri, G.,Irvine, D.J.,Crotty, S.,Ward, A.B. Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques. Biorxiv, 2024 Cited by PubMed Abstract: During infection, the fusion peptide (FP) of HIV envelope glycoprotein (Env) serves a central role in viral fusion with the host cell. As such, the FP is highly conserved and therefore an attractive epitope for vaccine design. Here, we describe a vaccination study in non-human primates (NHPs) where glycan deletions were made on soluble HIV Env to increase FP epitope exposure. When delivered via implantable osmotic pumps, this immunogen primed immune responses against the FP, which were then boosted with heterologous trimers resulting in a focused immune response targeting the conserved FP epitope. Although autologous immunizations did not elicit high affinity FP-targeting antibodies, the conserved FP epitope on a heterologous trimer further matured the lower affinity, FP-targeting B cells. This study suggests using epitope conservation strategies on distinct Env trimer immunogens can focus humoral responses on desired neutralizing epitopes and suppress immune-distracting antibody responses against non-neutralizing epitopes. PubMed: 39651156DOI: 10.1101/2024.11.27.625755 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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