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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
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Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion

机译：流感病毒血凝素集中在脂质筏的微区中，以实现有效的病毒融合

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摘要

Lipid raft microdomains are enriched in sphingomyelin and cholesterol and function as platforms for signal transduction and as the site of budding of several enveloped viruses, including influenza virus. The influenza virus hemagglutinin (HA) glycoprotein, which mediates both viral-cell attachment and membrane fusion, associates intrinsically with lipid rafts. Residues in the HA trans-membrane (TM) domain are important for raft association as sequence substitutions in the HA TM domain ablate HA association with rafts (nonraft HA). Cells expressing either WT or nonraft HA cause complete fusion (lipid mixing and content mixing) over widely varying HA expression levels. However, the number of fusion events measured for nonraft HA mutant protein at all HA surface densities was reduced to ≈55% of the events for WT HA protein. Mutant influenza viruses were generated that contain the nonraft HA TM domain alterations. Electron microscopy experiments showed that WT HA was distributed at the cell surface in clusters of 200-280 nm in diameter, whereas nonraft HA was distributed mostly randomly at the plasma membrane. Nonraft HA virus showed reduced budding, contained reduced amounts of HA protein, was greatly reduced in infectivity, and exhibited decreased virus-membrane fusion activity. Cholesterol depletion of virus did not affect the ability of virions to cause either virus-cell lipid mixing or virus-mediated hemolysis, a surrogate for content mixing. Taken together, the data suggest that HA clusters in rafts to provide a sufficient concentration of HA in budding virus to mediate efficient virus-cell fusion.
机译：脂质筏微结构域富含鞘磷脂和胆固醇，并充当信号转导的平台和几种包膜病毒（包括流感病毒）的出芽位点。流感病毒血凝素（HA）糖蛋白介导病毒细胞附着和膜融合，与脂质筏固有地相关。 HA跨膜（TM）域中的残基对于木筏关联非常重要，因为HA TM域中的序列取代会消除HA与木筏的关联（非筏式HA）。表达WT或非筏HA的细胞在广泛变化的HA表达水平上引起完全融合（脂质混合和内容混合）。但是，在所有HA表面密度下，针对非筏HA突变蛋白测得的融合事件数量降至WT HA蛋白的融合事件的≈55％。产生了包含非筏HA TM结构域改变的突变流感病毒。电子显微镜实验表明，WT HA以直径200-280 nm的簇状分布在细胞表面，而非筏HA则大部分随机分布在质膜上。 Nonraft HA病毒显示出芽减少，HA蛋白含量降低，传染性大大降低，病毒-膜融合活性降低。胆固醇的胆固醇消耗并没有影响病毒体引起病毒-细胞脂质混合或病毒介导的溶血（内容混合的替代物）的能力。两者合计，数据表明HA在筏中群集，以在萌芽病毒中提供足够的HA浓度，以介导有效的病毒-细胞融合。

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