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-Structure paper
タイトル | Potent human neutralizing antibodies against Nipah virus derived from two ancestral antibody heavy chains. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 2987, Year 2024 |
掲載日 | 2024年4月6日 |
著者 | Li Chen / Mengmeng Sun / Huajun Zhang / Xinghai Zhang / Yanfeng Yao / Ming Li / Kangyin Li / Pengfei Fan / Haiwei Zhang / Ye Qin / Zhe Zhang / Entao Li / Zhen Chen / Wuxiang Guan / Shanshan Li / Changming Yu / Kaiming Zhang / Rui Gong / Sandra Chiu / |
PubMed 要旨 | Nipah virus (NiV) is a World Health Organization priority pathogen and there are currently no approved drugs for clinical immunotherapy. Through the use of a naïve human phage-displayed Fab library, ...Nipah virus (NiV) is a World Health Organization priority pathogen and there are currently no approved drugs for clinical immunotherapy. Through the use of a naïve human phage-displayed Fab library, two neutralizing antibodies (NiV41 and NiV42) targeting the NiV receptor binding protein (RBP) were identified. Following affinity maturation, antibodies derived from NiV41 display cross-reactivity against both NiV and Hendra virus (HeV), whereas the antibody based on NiV42 is only specific to NiV. Results of immunogenetic analysis reveal a correlation between the maturation of antibodies and their antiviral activity. In vivo testing of NiV41 and its mature form (41-6) show protective efficacy against a lethal NiV challenge in hamsters. Furthermore, a 2.88 Å Cryo-EM structure of the tetrameric RBP and antibody complex demonstrates that 41-6 blocks the receptor binding interface. These findings can be beneficial for the development of antiviral drugs and the design of vaccines with broad spectrum against henipaviruses. |
リンク | Nat Commun / PubMed:38582870 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.88 Å |
構造データ | EMDB-36849, PDB-8k3c: |
由来 |
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キーワード | VIRAL PROTEIN/IMMUNE SYSTEM / Nipah virus / Attachment glycoprotein / tetramer complex / Neutralizing antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex |