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DOI | 10.1038/s41467-019-12167-9 |
Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope | |
Rouvinski, Alexander1,2,7; Dejnirattisai, Wanwisa3; Guardado-Calvo, Pablo1,2; Vaney, Marie-Christine1,2; Sharma, Arvind1,2; Duquerroy, Stephane1,2,4; Supasa, Piyada3; Wongwiwat, Wiyada3; Haouz, Ahmed5; Barba-Spaeth, Giovanna1,2; Mongkolsapaya, Juthathip3,6; Rey, Felix A.1,2; Screaton, Gavin R.3 | |
2019-09-19 | |
发表期刊 | NATURE COMMUNICATIONS
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ISSN | 2041-1723 |
出版年 | 2017 |
卷号 | 8 |
文章类型 | Article |
语种 | 英语 |
国家 | France; England; Thailand; Israel |
英文摘要 | A problem in the search for an efficient vaccine against dengue virus is the immunodominance of the fusion loop epitope (FLE), a segment of the envelope protein E that is buried at the interface of the E dimers coating mature viral particles. Anti-FLE antibodies are broadly cross-reactive but poorly neutralizing, displaying a strong infection enhancing potential. FLE exposure takes place via dynamic 'breathing' of E dimers at the virion surface. In contrast, antibodies targeting the E dimer epitope (EDE), readily exposed at the E dimer interface over the region of the conserved fusion loop, are very potent and broadly neutralizing. We here engineer E dimers locked by inter-subunit disulfide bonds, and show by X-ray crystallography and by binding to a panel of human antibodies that these engineered dimers do not expose the FLE, while retaining the EDE exposure. These locked dimers are strong immunogen candidates for a next-generation vaccine. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000401848600001 |
WOS关键词 | ANTIBODY-DEPENDENT ENHANCEMENT ; ZIKA VIRUS ; MACROMOLECULAR CRYSTALLOGRAPHY ; NEUTRALIZING ANTIBODIES ; CROSS-NEUTRALIZATION ; MONOCLONAL-ANTIBODY ; STRUCTURAL BASIS ; HIGHLY POTENT ; SEROTYPE 3 ; INFECTION |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/204549 |
专题 | 资源环境科学 |
作者单位 | 1.Inst Pasteur, Dept Virol, Unite Virol Struct, F-75724 Paris 15, France; 2.CNRS UMR Virol 3569, F-75724 Paris 15, France; 3.Imperial Coll London, Dept Med, Div Immunol & Inflammat, Hammersmith Hosp Campus, London W12 0NN, England; 4.Univ Paris 11, Fac Sci, F-91405 Orsay, France; 5.Inst Pasteur, Proteopole, CNRS UMR 3528, F-75724 Paris 15, France; 6.Mahidol Univ, Siriraj Hosp, Off Res & Dev, Dengue Haemorrhag Fever Res Unit,Fac Med, Bangkok 10700, Thailand; 7.Hebrew Univ Jerusalem, Hebrew Univ Hadassah Med Sch, Inst Med Res Israel Canada, Dept Microbiol & Mol Genet,Kuvin Ctr Study Infect, Jerusalem, Israel |
推荐引用方式 GB/T 7714 | Rouvinski, Alexander,Dejnirattisai, Wanwisa,Guardado-Calvo, Pablo,et al. Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope[J]. NATURE COMMUNICATIONS,2019,8. |
APA | Rouvinski, Alexander.,Dejnirattisai, Wanwisa.,Guardado-Calvo, Pablo.,Vaney, Marie-Christine.,Sharma, Arvind.,...&Screaton, Gavin R..(2019).Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope.NATURE COMMUNICATIONS,8. |
MLA | Rouvinski, Alexander,et al."Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope".NATURE COMMUNICATIONS 8(2019). |
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