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DOI | 10.1126/science.aao1140 |
The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion | |
Tenthorey, Jeannette L.1; Haloupek, Nicole1; Ramon Lopez-Blanco, Jose2; Grob, Patricia3; Adamson, Elise1,4; Hartenian, Ella1; Lind, Nicholas A.1; Bourgeois, Natasha M.1; Chacon, Pablo2; Nogales, Eva1,3,5; Vance, Russell E.1,3,6,7 | |
2017-11-17 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 358期号:6365页码:888-+ |
文章类型 | Article |
语种 | 英语 |
国家 | USA; Spain |
英文摘要 | Robust innate immune detection of rapidly evolving pathogens is critical for host defense. Nucleotide-binding domain leucine-rich repeat (NLR) proteins function as cytosolic innate immune sensors in plants and animals. However, the structural basis for ligand-induced NLR activation has so far remained unknown. NAIP5 (NLR family, apoptosis inhibitory protein 5) binds the bacterial protein flagellin and assembleswithNLRC4 to form amultiprotein complex called an inflammasome. Here we report the cryo-electron microscopy structure of the assembled similar to 1.4-megadalton flagellin-NAIP5-NLRC4 inflammasome, revealing how a ligand activates an NLR. Six distinct NAIP5 domains contact multiple conserved regions of flagellin, prying NAIP5 into an open and active conformation. We show that innate immune recognition of multiple ligand surfaces is a generalizable strategy that limits pathogen evolution and immune escape. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000415293000038 |
WOS关键词 | BACTERIAL LIGANDS ; TERMINAL REGIONS ; RECOGNITION ; NLRC4 ; ACTIVATION ; RECEPTORS ; FILAMENT ; REVEALS ; PROTEIN ; SYSTEM |
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/197346 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Calif Berkeley, Dept Mol & Cell Biol, 229 Stanley Hall, Berkeley, CA 94720 USA; 2.CSIC, Inst Quim Fis Rocasolano, Dept Quim Fis Biol, Madrid 28006, Spain; 3.Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA; 4.Univ Maryland Baltimore Cty, Baltimore, MD 21250 USA; 5.Lawrence Berkeley Natl Lab, Mol Biophys & Integrat Bioimaging Div, Berkeley, CA 94720 USA; 6.Univ Calif Berkeley, Canc Res Lab & Immunotherapeut, Berkeley, CA 94720 USA; 7.Univ Calif Berkeley, Vaccine Res Initiat, Berkeley, CA 94720 USA |
推荐引用方式 GB/T 7714 | Tenthorey, Jeannette L.,Haloupek, Nicole,Ramon Lopez-Blanco, Jose,et al. The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion[J]. SCIENCE,2017,358(6365):888-+. |
APA | Tenthorey, Jeannette L..,Haloupek, Nicole.,Ramon Lopez-Blanco, Jose.,Grob, Patricia.,Adamson, Elise.,...&Vance, Russell E..(2017).The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion.SCIENCE,358(6365),888-+. |
MLA | Tenthorey, Jeannette L.,et al."The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion".SCIENCE 358.6365(2017):888-+. |
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