1. 尼帕病毒概述：起源、演化與全球流行病學(xué)風(fēng)險
尼帕病毒（Nipah virus, NiV）自1998年在馬來西亞暴發(fā)以來，被公認(rèn)為一種具有高致死率和顯著跨物種傳播能力的人畜共患病毒。該單股負(fù)鏈 RNA 病毒以果蝠（尤其是狐蝠屬 Pteropus）為天然宿主，可經(jīng)由中間宿主（如豬）或直接暴露傳播至人類，并在不同地理區(qū)域形成了穩(wěn)定的遺傳分化。系統(tǒng)發(fā)育研究表明，NiV主要分為孟加拉譜系（NiV-B）和馬來西亞譜系（NiV-M），反映了病毒在區(qū)域性蝙蝠種群中的長期演化過程 [1]。
在跨物種傳播過程中，病毒對人類受體的分子適應(yīng)性是決定其外溢風(fēng)險的關(guān)鍵因素。研究發(fā)現(xiàn)，NiV G 蛋白在受體結(jié)合區(qū)域承受明顯選擇壓力，其中498位點(diǎn)的變異可調(diào)節(jié)其與人源 ephrin-B2 受體的親和力，從而促進(jìn)病毒實(shí)現(xiàn)宿主跳躍 [1]。此外，L 蛋白連接結(jié)構(gòu)域中1645位點(diǎn)的正向選擇特征，提示病毒復(fù)制與加帽過程亦參與了宿主適應(yīng)性調(diào)控。
NiV 的流行風(fēng)險與其自然宿主的生態(tài)分布高度重合。生態(tài)位建模顯示，南亞和東南亞約有 19%（約296萬 km^2）的區(qū)域處于高風(fēng)險覆蓋范圍內(nèi) [2]。長期血清學(xué)監(jiān)測表明，NiV 在野生狐蝠種群中以持續(xù)循環(huán)形式存在，個體抗體水平呈動態(tài)變化。病毒在蝙蝠體內(nèi)的周期性再排毒（recrudescence）被認(rèn)為是維持群體內(nèi)傳播并引發(fā)人類偶發(fā)感染的重要機(jī)制，而母源抗體雖可提供短期保護(hù)，但不足以阻斷病毒的長期存在 [3]。
在人群中，NiV 感染通常表現(xiàn)出極高病死率。以2018年印度喀拉拉邦疫情為例，其病死率高達(dá) 1%，凸顯了該病毒的嚴(yán)重公共衛(wèi)生威脅 [4]。體外研究進(jìn)一步表明，NiV 在人呼吸道上皮細(xì)胞中的復(fù)制效率顯著高于豬源細(xì)胞，這一差異與 ephrin-B2 受體表達(dá)水平密切相關(guān) [5]。相比之下，同屬亨尼帕病毒的錫達(dá)病毒（Cedar virus）雖同樣利用 ephrin-B2 進(jìn)入細(xì)胞，但由于缺乏關(guān)鍵免疫逃逸因子，在動物模型中致病性明顯降低 [6]。這一對比為理解 NiV 高致病性的分子基礎(chǔ)提供了重要線索，并為后續(xù)結(jié)構(gòu)與干預(yù)研究奠定了基礎(chǔ)。
2. 分子結(jié)構(gòu)基礎(chǔ)：受體識別與膜融合觸發(fā)
2.1 表面糖蛋白 G 與 F 的協(xié)同作用機(jī)制
尼帕病毒侵染宿主細(xì)胞的起始步驟依賴于其包膜表面兩種關(guān)鍵糖蛋白——受體結(jié)合蛋白 G 與融合蛋白 F 的高度協(xié)同。與多數(shù)副黏病毒不同，NiV-G 蛋白不具備血凝素或神經(jīng)氨酸酶活性，而是通過高度特異性的蛋白-蛋白相互作用識別宿主細(xì)胞表面的 ephrin-B2 或 ephrin-B3 受體。
結(jié)構(gòu)生物學(xué)研究表明，NiV-G 蛋白的受體結(jié)合域呈現(xiàn)典型的六葉 β-螺旋槳結(jié)構(gòu)。在復(fù)合物中，ephrin-B2/B3 的環(huán)狀結(jié)構(gòu)插入 G 蛋白中央凹槽，形成廣泛的相互作用界面，其中 ephrin-B2 的 Trp122 殘基發(fā)揮“插銷”式關(guān)鍵作用，顯著增強(qiáng)結(jié)合親和力 [7,8]。深度突變掃描結(jié)果進(jìn)一步顯示，G 蛋白界面殘基（如 Y228H）的改變可通過調(diào)節(jié)復(fù)合體穩(wěn)定性與柔性，顯著影響病毒入侵效率 [9,10]。
受體結(jié)合并非終點(diǎn)，而是觸發(fā)膜融合的分子開關(guān)。ephrin 結(jié)合后，G 蛋白頭部構(gòu)象發(fā)生重排，該信號沿莖部傳遞，誘導(dǎo)處于預(yù)融合態(tài)（pre-fusion）的 F 蛋白發(fā)生不可逆構(gòu)象轉(zhuǎn)變 [8]。NiV-F 蛋白在預(yù)融合狀態(tài)下以獨(dú)特的“六聚體-三聚體（hexamer-of-trimers）”形式組裝，這一高級結(jié)構(gòu)被認(rèn)為有助于穩(wěn)定能量較高的預(yù)融合構(gòu)象，并在觸發(fā)時協(xié)同降低融合孔形成的能壘 [11]。
