Rogers G N, Paulson J C
Virology. 1983 Jun;127(2):361-73. doi: 10.1016/0042-6822(83)90150-2.
The binding of influenza virus to erythrocytes and host cells is mediated by the interaction of the viral hemagglutinin (H) with cell surface receptors containing sialic acid (SA). The specificity of this interaction for 19 human and animal influenza isolates was examined using human erythrocytes enzymatically modified to contain cell surface sialyloligosaccharides with the sequence SA alpha 2,6Gal beta 1,4GlcNAc; SA alpha 2,3Gal beta 1,4(3)GlcNAc; SA alpha 2,3Gal beta 1,3GalNAc; or SA alpha 2,6GalNAc. Although none of the viruses agglutinated cells containing the SA alpha 2,6GalNAc linkage, differential agglutination of cells containing the other three sequences revealed at least three distinct receptor binding types. Several virus isolates exhibited marked receptor specificity, binding only to cells containing the SA alpha 2,6Gal or the SA alpha 2,3Gal linkage, while others bound equally well to cells containing either linkage. Moreover, some viruses could distinguish between two oligosaccharide receptor determinants containing the terminal SA alpha 2,3Gal linkage when present in the SA alpha 2,3Gal beta 1,4(3)GlcNAc sequence or the SA alpha 2,3Gal beta 1,3GalNAc sequence binding cells containing only the former. The observed receptor specificities were not significantly influenced by the viral neuraminidases as shown by the use of the potent neuraminidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. Receptor specificity appeared, to some extent, to be dependent on the species from which the virus was isolated. In particular, human isolates of the H3 serotype all agglutinated cells containing the SA alpha 2,6Gal linkage, but not cells bearing the SA alpha 2,3Gal beta 1,3GalNAc sequence. In contrast, antigenically similar (H3) isolates from avian and equine species preferentially bound erythrocytes containing the SA alpha 2,3Gal linkage. This is of particular interest in view of the identification of the avian virus H3 hemagglutinin as the progenitor of the H3 hemagglutinin present on the current human Hong Kong viruses.
流感病毒与红细胞及宿主细胞的结合是由病毒血凝素（H）与含有唾液酸（SA）的细胞表面受体相互作用介导的。使用经酶修饰的人红细胞来检测19种人和动物流感病毒分离株这种相互作用的特异性，这些红细胞含有序列为SAα2,6Galβ1,4GlcNAc、SAα2,3Galβ1,4(3)GlcNAc、SAα2,3Galβ1,3GalNAc或SAα2,6GalNAc的细胞表面唾液酸寡糖。尽管没有一种病毒能凝集含有SAα2,6GalNAc连接的细胞，但对含有其他三种序列的细胞的差异凝集显示出至少三种不同的受体结合类型。几种病毒分离株表现出明显的受体特异性，仅与含有SAα2,6Gal或SAα2,3Gal连接的细胞结合，而其他一些则与含有这两种连接的细胞结合得同样好。此外，当存在于SAα2,3Galβ1,4(3)GlcNAc序列或SAα2,3Galβ1,3GalNAc序列中时，一些病毒能够区分两种含有末端SAα2,3Gal连接的寡糖受体决定簇，仅与含有前者的细胞结合。使用强效神经氨酸酶抑制剂2-脱氧-2,3-脱氢-N-乙酰神经氨酸表明，观察到的受体特异性不受病毒神经氨酸酶的显著影响。受体特异性在一定程度上似乎取决于分离病毒的物种。特别是，H3血清型的人分离株都能凝集含有SAα2,6Gal连接的细胞，但不能凝集含有SAα2,3Galβ1,3GalNAc序列的细胞。相反，来自禽类和马类的抗原相似（H3）分离株优先结合含有SAα2,3Gal连接的红细胞。鉴于已鉴定出禽病毒H3血凝素是当前人类香港病毒上存在的H3血凝素的祖先，这一点尤其令人感兴趣。
