Binding kinetics of influenza viruses to sialic acid-containing carbohydrates

Binding kinetics of influenza viruses to sialic acid-containing carbohydrates
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DOI:
10.1007/s10719-007-9055-y
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发表时间:
2007-12-01
影响因子:
3
通讯作者:
Suzuki, Takashi
Suzuki, Takashi
中科院分区:
生物学4区
文献类型:
--
作者:
Hidari, Kazuya I. P. J.;Shimada, Shizumi;Suzuki, Takashi

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为了阐明流感病毒在不同宿主物种(如人类和鸟类)之间传播的分子机制,采用表面等离子体共振(SPR)方法对人类和/或禽流感病毒识别的含唾液酸碳水化合物的结合特性进行了表征。实时监测流感病毒与三种神经节苷脂结合的差异,并与禽流感病毒和人类病毒之间的受体特异性相关。含有神经节苷脂双分子层的SPR分析表明,流感病毒不仅识别唾液酸键,而且根据平衡速率常数识别核心碳水化合物结构。动力学分析表明禽毒株和人毒株对神经节苷类的结合偏好不同。禽毒株在脂质双分子层上与Neu5Ac α 2-3nLc(4)Cer结合,其解离速度比其唾液连锁类似物Neu5Ac α 2-6nLc(4)Cer慢得多。相比之下,人类的一种菌株与两种神经节苷脂的结合是相等的。一种禽类菌株,而不是人类菌株,也与携带较短碳水化合物链的GM(3)相互作用。我们的研究结果表明,禽流感病毒和人流感病毒在含唾液酸的碳水化合物在脂质双分子层上的结合动力学有显著的区别。
To elucidate the molecular mechanisms of transmission of influenza viruses between different host species, such as human and birds, binding properties of sialic acid-containing carbohydrates that are recognized by human and/or avian influenza viruses were characterized by the surface plasmon resonance (SPR) method. Differences in the binding of influenza viruses to three gangliosides were monitored in real-time and correlated with receptor specificity between avian and human viruses. SPR analysis with ganglioside-containing lipid bilayers demonstrated the recognition profile of influenza viruses to not only sialic acid linkages, but also core carbohydrate structures on the basis of equilibrated rate constants. Kinetic analysis showed different binding preferences to gangliosides between avian and human strains. An avian strain bound to Neu5Ac alpha 2-3nLc(4)Cer with much slower dissociation rate than its sialyl-linkage analog, Neu5Ac alpha 2-6nLc(4)Cer, on the lipid bilayer. In contrast, a human strain bound equally to both gangliosides. An avian strain, but not a human strain, also interacted with GM(3) carrying a shorter carbohydrate chain. Our findings demonstrated the remarkable distinction in the binding kinetics of sialic acid-containing carbohydrates between avian and human influenza viruses on the lipid bilayer.