研究工具：
2.2 F 蛋白的構(gòu)象調(diào)控與膜環(huán)境依賴性
F 蛋白胞質(zhì)尾部在融合調(diào)控中發(fā)揮“由內(nèi)而外”的信號作用。其近膜區(qū)的 KKR 基序被證實(shí)是融合效率的關(guān)鍵調(diào)控元件：不同殘基突變對融合活性產(chǎn)生相反影響，并通過調(diào)節(jié)胞外結(jié)構(gòu)域穩(wěn)定性影響六螺旋束（6HB）的形成速率 [13]。此外，K2 殘基對于 F 蛋白進(jìn)入脂質(zhì)筏區(qū)域至關(guān)重要，揭示了空間定位與功能激活之間的內(nèi)在聯(lián)系。
N-糖基化修飾同樣在維持蛋白功能與免疫逃逸中扮演重要角色。NiV-G 蛋白的多糖基化位點(diǎn)可通過空間遮蔽限制中和抗體識別 [15]。與此同時，宿主因子如半乳糖凝集素-1（Galectin-1）可結(jié)合 F 蛋白糖鏈，抑制其構(gòu)象轉(zhuǎn)變，從而在宿主防御層面阻斷膜融合 [16]。
研究工具：
3. 病毒復(fù)制機(jī)器：復(fù)制酶復(fù)合物與核衣殼
尼帕病毒的基因組復(fù)制與轉(zhuǎn)錄由高度復(fù)雜的復(fù)制酶系統(tǒng)驅(qū)動，其核心是由大蛋白 L 與磷蛋白 P 構(gòu)成的 L-P 復(fù)合物。冷凍電鏡研究揭示，L 蛋白整合了 RNA 依賴性 RNA 聚合酶（RdRp）、PRNTase 及甲基轉(zhuǎn)移酶等多個功能模塊，而 P 蛋白則以四聚化螺旋束形式維持整體結(jié)構(gòu)穩(wěn)定性 [17-19]。
NiV-L 蛋白中存在一段在其他非分節(jié)段負(fù)鏈 RNA 病毒中較少見的長插入結(jié)構(gòu)，其在調(diào)控復(fù)制與轉(zhuǎn)錄平衡中發(fā)揮關(guān)鍵作用 [19]。P 蛋白的 XD 鏈接子獨(dú)特地錨定于核苷酸入口通道區(qū)域，這種構(gòu)象安排被認(rèn)為可精細(xì)調(diào)控底物進(jìn)入與 RNA 合成起始 [17]。
在核衣殼層面，基因組 RNA 被 N 蛋白包裹形成 α-螺旋結(jié)構(gòu)。N-P 相互作用高度依賴內(nèi)在無序區(qū)域（IDRs），其高度柔性有助于病毒在細(xì)胞內(nèi)復(fù)雜環(huán)境中實(shí)現(xiàn)高效復(fù)制 [23]。超分辨顯微研究提出的隨機(jī)組裝模型進(jìn)一步指出，病毒復(fù)制與裝配并非完全線性過程，而是具備一定隨機(jī)性 [24]。
研究工具：
4. 宿主相互作用與免疫逃逸機(jī)制
NiV 的高致死性在很大程度上源于其高度精密的先天免疫逃逸策略，其中由 P 基因編碼的 W 蛋白發(fā)揮核心作用。W 蛋白通過與 Importin-α3 的高親和力結(jié)合，競爭性阻斷 STAT1 等關(guān)鍵轉(zhuǎn)錄因子的核轉(zhuǎn)運(yùn)，從而抑制干擾素信號通路 [25]。
結(jié)構(gòu)研究顯示，W 蛋白 C 端結(jié)構(gòu)域可通過二硫鍵形成二聚體，并誘導(dǎo)其 N 端無序區(qū)域發(fā)生由無序向有序的構(gòu)象轉(zhuǎn)換，甚至形成類淀粉樣結(jié)構(gòu) [26]。這一特性被認(rèn)為可能與病毒在宿主細(xì)胞內(nèi)的長期存續(xù)及致病性增強(qiáng)相關(guān)。
在自然宿主層面，這種免疫逃逸策略轉(zhuǎn)化為病毒在蝙蝠體內(nèi)的潛伏與復(fù)發(fā)特征，即便在存在血清抗體的情況下仍可發(fā)生周期性排毒 [3]。此外，不同宿主中 ephrin-B2 表達(dá)水平的差異，進(jìn)一步塑造了感染效率與組織趨向性 [5]。
研究工具：
5. 臨床前研究模型與評價體系
由于 NiV 需在 BSL-4 條件下操作，開發(fā)安全、可替代的評價模型至關(guān)重要。雪貂模型因高度模擬人類呼吸道與神經(jīng)系統(tǒng)病理，被廣泛用于治療性抗體和疫苗驗(yàn)證 [27]。人肺異種移植小鼠模型則在解析人類特異性肺損傷機(jī)制方面展現(xiàn)獨(dú)特優(yōu)勢 [28]。
