A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases
A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases
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DOI：
10.1016/s0014-5793(03)00403-4
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发表时间：
2003-05-22
期刊：
影响因子：
3.5
通讯作者：
Suzuki, Y
中科院分区：
文献类型：
--
作者：
Takahashi, T;Suzuki, T;Suzuki, Y
1957年和1968年分离的四种人类大流行性甲型流感病毒株在低pH条件下具有唾液酸酶活性，但1968年后分离的流行性毒株并非大多数。在这里，我们使用细胞表达的神经氨酸酶（NAs），以确定与唾液酸酶活性的低pH稳定性相关的N2 NA区域。我们发现负责低pH稳定性的共有氨基酸区域在大流行NA中不存在，但是低pH稳定的A/Hong Kong/1/68（H3 N2）NA中的两个氨基酸取代和低pH不稳定的A/Texas/68（H2 N2）NA中的单个取代导致低pH稳定性的显著变化。(C)2003年由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
Four human pandemic influenza A virus strains isolated in 1957 and 1968, but not most of the epidemic strains isolated after 1968, possess sialidase activity under low-pH conditions. Here, we used cell-expressed neuraminidases (NAs) to determine the region of the N2 NA that is associated with low-pH stability of sialidase activity. We found that consensus amino acid regions responsible for low-pH stability did not exist in pandemic NAs but that two amino acid substitutions in the low-pH-stable A/Hong Kong/1/68 (H3N2) NA and a single substitution in the low-pH-unstable A/Texas/68 (H2N2) NA resulted in significant change in low-pH stability. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.