8EZ7
Structure of 1F04 Fab in complex with A/Moscow/10/1999 (H3N2) influenza virus neuraminidase
8EZ7 の概要
| エントリーDOI | 10.2210/pdb8ez7/pdb |
| EMDBエントリー | 28729 |
| 分子名称 | Heavy chain of influenza virus neuraminidase antibody 1F04, Light chain of influenza virus neuraminidase antibody 1F04, Neuraminidase, ... (6 entities in total) |
| 機能のキーワード | antibody, neuraminidase, influenza, hydrolase-immune system complex, hydrolase/immune system |
| 由来する生物種 | Homo sapiens 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 70326.88 |
| 構造登録者 | |
| 主引用文献 | Lei, R.,Kim, W.,Lv, H.,Mou, Z.,Scherm, M.J.,Schmitz, A.J.,Turner, J.S.,Tan, T.J.C.,Wang, Y.,Ouyang, W.O.,Liang, W.,Rivera-Cardona, J.,Teo, C.,Graham, C.S.,Brooke, C.B.,Presti, R.M.,Mok, C.K.P.,Krammer, F.,Dai, X.,Ellebedy, A.H.,Wu, N.C. Leveraging vaccination-induced protective antibodies to define conserved epitopes on influenza N2 neuraminidase. Immunity, 56:2621-, 2023 Cited by PubMed Abstract: There is growing appreciation for neuraminidase (NA) as an influenza vaccine target; however, its antigenicity remains poorly characterized. In this study, we isolated three broadly reactive N2 antibodies from the plasmablasts of a single vaccinee, including one that cross-reacts with NAs from seasonal H3N2 strains spanning five decades. Although these three antibodies have diverse germline usages, they recognize similar epitopes that are distant from the NA active site and instead involve the highly conserved underside of NA head domain. We also showed that all three antibodies confer prophylactic and therapeutic protection in vivo, due to both Fc effector functions and NA inhibition through steric hindrance. Additionally, the contribution of Fc effector functions to protection in vivo inversely correlates with viral growth inhibition activity in vitro. Overall, our findings advance the understanding of NA antibody response and provide important insights into the development of a broadly protective influenza vaccine. PubMed: 37967533DOI: 10.1016/j.immuni.2023.10.005 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.6 Å) |
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