在低生物安全等級體系中，基于 HIV 骨架的 NiV-F/G 偽病毒系統(tǒng)可在 BSL-2 條件下評估中和抗體效價 [29]；而基于雪松病毒的嵌合病毒平臺在生物學(xué)相關(guān)性與安全性之間取得良好平衡 [30]。類病毒顆粒（VLPs）則兼具免疫原展示與機(jī)制研究價值 [31]。
6. 治療干預(yù)：疫苗策略與中和抗體
結(jié)構(gòu)生物學(xué)驅(qū)動的抗原設(shè)計已成為 NiV 疫苗研發(fā)的核心方向。穩(wěn)定態(tài)預(yù)融合 F 蛋白（pre-F）因保留關(guān)鍵中和表位，被證實(shí)具有顯著優(yōu)于后融合構(gòu)象的免疫原性 [32]。與 G 蛋白組合或形成嵌合抗原，可進(jìn)一步拓展抗體譜系 [32,33]。
在治療性抗體方面，靶向 F 蛋白 pre-fusion 構(gòu)象的 hu1F5 在非人靈長類模型中展現(xiàn)出顯著優(yōu)于 m102.4 的后暴露保護(hù)效果 [34]。F 蛋白膜遠(yuǎn)端結(jié)構(gòu)域（DIII）被識別為關(guān)鍵脆弱位點(diǎn)，因其功能約束強(qiáng)、逃逸突變風(fēng)險低，成為廣譜干預(yù)的重要靶標(biāo) [35]。
7. 推薦產(chǎn)品
重組蛋白：
● 尼帕病毒蛋白
| Code | Product Name | Source |
|---|---|---|
| CSB-MP862323NDT | Recombinant Nipah virus Glycoprotein G (G)-VLPs | Mammalian cell |
| CSB-CF862323NDT | Recombinant Nipah virus Glycoprotein G (G) | in vitro E.coli expression system |
| CSB-MP884868NDT | Recombinant Nipah virus Fusion glycoprotein F0 (F), partial | Mammalian cell |
| CSB-MP860779NDT | Recombinant RNA-directed RNA polymerase L (L), partial | Mammalian cell |
| CSB-MP878021NDT | Recombinant Phosphoprotein (P/V/C), partial | Mammalian cell |
| CSB-MP313495NDT | Recombinant Protein W (P/V/C) | Mammalian cell |
● 受體蛋白或相關(guān)研究蛋白
| Code | Product Name | Source |
|---|---|---|
| CSB-MP007730HU | Recombinant Human Ephrin type-B receptor 2 (EPHB2), partial | Mammalian cell |
| CSB-MP007731HU | Recombinant Human Ephrin type-B receptor 3 (EPHB3), partial | Mammalian cell |
| CSB-EP012882HU | Recombinant Human Galectin-1 (LGALS1) | E.coli |
| CSB-MP012485HU | Recombinant Human Importin subunit alpha-3 (KPNA3) | Mammalian cell |
| CSB-EP022810HU | Recombinant Human Signal transducer and activator of transcription 1-alpha/beta (STAT1) | E.coli |
如需其他尼帕病毒相關(guān)產(chǎn)品或試劑盒，請聯(lián)系我們
[1] Kemang Li, Shiyu Yan, Ningning Wang, Wanting He, Haifei Guan, Chengxi He, Zhixue Wang, Meng Lu, Wei He, Rui Ye, Michael Veit, Shuo Su.(2019). Emergence and adaptive evolution of Nipah virus.
