Second sialic acid-binding site of influenza A virus neuraminidase: binding receptors for efficient release,The FEBS Journal

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Second sialic acid-binding site of influenza A virus neuraminidase: binding receptors for efficient release
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-12-14 , DOI: 10.1111/febs.15668
Wenjuan Du ₁ , Erik de Vries ₁ , Frank J M van Kuppeveld ₁ , Mikhail Matrosovich ₂ , Cornelis A M de Haan ₁

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Influenza A viruses (IAVs) are a major cause of human respiratory tract infections and cause significant disease and mortality. Human IAVs originate from animal viruses that breached the host species barrier. IAV particles contain sialoglycan receptor-binding hemagglutinin (HA) and receptor-destroying neuraminidase (NA) in their envelope. When IAV crosses the species barrier, the functional balance between HA and NA needs to be adjusted to the sialoglycan repertoire of the novel host species. Relatively little is known about the role of NA in host adaptation in contrast to the extensively studied HA. NA prevents virion aggregation and facilitates release of (newly assembled) virions from cell surfaces and from decoy receptors abundantly present in mucus and cell glycocalyx. In addition to a highly conserved catalytic site, NA carries a second sialic acid-binding site (2SBS). The 2SBS preferentially binds α2,3-linked sialic acids and enhances activity of the neighboring catalytic site by bringing/keeping multivalent substrates in close contact with this site. In this way, the 2SBS contributes to the HA-NA balance of virus particles and affects virus replication. The 2SBS is highly conserved in all NA subtypes of avian IAVs, with some notable exceptions associated with changes in the receptor-binding specificity of HA and host tropism. Conservation of the 2SBS is invariably lost in human (pandemic) viruses and in several other viruses adapted to mammalian host species. Preservation or loss of the 2SBS is likely to be an important factor of the viral host range.

中文翻译：

甲型流感病毒神经氨酸酶的第二个唾液酸结合位点：结合受体以有效释放

甲型流感病毒 (IAV) 是人类呼吸道感染的主要原因，可导致严重疾病和死亡。人类IAV源自突破宿主物种屏障的动物病毒。 IAV 颗粒的包膜中含有唾液聚糖受体结合血凝素 (HA) 和受体破坏性神经氨酸酶 (NA)。当 IAV 跨越物种屏障时，HA 和 NA 之间的功能平衡需要根据新宿主物种的唾液酸聚糖库进行调整。与广泛研究的 HA 相比，人们对 NA 在宿主适应中的作用知之甚少。 NA 可防止病毒粒子聚集，并促进（新组装的）病毒粒子从细胞表面以及粘液和细胞糖萼中大量存在的诱饵受体中释放。除了高度保守的催化位点外，NA 还带有第二个唾液酸结合位点 (2SBS)。 2SBS 优先结合 α2,3-连接的唾液酸，并通过使/保持多价底物与该位点紧密接触来增强邻近催化位点的活性。这样，2SBS有助于病毒颗粒的HA-NA平衡并影响病毒复制。 2SBS 在禽类 IAV 的所有 NA 亚型中高度保守，但有一些与 HA 受体结合特异性和宿主向性变化相关的显着例外。 2SBS 的保守性在人类（大流行）病毒和适应哺乳动物宿主物种的其他几种病毒中总是会丢失。 2SBS 的保留或丢失可能是病毒宿主范围的一个重要因素。

更新日期：2020-12-14

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