RECEPTOR DETERMINANTS OF HUMAN AND ANIMAL INFLUENZA-VIRUS ISOLATES - DIFFERENCES IN RECEPTOR SPECIFICITY OF THE HEMAGGLUTININ-H-3 BASED ON SPECIES OF ORIGIN
RECEPTOR DETERMINANTS OF HUMAN AND ANIMAL INFLUENZA-VIRUS ISOLATES - DIFFERENCES IN RECEPTOR SPECIFICITY OF THE HEMAGGLUTININ-H-3 BASED ON SPECIES OF ORIGIN
复制标题
DOI:
10.1016/0042-6822(83)90150-2
复制
发表时间:
1983-01-01
期刊:
影响因子:
3.7
通讯作者:
PAULSON, JC
中科院分区:
文献类型:
--
作者:
ROGERS, GN;PAULSON, JC
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 3 sequences revealed at least 3 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. Some viruses could distinguish between 2 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 H3 serotype all agglutinated cells containing the SA.alpha.2,6Gal linkage, but not cells bearing the SA.alpha.2,3Gal.beta.1,GalNAc sequence. Antigenically similar (H3) isolates from avian and equine species preferentially bound erythrocytes containing the SA.alpha.2,3Gal linkages. 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.