[2] Mark A. Deka, Niaz Morshed.(2018). Mapping Disease Transmission Risk of Nipah Virus in South and Southeast Asia.
[3] A. R. Sohayati, Latiffah Hassan, Sharifah Syed Hassan, Karen Lazarus, C M Zaini, Jonathan H. Epstein, Norris Naim, Hume Field, Siti Suri Arshad, Jazli Aziz, Peter Daszak, EcoHealth Alliance.(2011). Evidence for Nipah virus recrudescence and serological patterns of captivePteropus vampyrus.
[4] Rima R. Sahay, Pragya D. Yadav, Nivedita Gupta, Anita M. Shete, Chandni Radhakrishnan, Ganesh Mohan, Nikhilesh Menon, Tarun Bhatnagar, Krishnasastry Suma, Abhijeet Kadam, Padinjaremattathil Thankappan Ullas, Brijesh Kumar, AP Sugunan, V. K. Sreekala, Rajan Khobragade, Raman Gangakhedkar, Devendra T. Mourya.(2020). Experiential learnings from the Nipah virus outbreaks in Kerala towards containment of infectious public health emergencies in India.
[5] Lucie Sauerhering, Martin Zickler, Mareike Elvert, Laura Behner, Tatyana Matrosovich, Stephanie Erbar, Mikhail Matrosovich, Andrea Maisner.(2016). Species-specific and individual differences in Nipah virus replication in porcine and human airway epithelial cells.
[6] Glenn A. Marsh, Carol de Jong, Jennifer Barr, Mary Tachedjian, Craig Smith, Deborah Middleton, Meng Yu, Shawn Todd, Adam J. Foord, Volker H?ring, Jean Payne, Rachel Robinson, Ivano Broz, Gary Crameri, Hume Field, Lin‐Fa Wang.(2012). Cedar Virus: A Novel Henipavirus Isolated from Australian Bats.
[7] Kai Xu, Kanagalaghatta R. Rajashankar, Yee‐Peng Chan, Juha P. Himanen, Christopher C. Broder, Dimitar B. Nikolov.(2008). Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3.
[8] Kai Xu, Yee‐Peng Chan, Kanagalaghatta R. Rajashankar, Dimple Khetawat, Lianying Yan, Momchil V. Kolev, Christopher C. Broder, Dimitar B. Nikolov.(2012). New Insights into the Hendra Virus Attachment and Entry Process from Structures of the Virus G Glycoprotein and Its Complex with Ephrin-B2.
[9] Brendan B. Larsen, Teagan E. McMahon, Jack T Brown, Zhaoqian Wang, Caelan E. Radford, James E. Crowe, David Veesler, Jesse D. Bloom.(2025). Functional and antigenic landscape of the Nipah virus receptor-binding protein.
[10] Emre Akta?, ?rem Sayg?l?, E. Kahveci, Zeynep Tekb?y?k, Nehir ?zdemir ?zgentürk.(2023). Bioinformatic investigation of Nipah virus surface protein mutations: Molecular docking with Ephrin B2 receptor, molecular dynamics simulation, and structural impact analysis.
