Phosphorylation of Highly Conserved Serine Residues in the Influenza A Virus Nuclear Export Protein NEP Plays a Minor Role in Viral Growth in Human Cells and Mice
Phosphorylation of Highly Conserved Serine Residues in the Influenza A Virus Nuclear Export Protein NEP Plays a Minor Role in Viral Growth in Human Cells and Mice
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DOI：
10.1128/jvi.00854-14
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发表时间：
2014-07-01
影响因子：
5.4
通讯作者：
Schwemmle, Martin
中科院分区：
文献类型：
--
作者：
Reuther, Peter;Giese, Sebastian;Schwemmle, Martin
甲型流感病毒核输出蛋白（NEP）高度保守的丝氨酸残基S23至S25的磷酸化被怀疑调节其核输出活性或聚合酶活性增强功能。这些磷酸受体位点突变为丙氨酸或天冬氨酸，对这两种活性只有轻微的影响，但揭示了可能参与调节NEP活性的其他磷酸受体位点的存在。
Phosphorylation at the highly conserved serine residues S23 to S25 in the nuclear export protein (NEP) of influenza A viruses was suspected to regulate its nuclear export activity or polymerase activity-enhancing function. Mutation of these phosphoacceptor sites to either alanine or aspartic acid showed only a minor effect on both activities but revealed the presence of other phosphoacceptor sites that might be involved in regulating NEP activity.