A unique phosphatidylinositol bearing a novel branched-chain fatty acid from Rhodococcus equi binds to influenza virus hemagglutinin and inhibits the infection of cells
A unique phosphatidylinositol bearing a novel branched-chain fatty acid from Rhodococcus equi binds to influenza virus hemagglutinin and inhibits the infection of cells
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DOI：
10.1093/oxfordjournals.jbchem.a002996
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发表时间：
2001-09-01
影响因子：
2.7
通讯作者：
Suzuki, Y
中科院分区：
文献类型：
--
作者：
Guo, CT;Ohta, S;Suzuki, Y
从水生细菌马红球菌菌株S-420中，我们分离出一种与流感病毒强烈结合的物质。结构分析表明，它是一种独特类型的磷脂酰肌醇（PtdIns），带有支链脂肪酸（14-甲基十八烷酸）。在TLC/病毒结合免疫染色测定中，该PtdIns与从人、鸭和猪分离的测试的甲型流感病毒的血凝素（HA）的所有亚型结合，并且还与人流感B病毒结合。此外，PtdIns显著地防止流感病毒感染MDCK细胞，并且还抑制病毒介导的血凝和低pH诱导的人红细胞溶血，这代表了病毒HA的融合活性。我们还使用纯化的血凝素代替病毒粒子来检查病毒EIA和PtdIns之间的相互作用，表明PtdIns与血凝素结合。这些发现表明PtdIns对流感病毒感染的抑制机制可能是通过其与病毒HA刺突和宿主细胞内体/溶酶体膜的结合，这些结合是由病毒HA的功能介导的。
From the aquatic bacterium Rhodococcus equi strain S-420, we isolated a substance that strongly binds to influenza viruses. Structural analyses revealed that it is a unique type of phosphatidylinositol (PtdIns) bearing a branched-chain fatty acid (14-methyloctadecanoic acid). In a TLC/virus-binding immunostaining assay, this PtdIns bound to all subtypes of hemagglutinin (HA) of influenza A viruses tested, isolated from humans, ducks and swine, and also to human influenza B viruses. Furthermore, the PtdIns significantly prevented the infection of MDCK cells by influenza viruses, and also inhibited the virus-mediated hemagglutination and low pH-induced hemolysis of human erythrocytes,,which represents the fusogenic activities of the viral HA. We also used purified hemagglutinin instead of virions to examine the interaction between viral EIA and PtdIns, showing that the PtdIns binds to hemagglutinin. These findings indicate that the inhibitory mechanism of PtdIns on the influenza virus infection may be through its binding to viral HA spikes and host cell endosomal/lysosomal membranes, which are mediated by the function of viral HA.