Influenza A viruses (IAVs) originating from aquatic waterfowl recurrently cross interspecies barriers, which is greatly facilitated by utilizing cell surface–exposed monosaccharide sialic acids located on vertebrate cells as a universal host cell receptor. These glycan structures are first bound by the viral hemagglutinin (HA) for cell entry and then cleaved by the viral neuraminidase (NA) for particle release. In contrast, viruses of the recently identified bat-borne IAV subtypes H17N10 and H18N11 encode HA and NA homologs unable to interact with sialic acid residues despite a high degree of structural homology with their conventional counterparts. However, the most recent findings show that bat IAV HAs make use of the major histocompatibility complex class II proteins of different vertebrate species to gain entry into host cells, potentially permitting a broader host tropism. This review recapitulates current progress in the field of bat IAV research including the first assessment of the spillover potential of these bat viruses into other mammals.
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机译：起源于水生水禽的甲型流感病毒 （IAV） 经常跨越物种间屏障，利用位于脊椎动物细胞上的细胞表面暴露的单糖唾液酸作为通用宿主细胞受体，极大地促进了这一点。这些聚糖结构首先与病毒血凝素 （HA） 结合以进入细胞，然后被病毒神经氨酸酶 （NA） 裂解以释放颗粒。相比之下，最近发现的蝙蝠传播的 IAV 亚型 H17N10 和 H18N11 的病毒编码 HA 和 NA 同源物，尽管与传统同类具有高度的结构同源性，但无法与唾液酸残基相互作用。然而，最新的发现表明，蝙蝠 IAV HA 利用不同脊椎动物物种的主要组织相容性复合物 II 类蛋白进入宿主细胞，从而可能允许更广泛的宿主嗜性。本综述概括了蝙蝠 IAV 研究领域的当前进展，包括首次评估这些蝙蝠病毒对其他哺乳动物的溢出潜力。
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