DIFFERENTIAL SENSITIVITY OF HUMAN, AVIAN, AND EQUINE INFLUENZA-A VIRUSES TO A GLYCOPROTEIN INHIBITOR OF INFECTION - SELECTION OF RECEPTOR SPECIFIC VARIANTS
DIFFERENTIAL SENSITIVITY OF HUMAN, AVIAN, AND EQUINE INFLUENZA-A VIRUSES TO A GLYCOPROTEIN INHIBITOR OF INFECTION - SELECTION OF RECEPTOR SPECIFIC VARIANTS
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DOI：
10.1016/0042-6822(83)90507-x
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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：
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作者：
ROGERS, GN;PRITCHETT, TJ;PAULSON, JC
人类和动物（禽和马）甲型流感病毒H3血清型分离株在结合作为细胞表面受体决定因子的特异性唾液寡糖序列的能力方面表现出显著差异。而该亚型的人分离株则能强烈凝集酶修饰的含有末端sa . α的人红细胞。2,6 gal序列，禽和马分离物优先凝集携带sa . α的红细胞。2、3加序列。一种在马血清中发现的糖蛋白。2-巨球蛋白是人类H3分离株细胞表面病毒吸附的有效抑制剂。禽和马分离株的抑制作用较差，提示受体特异性和抑制剂敏感性之间存在相关性。人H3分离物（a /Memphis/102/72）在马血清存在的情况下在Madin-Darby犬肾MDCK细胞上生长，导致病毒受体特异性从优先结合SA.alpha的整体转变。2,6 gal键与sa . α优先结合。禽和马分离株的2,3 gal连锁特征。在存在或不存在马血清的情况下生长的A/Memphis/102/72的克隆分离变体显示出与现场分离株观察到的结合特性。优先绑定sa。alpha的克隆。2,6 gal连锁与亲本人病毒一样，对马血清和马α - 2巨球蛋白的血凝抑制作用非常敏感。受体变异优先结合sa。alpha。2,3 gal连锁与禽和马分离株一样，对这些抑制剂不敏感。这些变异对人α - 2巨球蛋白抑制血凝反应均不敏感。这些结果表明，体内存在一种糖蛋白抑制剂，如马α。2-巨球蛋白能抑制带有sa . α的H3血凝素的流感病毒的感染。2,6 gal特异性，抑制剂敏感表型，允许SA.alpha病毒的优势生长。在禽和马分离株中发现的2,3 gal特异性和抑制剂不敏感。
Human and animal (avian and equine) influenza A virus isolates of the H3 serotype exhibit marked differences in their ability to bind specific sialyloligosaccharide sequences that serve as cell surface receptor determinants. Whereas human isolates of this subtype strongly agglutinate enzymatically modified human erythrocytes containing the terminal SA.alpha.2,6Gal sequence, avian and equine isolates preferentially agglutinate erythrocytes bearing the SA.alpha.2,3Gal sequence. A glycoprotein found in horse serum, .alpha.2-macroglobulin, is a potent inhibitor of viral adsorption to the cell surface for human H3 isolates. Avian and equine isolates are poorly inhibited suggesting a correlation between receptor specificity and inhibitor sensitivity. Growth of a human H3 isolate (A/Memphis/102/72) on Madin-Darby canine kidney MDCK cells in the presence of horse serum resulted in an overall shift in the virus receptor specificity from preferential binding of the SA.alpha.2,6Gal linkage to preferential binding of the SA.alpha.2,3Gal linkage characteristic of avian and equine isolates. Clonally isolated variants of A/Memphis/102/72 grown in the presence or absence of horse serum exhibited binding properties that account for those observed in the field isolates. Clones which preferentially bound the SA.alpha.2,6Gal linkage, like the parent human virus, were very sensitive to inhibition of hemagglutination by horse serum and equine .alpha.2-macroglobulin. Receptor variants which preferentially bound the SA.alpha.2,3Gal linkage, like the avian and equine isolate, were insensitive to such inhibitors. None of the variants was very sensitive to inhibition of hemagglutination by human .alpha.2-macroglobulin. These results suggest that the presence, in vivo, of a glycoprotein inhibitor such as equine .alpha.2-macroglobulin could suppress infection of influenza viruses bearing an H3 hemagglutinin with a SA.alpha.2,6Gal specific, inhibitor sensitive phenotype, allowing growth to predominance of a virus which is SA.alpha.2,3Gal specific and inhibitor insensitive as found in avian and equine isolates.