Evolution of the receptor binding phenotype of influenza A (H5) viruses
Evolution of the receptor binding phenotype of influenza A (H5) viruses
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DOI：
10.1016/j.virol.2005.08.035
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发表时间：
2006-01-20
期刊：
影响因子：
3.7
通讯作者：
Klimov, A
中科院分区：
文献类型：
--
作者：
Gambaryan, A;Tuzikov, A;Klimov, A
研究了包括人2003-04分离株在内的甲型流感/H5病毒的受体特异性。除了两个分离株外，所有分离株均对Sia 2 -3Gal（禽类样）受体保持高亲和力。然而，两个分离株（2003年2月，香港）显示对Sia 2 -3Gal的亲和力降低，对Sia 2 - 6 Gal（类人）受体的亲和力中等。这两种病毒在血凝素分子中具有独特的Ser 227-Asn变化。因此，单个氨基酸取代可以显著改变禽H5 N1病毒的受体特异性，使其具有与人流感病毒的最佳受体结合的能力。来自鸡和人的亚洲2003-04 H5分离株表现出对硫酸化三糖Neu 5Ac α 2-3Gal β 1-4（6-HSO 3）GlcNAc β（Su-3 'SLN）受体的最高亲和力，但与1997分离株相比，对岩藻糖基化Su-3' SLN的亲和力增加。美国家禽H5病毒对Su-3 'SLN的亲和力也增加。这些数据表明，禽流感A（H5 NI）病毒的遗传进化是伴随着在适应家禽的进化，其受体特异性。(C)2005年由Elsevier Inc.出版
Receptor specificity of influenza A/H5 viruses including human 2003-04 isolates was studied. All but two isolates preserved high affinity to Sia2-3Gal (avian-like) receptors. However, two isolates (February, 2003, Hong Kong) demonstrated decreased affinity to Sia2-3Gal and moderate affinity to a Sia2-6Gal (human-like) receptors. These two viruses had a unique Ser227-Asn change in the hemagglutinin molecule. Thus, a single amino acid substitution can significantly alter receptor specificity of avian H5N1 viruses, providing them with an ability to bind to receptors optimal for human influenza viruses. Asian 2003-04 H5 isolates from chickens and humans demonstrated highest affinity to the sulfated trisaccharide Neu5Ac alpha 2-3Gal beta 1-4(6-HSO3)GlcNAc beta (Su-3'SLN) receptor but, in contrast to 1997 isolates, had increased affinity to fucosylated Su-3'SLN. American poultry H5 viruses also had increased affinity to Su-3'SLN. These data demonstrate that the genetic evolution of avian influenza A(H5NI) viruses is accompanied during adaptation to poultry by the evolution of their receptor specificity. (C) 2005 Published by Elsevier Inc.