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首页> 外文期刊>Trends in Microbiology >Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk
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Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk

机译：流感血凝素蛋白质稳定性，激活和大流行风险

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摘要

For decades, hemagglutinin (HA) protein structure and its refolding mechanism have served as a paradigm for understanding protein-mediated membrane fusion. HA trimers are in a high-energy state and are functionally activated by low pH. Over the past decade, HA stability (or the pH at which irreversible conformational changes are triggered) has emerged as an important determinant in influenza virus host range, infectivity, transmissibility, and human pandemic potential. Here, we review HA protein structure, assays to measure its stability, measured HA stability values, residues and mutations that regulate its stability, the effect of HA stability on interspecies adaptation and transmissibility, and mechanistic insights into this process. Most importantly, HA stabilization appears to be necessary for adapting emerging influenza viruses to humans.
机译：几十年来，血凝素（HA）蛋白质结构及其复性机制一直是理解蛋白质介导的膜融合的范例。HA三聚体处于高能状态，在低pH值下功能性激活。在过去十年中，HA稳定性（或触发不可逆构象变化的pH值）已成为流感病毒宿主范围、传染性、传播性和人类大流行潜力的重要决定因素。在这里，我们回顾了HA蛋白质结构、测量其稳定性的分析、测量的HA稳定性值、调节其稳定性的残基和突变、HA稳定性对种间适应和遗传性的影响，以及对这一过程的机制见解。最重要的是，稳定HA对于使新出现的流感病毒适应人类似乎是必要的。

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