期刊
NATURE MICROBIOLOGY
卷 2, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nmicrobiol.2016.191
关键词
-
类别
资金
- Basic Science Research Program through National Research Foundation of Korea (NRF) - Ministry of Education [2010-0012505]
- Bio-Synergy/research Project [2014M3A9C4066465]
- Global Frontier Project of the National Research Foundation [NRF-M3A6A4-2010-0029785, 2015M3A6A4065732]
- Ministry of Science, ICT & Future Planning (MSIP) of Korea
- National Research Foundation of Korea [2010-0012505, 2015M3A6A4065732] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The N-terminal truncated form of a protein synthesis enzyme, tryptophanyl-tRNA synthetase (mini-WRS), is secreted as an angiostatic ligand. However, the secretion and function of the full-length WRS (FL-WRS) remain unknown. Here, we report that the FL-WRS, but not mini-WRS, is rapidly secreted upon pathogen infection to prime innate immunity. Blood levels of FL-WRS were increased in sepsis patients, but not in those with sterile inflammation. FL-WRS was secreted from monocytes and directly bound to macrophages via a toll-like receptor 4 (TLR4)-myeloid differentiation factor 2 (MD2) complex to induce phagocytosis and chemokine production. Administration of FL-WRS into Salmonella typhimurium-infected mice reduced the levels of bacteria and improved mouse survival, whereas its titration with the specific antibody aggravated the infection. The N-terminal 154-amino-acid eukaryote-specific peptide of WRS was sufficient to recapitulate FL-WRS activity and its interaction mode with TLR4-MD2 is now suggested. Based on these results, secretion of FL-WRS appears to work as a primary defence system against infection, acting before full activation of innate immunity.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据