8F38
Cryo-EM structure of X6 COBRA (H1N1) hemagglutinin bound to CR6261 Fab
8F38 の概要
エントリーDOI | 10.2210/pdb8f38/pdb |
EMDBエントリー | 28833 |
分子名称 | CR6261 Fab light chain, CR6261 Fab heavy chain, hemagglutinin, ... (7 entities in total) |
機能のキーワード | niaid hemagglutinin stalk binding antibody, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein, viral protein-immune system complex, viral protein/immune system |
由来する生物種 | Homo sapiens 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 340731.27 |
構造登録者 | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2022-11-09, 公開日: 2023-12-13, 最終更新日: 2024-10-16) |
主引用文献 | Nagashima, K.A.,Dzimianski, J.V.,Yang, M.,Abendroth, J.,Sautto, G.A.,Ross, T.M.,DuBois, R.M.,Edwards, T.E.,Mousa, J.J. Structural basis for the broad antigenicity of the computationally optimized influenza hemagglutinin X6. Structure, 32:1079-, 2024 Cited by PubMed Abstract: Influenza causes significant morbidity and mortality. As an alternative approach to current seasonal vaccines, the computationally optimized broadly reactive antigen (COBRA) platform has been previously applied to hemagglutinin (HA). This approach integrates wild-type HA sequences into a single immunogen to expand the breadth of accessible antibody epitopes. Adding to previous studies of H1, H3, and H5 COBRA HAs, we define the structural features of another H1 subtype COBRA, X6, that incorporates HA sequences from before and after the 2009 H1N1 influenza pandemic. We determined structures of this antigen alone and in complex with COBRA-specific as well as broadly reactive and functional antibodies, analyzing its antigenicity. We found that X6 possesses features representing both historic and recent H1 HA strains, enabling binding to both head- and stem-reactive antibodies. Overall, these data confirm the integrity of broadly reactive antibody epitopes of X6 and contribute to design efforts for a next-generation vaccine. PubMed: 38810648DOI: 10.1016/j.str.2024.05.001 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.64 Å) |
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