8U1C
A mechanistic understanding of protective influenza B neuraminidase mAbs at the airway interface
8U1C の概要
エントリーDOI | 10.2210/pdb8u1c/pdb |
EMDBエントリー | 41809 |
分子名称 | mAb-400 heavy chain, mAb-400 light chain, Neuraminidase, ... (4 entities in total) |
機能のキーワード | neuraminidase sialidase, hydrolase |
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 | 77496.65 |
構造登録者 | |
主引用文献 | Wolters, R.M.,Ferguson, J.A.,Nunez, I.A.,Chen, E.E.,Sornberger, T.,Myers, L.,Oeverdieck, S.,Raghavan, S.S.R.,Kona, C.,Handal, L.S.,Esilu, T.E.,Davidson, E.,Doranz, B.J.,Engdahl, T.B.,Kose, N.,Williamson, L.E.,Creech, C.B.,Gibson-Corley, K.N.,Ward, A.B.,Crowe Jr., J.E. Isolation of human antibodies against influenza B neuraminidase and mechanisms of protection at the airway interface. Immunity, 57:1413-1427.e9, 2024 Cited by PubMed Abstract: Influenza B viruses (IBVs) comprise a substantial portion of the circulating seasonal human influenza viruses. Here, we describe the isolation of human monoclonal antibodies (mAbs) that recognized the IBV neuraminidase (NA) glycoprotein from an individual following seasonal vaccination. Competition-binding experiments suggested the antibodies recognized two major antigenic sites. One group, which included mAb FluB-393, broadly inhibited IBV NA sialidase activity, protected prophylactically in vivo, and bound to the lateral corner of NA. The second group contained an active site mAb, FluB-400, that broadly inhibited IBV NA sialidase activity and virus replication in vitro in primary human respiratory epithelial cell cultures and protected against IBV in vivo when administered systemically or intranasally. Overall, the findings described here shape our mechanistic understanding of the human immune response to the IBV NA glycoprotein through the demonstration of two mAb delivery routes for protection against IBV and the identification of potential IBV therapeutic candidates. PubMed: 38823390DOI: 10.1016/j.immuni.2024.05.002 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.89 Å) |
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