[11] Kai Xu, Yee‐Peng Chan, Birgit Bradel-Tretheway, Zeynep Akyol-Ataman, Yongqun Zhu, Somnath Dutta, Lianying Yan, YanRu Feng, Lin‐Fa Wang, Georgios Skiniotis, Benhur Lee, Z. Hong Zhou, Christopher C. Broder, Hector C. Aguilar, Dimitar B. Nikolov.(2015). Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly.
[12] Sofia Cheliout Da Silva, Lianying Yan, Ha V. Dang, Kai Xu, Jonathan H. Epstein, David Veesler, Christopher C. Broder.(2021). Functional Analysis of the Fusion and Attachment Glycoproteins of Mojiang Henipavirus.
[13] Hector C. Aguilar, Kenneth A. Matreyek, Daniel Choi, Claire Marie Filone, Sophia Young, Benhur Lee.(2007). Polybasic KKR Motif in the Cytoplasmic Tail of Nipah Virus Fusion Protein Modulates Membrane Fusion by Inside-Out Signaling.
[14] Michael Weis, Laura Behner, Markus Hoffmann, Nadine Krüger, Georg Herrler, Christian Drosten, Jan Felix Drexler, Erik Dietzel, Andrea Maisner.(2013). Characterization of African bat henipavirus GH-M74a glycoproteins.
[15] Birgit Bradel-Tretheway, Qian Liu, Jacquelyn A. Stone, Samantha McInally, Hector C. Aguilar.(2015). Novel Functions of Hendra Virus G N-Glycans and Comparisons to Nipah Virus.
[16] Omai B. Garner, Hector C. Aguilar, Jennifer A. Fulcher, Ernest L. Levroney, Rebecca A. Harrison, Lacey Wright, Lindsey R. Robinson, Vanessa Aspericueta, Maria Panico, Stuart M. Haslam, Howard R. Morris, Anne Dell, Benhur Lee, Linda G. Baum.(2010). Endothelial Galectin-1 Binds to Specific Glycans on Nipah Virus Fusion Protein and Inhibits Maturation, Mobility, and Function to Block Syncytia Formation.
[17] Xue Lu, Tiancai Chang, Jiawei Gui, Zimu Li, Heyu Zhao, B. S. Zou, Junnan Lu, Mei Li, Xin Wen, Shenghua Gao, Shujing Xu, Lijun Rong, Liqiang Feng, Peng Gong, Jun He, Xinwen Chen, Xiaoli Xiong.(2025). Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.
[18] Jonathan M. Grimes, Franziska Günl, Lo?c Carrique, J.R. Keown, Ervin Fodor, Ervin Fodor.(2024). Structure of the Nipah virus polymerase complex.
[19] Side Hu, Heesu Kim, Pan Yang, Zishuo Yu, Barbara Ludeke, Shawna Mobilia, Junhua Pan, Margaret M. Stratton, Yuemin Bian, Rachel Fearns, Jonathan Abraham.(2024). Structural and functional analysis of the Nipah virus polymerase complex.
[20] F. Sala, Katja Ditter, Olexandr Dybkov, Henning Urlaub, Hauke S. Hillen.(2025). Structural basis of Nipah virus RNA synthesis.
[21] Paul C. Jordan, Cheng Liu, Pauline Raynaud, Michael K. Lo, Christina F. Spiropoulou, Julian Symons, Leo Beigelman, Jér?me Deval.(2018). Initiation, extension, and termination of RNA synthesis by a paramyxovirus polymerase.
[22] Jin Xie, Mohamed Ouizougun-Oubari, Li Wang, Guanglei Zhai, Daitze Wu, Zhaohu Lin, Manfu Wang, Barbara Ludeke, Xiaodong Yan, Tobias Nilsson, Lu Gao, Xinyi Huang, Rachel Fearns, Shuai Chen.(2024). Structural basis for dimerization of a paramyxovirus polymerase complex.
[23] Johnny Habchi, Laurent Mamelli, Hervé Darbon, Sonia Longhi.(2010). Structural Disorder within Henipavirus Nucleoprotein and Phosphoprotein: From Predictions to Experimental Assessment.
[24] Qian Liu, Lei Chen, Hector C. Aguilar, Keng C. Chou.(2018). A stochastic assembly model for Nipah virus revealed by super-resolution microscopy.
