Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing Epitopes.

Abstract:
:Respiratory syncytial virus (RSV) is a top cause of severe lower respiratory tract disease and mortality in infants and the elderly. Currently, no vaccine or effective treatment exists for RSV. The RSV G glycoprotein mediates viral attachment to cells and contributes to pathogenesis by modulating host immunity through interactions with the human chemokine receptor CX3CR1. Antibodies targeting the RSV G central conserved domain are protective in both prophylactic and postinfection animal models. Here, we describe the crystal structure of the broadly neutralizing human monoclonal antibody 3G12 bound to the RSV G central conserved domain. Antibody 3G12 binds to a conformational epitope composed of highly conserved residues, explaining its broad neutralization activity. Surprisingly, RSV G complexed with 3G12 adopts a distinct conformation not observed in previously described RSV G-antibody structures. Comparison to other structures reveals that the RSV G central conserved domain is flexible and can adopt multiple conformations in the regions flanking the cysteine noose. We also show that restriction of RSV G flexibility with a proline mutation abolishes binding to antibody 3G12 but not antibody 3D3, which recognizes a different conformation of RSV G. Our studies provide new insights for rational vaccine design, indicating the importance of preserving both the global structural integrity of antigens and local conformational flexibility at antigenic sites, which may elicit a more diverse antibody response and broader protection against infection and disease.IMPORTANCE Respiratory syncytial virus (RSV) causes severe respiratory infections in infants, young children, and the elderly, and currently, no licensed vaccine exists. In this study, we describe the crystal structure of the RSV surface glycoprotein G in complex with a broadly neutralizing human monoclonal antibody. The antibody binds to RSV G at a highly conserved region stabilized by two disulfide bonds, but it captures RSV G in a conformation not previously observed, revealing that this region is both structured and flexible. Importantly, our findings provide insight for the design of vaccines that elicit diverse antibodies, which may provide broad protection from infection and disease.
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JOURNAL OF VIROLOGY
J VIROL
最新影响因子:6.549 | 期刊ISSN:0022-538X | CiteScore:4.24 |
出版周期:Semimonthly | 是否OA:YES | 出版年份:1967 |
期刊官方网址:http://jvi.asm.org/
自引率:12.30% | 研究方向:医学-病毒学 |
出版地区:UNITED STATES |
SCI期刊coverage:Science Citation Index Expanded(科学引文索引扩展)
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JOURNAL OF VIROLOGY 期刊简介
英文简介:
The Journal of Virology is the best source of broad-based, high-quality, original research concerning viruses. The journal provides fundamental new information using cross-disciplinary approaches of biochemistry, biophysics, cell biology, genetics, immunology, molecular biology, morphology, physiology, and pathogenesis and immunity.
中文简介:(来自Google、百度翻译)
《病毒学杂志》是关于病毒的基础广泛、高质量、原始研究的最佳来源。该杂志利用生物化学、生物物理学、细胞生物学、遗传学、免疫学、分子生物学、形态学、生理学、发病机制和免疫学等跨学科方法提供了基本的新信息。
JOURNAL OF VIROLOGY 期刊中科院评价数据
最新中科院分区
大类(学科) | 小类(学科) | 学科排名 |
医学 |
VIROLOGY(病毒学) 2区 |
8/35 |
最新公布的期刊年发文量
年度总发文量 | 年度论文发表量 | 年度综述发表量 |
850 | 844 | 6 |
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JOURNAL OF VIROLOGY 期刊CiteScore评价数据
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引文计数(2018)
文献(2015-2017)
14616次引用
3447篇文献
CiteScore排名
序号 | 类别 | 排名 | 百分位 |
1 |
大类(学科):Immunology and Microbiology
小类(学科):Microbiology
|
#20/135
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2 |
大类(学科):Immunology and Microbiology
小类(学科):Immunology
|
#39/193
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3 |
大类(学科):Agricultural and Biological Sciences
小类(学科):Insect Science
|
#2/136
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4 |
大类(学科):Immunology and Microbiology
小类(学科):Virology
|
#14/68
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liting7111
研究方向:生命科学 兽医学 兽医免疫学
审稿时间: 1个月内
编辑效率很高,就算拒稿反馈也很快,如果有修改机会一般20天就给消息,我投稿已经接受,感谢编辑!2020-02-16 -
liting7111
研究方向:生命科学 微生物学 病原真菌学
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本专业很不错的期刊,今年影响因子终于止住了跌势。2019-09-13 -
liting7111
研究方向:病毒学 免疫学
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一审20天,给了小修,提的问题很难回答,好在文章比较新颖,修回三天就接收。2019-05-26 -
liting7111
研究方向:病毒 结构生物学
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今年投稿两篇,第一篇拒稿,修改后再投就接收了。2019-02-03
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