The Laminin Receptor Is a Cellular Attachment Receptor for Classical Swine Fever Virus
文献类型: 外文期刊
第一作者: Chen, Jianing
作者: Chen, Jianing;He, Wen-Rui;Shen, Liang;Dong, Hong;Yu, Jiahui;Wang, Xiao;Yu, Shaoxiong;Li, Yongfeng;Li, Su;Luo, Yuzi;Sun, Yuan;Qiu, Hua-Ji
作者机构:
期刊名称:JOURNAL OF VIROLOGY ( 影响因子:5.103; 五年影响因子:5.078 )
ISSN:
年卷期:
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收录情况: SCI
摘要: Classical swine fever virus (CSFV) is the causative agent of classical swine fever (CSF), a highly contagious, economically important viral disease in many countries. The Erns and E2 envelope glycoproteins are responsible for the binding to and entry into the host cell by CSFV. To date, only one cellular receptor, heparan sulfate (HS), has been identified as being involved in CSFV attachment. HS is also present on the surface of various cells that are nonpermissive to CSFV. Hence, there must be another receptor(s) that has been unidentified to date. In this study, we used a set of small interfering RNAs (siRNAs) against a number of porcine cell membrane protein genes to screen cellular proteins involved in CSFV infection. This approach resulted in the identification of several proteins, and of these, the laminin receptor (LamR) has been demonstrated to be a cellular receptor for several viruses. Confocal analysis showed that LamR is colocalized with CSFV virions on the membrane, and a coimmunoprecipitation assay indicated that LamR interacts with the CSFVErns protein. In inhibition assays, anti-LamR antibodies, soluble laminin, or LamR protein significantly inhibited CSFV infection in a dose-dependent manner. Transduction of PK-15 cells with a recombinant lentivirus expressing LamR yielded higher viral titers. Moreover, an attachment assay demonstrated that LamR functions during virus attachment. We also demonstrate that LamR acts as an alternative attachment receptor, especially in SK6 cells. These results indicate that LamR is a cellular attachment receptor for CSFV.
分类号: Q934.2
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