Receptor-binding properties of modern human influenza viruses primarily isolated in Vero and MDCK cells and chicken embryonated eggs
Receptor-binding properties of modern human influenza viruses primarily isolated in Vero and MDCK cells and chicken embryonated eggs
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DOI：
10.1016/s0042-6822(03)00377-5
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发表时间：
2003-09-01
期刊：
影响因子：
3.7
通讯作者：
Bovin, N
中科院分区：
文献类型：
--
作者：
Mochalova, L;Gambaryan, A;Bovin, N
为了研究现代人流感H1N1和H3 N2病毒的受体特异性，已经使用天然受体的类似物，即与高分子量（约1500 kDa）聚丙烯酰胺缀合的唾液酸寡糖作为生物素化和无标记的探针。从临床标本中分离的病毒在非洲绿色猴肾（Vero）或Madin-Darby犬肾（MDCK）细胞和鸡胚中生长。所有Vero衍生病毒的血凝素（HA）序列与临床样本中存在的原始病毒无法区分，但7个供试MDCK衍生分离株中有3个的HA有1个或2个氨基酸取代。尽管存在这些宿主依赖性突变和单个毒株HA分子结构的差异，但所有研究的Vero和MDCK分离病毒与Neu 5Ac α 2 - 6 GaI β 1 - 4GlcNAc（6 'SLN）的结合基本上强于与Neu 5Ac α 2 - 6 GaI β 1 - 4Glc（6' SL）的结合。这种受体结合特异性是早期分离的H1N1人流感病毒的典型特征，但近年来在人群中流行的H3 N2病毒有一个新的特性。人病毒在鸡胚蛋中的繁殖导致选择在HA受体结合位点附近具有氨基酸取代的变体，即H1N1病毒的GIn 226 Arg或Asp 225 Gly和H3 N2病毒的Leu 194 Ile和Arg 220 Ser。这些HA突变干扰了最近人流感病毒观察到的严格的6 'SLN特异性。(C)2003 Elsevier Science（美国）。All rights reserved.
To study the receptor specificity of modern human influenza H1N1 and H3N2 viruses, the analogs of natural receptors, namely sialyloligosaccharides conjugated with high molecular weight (about 1500 kDa) polyacrylamide as biotinylated and label-free probes, have been used. Viruses isolated from clinical specimens were grown in African green monkey kidney (Vero) or Madin-Darby canine kidney (MDCK) cells and chicken embryonated eggs. All Vero-derived viruses had hemagglutinin (HA) sequences indistinguishable from original viruses present in clinical samples, but HAs of three of seven tested MDCK-derived isolates had one or two amino acid substitutions. Despite these host-dependent mutations and differences in the structure of HA molecules of individual strains, all studied Vero- and MDCK-isolated viruses bound to Neu5Ac alpha2-6GaIbeta1-4GIcNAc (6'SLN) essentially stronger than to Neu5Acalpha2-6GaIbeta1-4GIc (6'SL). Such receptor-binding specificity has been typical for earlier isolated H1N1 human influenza viruses, but there is a new property of H3N2 viruses that has been circulating in the human population during recent years. Propagation of human viruses in chicken embryonated eggs resulted in a selection of variants with amino acid substitutions near the HA receptor-binding site, namely GIn226Arg or Asp225GIy for H1N1 viruses and Leu194Ile and Arg220Ser for H3N2 viruses. These HA mutations disturb the observed strict 6'SLN specificity of recent human influenza viruses. (C) 2003 Elsevier Science (USA). All rights reserved.