Sulfatide Negatively Regulates the Fusion Process of Human Parainfluenza Virus Type 3.
Sulfatide Negatively Regulates the Fusion Process of Human Parainfluenza Virus Type 3.
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硫脂对人副流感病毒 3 型的融合过程有负调控作用。
DOI：
10.1093/jb/mvs080
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
and Takashi Suzuki.
中科院分区：
文献类型：
--
作者：
Tadanobu Takahashi;Kazuhiko Ito;Keijo Fukushima;Masahiro Takaguchi;Takuya Hayakawa;Yasuo Suzuki;and Takashi Suzuki.
硫苷脂（HSO 3 -3-半乳糖神经酰胺）是宿主细胞有效生产甲型流感病毒的重要成分，在多种上皮细胞中富集于细胞膜脂筏中。然而，硫苷脂在其他针对上皮细胞的病毒感染中的功能仍然未知。在本研究中，通过使用基因产生的富含硫苷的细胞和用抗硫苷单克隆抗体（GS-5）处理hPIV 3感染的细胞以及向细胞中添加硫苷，证明了硫苷对人副流感病毒3型（hPIV 3）感染的影响。在病毒覆盖试验和固相结合试验中发现hPIV 3与硫苷脂结合。硫苷脂缺陷的COS-7细胞中硫苷脂的基因表达抑制了初始hPPV 3感染和多核病毒感染细胞的形成。用GS-5处理病毒感染的LLC-MK2细胞促进多核细胞的形成。相反，外源性硫苷脂对hPIV 3感染的COS-7细胞和表达hPIV 3-血凝素-神经氨酸酶（HN）基因和融合（F）基因的细胞明显减少多核细胞的形成。结果表明，硫苷脂负调控hPIV 3的融合过程，可能通过与细胞表面的HN或F糖蛋白的相互作用。
Sulfatide (HSO3-3-galactosylceramide), which enriched in lipid rafts of plasma membranes in various epithelial cell lines, is a critical component of host cells for effective production of influenza A virus. However, the function of sulfatide in other virus infections targeting epithelial cells remains unknown. In this study, the effect of sulfatide on infection of human parainfluenza virus type 3 (hPIV3) was demonstrated by using genetically produced sulfatide-enriched cells and by treatment of hPIV3-infected cells with anti-sulfatide monoclonal antibody (GS-5) as well as by addition of sulfatide to the cells. hPIV3 was found to bind to sulfatide in a virus overlay assay and a solid-phase binding assay. Genetic expression of sulfatide in COS-7 cells defective in sulfatide suppressed initial hPIV3 infection and formation of multinucleate virus-infected cells. Treatment of virus-infected LLC-MK2 cells with GS-5 promoted formation of multinucleate cells. In contrast, exogenous addition of sulfatide to hPIV3-infected COS-7 cells and cells expressing the hPIV3-hemagglutinin-neuraminidase(HN) gene andfusion(F) gene conspicuously reduced the formation of multinucleate cells. The results suggest that sulfatide negatively regulates the fusion process of hPIV3, possibly through interaction with HN or F glycoprotein on the cell surface.