[25] K.M. Smith, S. Tsimbalyuk, Megan R. Edwards, E.M. Cross, Jyoti Batra, Tatiana P. Soares da Costa, David Arag?o, Christopher F. Basler, Jade K. Forwood.(2018). Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses.
[26] Giulia Pesce, Frank Gondelaud, Denis Ptchelkine, Christophe Bignon, Patrick Fourquet, Sonia Longhi.(2024). DissectingHenipavirusW proteins conformational and fibrillation properties: contribution of their N‐ and C‐terminal constituent domains.
[27] Katharine N. Bossart, Zhongyu Zhu, Deborah Middleton, Jessica Klippel, Gary Crameri, John Bingham, Jennifer A. McEachern, Diane Green, Timothy J. Hancock, Yee‐Peng Chan, Andrew C. Hickey, Dimiter S. Dimitrov, Lin‐Fa Wang, Christopher C. Broder.(2009). A Neutralizing Human Monoclonal Antibody Protects against Lethal Disease in a New Ferret Model of Acute Nipah Virus Infection.
[28] Gustavo Valbuena, Hailey Halliday, Viktoriya Borisevich, Yenny Góez, Barry Rockx.(2014). A Human Lung Xenograft Mouse Model of Nipah Virus Infection.
[29] Jianhui Nie, Lin Liu, Qing Wang, Ruifeng Chen, Tingting Ning, Qiang Liu, Weijin Huang, Youchun Wang.(2019). Nipah pseudovirus system enables evaluation of vaccinesin vitroandin vivousing non-BSL-4 facilities.
[30] Moushimi Amaya, Randy Yin, Lianying Yan, Viktoriya Borisevich, Bishwo N. Adhikari, Andrew J. Bennett, Francisco Malagón, Regina Z. Cer, Kimberly A. Bishop‐Lilly, Antony S. Dimitrov, Robert W. Cross, Thomas W. Geisbert, Christopher C. Broder.(2023). A Recombinant Chimeric Cedar Virus-Based Surrogate Neutralization Assay Platform for Pathogenic Henipaviruses.
[31] Lori W. McGinnes, Homer Pantua, Jason P. Laliberte, Kathryn A. Gravel, Surbhi Jain, Trudy G. Morrison.(2010). Assembly and Biological and Immunological Properties of Newcastle Disease Virus-Like Particles.
[32] Rebecca J. Loomis, Guillaume B. E. Stewart-Jones, Yaroslav Tsybovsky, Ria T. Caringal, Kaitlyn M. Morabito, Jason S. McLellan, Amy L. Chamberlain, Sean Nugent, Geoffrey B. Hutchinson, Lisa A. Kueltzo, John R. Mascola, Barney S. Graham.(2020). Structure-Based Design of Nipah Virus Vaccines: A Generalizable Approach to Paramyxovirus Immunogen Development.
[33] Seo Young Moon, Rochelle A. Flores, Min Su Yim, Heeji Lim, Seung-Yeon Kim, Seung Yun Lee, Yoo-kyoung Lee, Jae‐Ouk Kim, Hyejin Park, Seong Eun Bae, In-Ohk Ouh, Woo Hyun Kim.(2024). Immunogenicity and Neutralization of Recombinant Vaccine Candidates Expressing F and G Glycoproteins against Nipah Virus.
[34] Larry Zeitlin, Robert W. Cross, Courtney Woolsey, Brandyn R. West, Viktoriya Borisevich, Krystle N. Agans, Abhishek N. Prasad, Daniel J. Deer, Lauren Stuart, Maria McCavitt-Malvido, Do H. Kim, James Pettitt, James E. Crowe, Kevin J. Whaley, David Veesler, Antony S. Dimitrov, Dafna M. Abelson, Thomas W. Geisbert, Christopher C. Broder.(2024). Therapeutic administration of a cross-reactive mAb targeting the fusion glycoprotein of Nipah virus protects nonhuman primates.
[35] Victoria A. Avanzato, Kasopefoluwa Y. Oguntuyo, Marina Escalera‐Zamudio, Bernardo Gutiérrez, Michael Golden, Sergei L. Kosakovsky Pond, Rhys Pryce, Thomas S. Walter, Jeffrey Seow, Katie J. Doores, Oliver G. Pybus, Vincent J. Munster, Benhur Lee, Thomas A. Bowden.(2019). A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex.
