设为首页 加入收藏 网站地图  
已发表的论文

浏览模式选择有摘要 无摘要 最简约
 
[1].       
 
Proc Natl Acad Sci USA (Proceedings of the National Academy of the Sciences of the USA). 2014, 111(37): 13469-13474
Two apextrin-like proteins mediate extracellular and intracellular bacterial recognition in amphioxus
Huang G, Huang S, Yan X, Yang P, Li J, Xu W, Zhang L, Wang R, Yu Y, Yuan S, Chen S, Luo G Xu A*.
State Key Laboratory of Biocontrol, Open Laboratory for Marine Functional Genomics of the State High-Tech Development Program, Guangdong Province Key Laboratory for Pharmaceutical Functional Genes, School of Life Sciences, Sun Yat-Sen University, Guangzhou, Guangdong 510006, China Email:lssxal@mail.sysu.edu.cn

Abstract:

Animals exploit different germ-line-encoded proteins with various domain structures to detect the signature molecules of pathogenic microbes. These molecules are known as pathogen-associated molecular patterns (PAMPs), and the host proteins that react with PAMPs are called pattern recognition proteins (PRPs). Here, we present a novel type of protein domain structure capable of binding to bacterial peptidoglycan (PGN) and the minimal PGN motif muramyl dipeptide (MDP). This domain is designated as apextrin C-terminal domain (ApeC), and its presence was confirmed in several invertebrate phyla and subphyla. Two apextrin-like proteins (ALP1 and ALP2) were identified in a basal chordate, the Japanese amphioxus Branchiostoma japonicum (bj). bjALP1 is a mucosal effector secreted into the gut lumen to agglutinate the Gram-positive bacterium Staphylococcus aureus via PGN binding. Neutralization of secreted bjALP1 by anti-bjALP1 monoclonal antibodies caused serious damage to the gut epithelium and rapid death of the animals after bacterial infection. bjALP2 is an intracellular PGN sensor that binds to TNF receptor-associated factor 6 (TRAF6) and prevents TRAF6 from self-ubiquitination and hence from NF-κB activation. MDP was found to compete with TRAF6 for bjALP2, which released TRAF6 to activate the NF-κB pathway. BjALP1 and bjALP2 therefore play distinct and complementary functions in amphioxus gut mucosal immunity. In conclusion, discovery of the ApeC domain and the functional analyses of amphioxus ALP1 and ALP2 allowed us to define a previously undocumented type of PRP that is represented across different animal phyla.
[PMID: 25187559] [ IF( 2014 ): 9.674] Download PDF(this site) Download PDF(origin site)

首页 上一页 下一页 尾页  页次:1/1页  共1条记录 10条记录/页 转到:
关键词:

中山大学医药分子实验室版权所有, 地址: 广东省广州市番禹区大学城中山大学生命科学院
电子邮件:lssxal@mail.sysu.edu.cn, 电话:86-020-39332990,传真: 86-020-39332950,邮编:510006

1023684