Receptor-binding properties of swine influenza viruses isolated and propagated in MDCK cells
Receptor-binding properties of swine influenza viruses isolated and propagated in MDCK cells
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DOI：
10.1016/j.virusres.2005.05.005
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发表时间：
2005-12-01
期刊：
影响因子：
5
通讯作者：
Klimov, AI
中科院分区：
文献类型：
--
作者：
Gambaryan, AS;Karasin, AI;Klimov, AI
为了研究最近从猪身上分离的H1和H3流感病毒的受体特异性，我们采用了天然受体的类似物，即生物素化和无标记形式的与聚丙烯酰胺缀合的唾液酸寡糖。所有Madin-Darby犬肾（MDCK）细胞增殖病毒与人H3或经典猪H1血凝素仅结合Neu 5Ac α 2- 6 Gal β 1-承载聚合物，而不结合Neu 5Ac α 2-3Gal β 1-承载聚合物。这种受体结合模式是人流感病毒的典型模式，它不同于先前描述的蛋适应猪流感病毒的受体结合特异性。具有禽样H1和H3血凝素的猪病毒分离物通过结合含Neu 5Ac α 2- 6 Gal和Neu 5Ac α 2- 3Gal的受体而显示出不同的受体特异性。这些病毒，以及具有经典猪HA的蛋适应性猪和火鸡病毒，与相关鸭病毒的不同之处在于对硫酸化唾液酸寡糖Su-SiaLe（x）的亲和力增加。除禽样H3病毒外，所研究的猪病毒均未与含Neu 5Gc的唾液酸共聚物结合，这表明与猪中大量表达的这些唾液酸种类的结合可能不是病毒在该宿主中复制所必需的。由爱思唯尔公司出版
To study the receptor specificities of H1 and H3 influenza viruses isolated recently from pigs, we employed the analogues of natural receptors, namely sialyloligosaccharides conjugated with polyacrylamide in biotinylated and label free forms. All Madin-Darby canine kidney (MDCK) cell-propagated viruses with human H3 or classical swine H1 hemagglutinins bound only to Neu5Ac alpha 2-6Gal beta 1-bearing polymers, and not to Neu5Ac alpha 2-3Gal beta 1-bearing polymers. This receptor-binding pattern is typical for human influenza viruses and it differs from the previously described receptor-binding specificity of egg-adapted swine influenza viruses. Swine virus isolates with avian-like H I and H3 hemagglutinins displayed distinct receptor specificity by binding to both Neu5Ac alpha 2-6Gal- and Neu5Ac alpha 2-3Gal-containing receptors. These viruses, as well as egg-adapted swine and turkey viruses with a classical swine HA, differed from the related duck viruses by increased affinity to sulfated sialyloligosaccaride, Su-SiaLe(x). Except for avian-like H3 viruses, none of the studied swine viruses bound to Neu5Gc-containing sialoglycopolymers, suggesting that binding to these sialic acid species abundantly expressed in pigs may not be essential for virus replication in this host. Published by Elsevier B.V.