您好，欢迎访问山东省农业科学院文献资源数据库平台

Glycosyl-phosphatidylinositol (GPI)-anchored membrane association of the porcine reproductive and respiratory syndrome virus GP4 glycoprotein and its co-localization with CD163 in lipid rafts

文献类型： 外文期刊

作者： Du, Yijun 1 ; Pattnaik, Asit K. 3 ; Song, Cheng 1 ; Yoo, Dongwan 1 ; Li, Gang 1 ;

作者机构： 1.Univ Illinois, Dept Pathobiol, Urbana, IL 61802 USA

2.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Jinan, Peoples R China

3.Univ Nebraska, Sch Vet Med & Biomed Sci, Lincoln, NE 68583 USA

4.Univ Nebraska, Nebraska Ctr Virol, Lincoln, NE 68583 USA

5.Chinese Acad Agr Sci, Inst Anim Sci & Vet Med, Beijing 100193, Peoples R China

关键词： CD163;GP4;GPI;Infectious clone;Lipid rafts;Membrane association;PRRS

期刊名称：VIROLOGY （ 影响因子：3.616； 五年影响因子：3.967 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The porcine reproductive and respiratory syndrome virus (PRRSV) glycoprotein 4 (GP4) resembles a typical type I membrane protein in its structure but lacks a hydrophilic tail at the C-terminus, suggesting that GP4 may be a lipid-anchored membrane protein. Using the human decay-accelerating factor (DAF; CD55), a known glycosyl-phosphatidylinositol (GPI) lipid-anchored protein, chimeric constructs were made to substitute the GPI-anchor domain of DAF with the putative lipid-anchor domain of GP4, and their membrane association and lipase cleavage were determined in cells. The DAF-GP4 fusion protein was transported to the plasma membrane and was cleaved by phosphatidylinositol-specific phospholipase C (PI-PLC), indicating that the C-terminal domain of GP4 functions as a GPI anchor. Mutational studies for residues adjacent to the GPI modification site and characterization of respective mutant viruses generated from infectious cDNA clones show that the ability of GP4 for membrane association corresponded to virus viability and growth characteristics. The residues T158 (ω -2, where ω is the GPI moiety at E160), P159 (ω -1), and M162 (ω + 2) of GP4 were determined to be important for virus replication, with M162 being of particular importance for virus infectivity. The complete removal of the peptide-anchor domain in GP4 resulted in a complete loss of virus infectivity. The depletion of cholesterol from the plasma membrane of cells reduced the virus production, suggesting a role of lipid rafts in PRRSV infection. Remarkably, GP4 was found to co-localize with CD163 in the lipid rafts on the plasma membrane. Since CD163 has been reported as a cellular receptor for PRRSV and GP4 has been shown to interact with this receptor, our data implicates an important role of lipid rafts during entry of the virus.

  • 相关文献

[1]一个猪场高致病性PRRSV的分离鉴定. 任素芳,郭立辉,李为栋,张召坤,李兴光,崔宝玉,吴家强,张玉玉. 2016

[2]Linolelaidic acid induces apoptosis, cell cycle arrest and inflammation stronger than elaidic acid in human umbilical vein endothelial cells through lipid rafts. Li, Jing,Rao, Huan,Bin, Qiu,Fan, Ya-Wei,Li, Hong-Yan,Deng, Ze-Yuan,Rao, Huan,Bin, Qiu.

[3]稳定高效表达猪CD163的Marc-145细胞系的构建与鉴定. 吴香菊,李芳韬,陈蕾,丛晓燕,孙文博,于江,陈智,郭立辉,吴家强. 2015

[4]猪繁殖与呼吸综合征疫苗研究进展. 李俊,王金宝,吴家强. 2005

[5]Mutant Rep protein of the porcine circovirus type 2 N-glycosylation:23-25aa, 256-258aa mutation reduced virus replication but 286-288aa mutation enhanced virus replication in PK-15 cells. Shi, Jianli,Peng, Zhe,Xu, Shaojian,Cong, Xiaoyan,Yuan, Xiaoyuan,Yu, Jiang,Wu, Jiaqiang,Sun, Wenbo,Du, Yijun,Li, Jun,Wang, Jinbao,Fu, Fang,Xu, Shengnan.

作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：山东省农业科学院文献资源数据库平台

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台