甲型流感病毒细胞毒性T淋巴细胞表位中有害氨基酸取代通过共突变实现功能补偿。
Functional compensation of a detrimental amino acid substitution in a cytotoxic-T-lymphocyte epitope of influenza a viruses by comutations.
作者信息
Rimmelzwaan G F, Berkhoff E G M, Nieuwkoop N J, Fouchier R A M, Osterhaus A D M E
机构信息
Erasmus MC, Department of Virology, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands.
出版信息
J Virol. 2004 Aug;78(16):8946-9. doi: 10.1128/JVI.78.16.8946-8949.2004.
Abstract
Influenza A viruses accumulate amino acid substitutions in cytotoxic-T-lymphocyte (CTL) epitopes, allowing these viruses to escape from CTL immunity. The arginine-to-glycine substitution at position 384 of the viral nucleoprotein is associated with escape from CTLs. Introduction of the R384G substitution in the nucleoprotein gene segment of influenza virus A/Hong Kong/2/68 by site-directed mutagenesis was detrimental to viral fitness. Introduction of one of the comutations associated with R384G, E375G, partially restored viral fitness and nucleoprotein functionality. We hypothesized that influenza A viruses need to overcome functional constraints to accumulate mutations in CTL epitopes and escape from CTLs.
摘要
甲型流感病毒在细胞毒性T淋巴细胞（CTL）表位中积累氨基酸替换，使这些病毒能够逃避CTL免疫。病毒核蛋白384位的精氨酸到甘氨酸替换与逃避CTL有关。通过定点诱变在甲型流感病毒A/香港/2/68的核蛋白基因片段中引入R384G替换对病毒适应性有害。引入与R384G相关的共突变之一E375G可部分恢复病毒适应性和核蛋白功能。我们推测甲型流感病毒需要克服功能限制才能在CTL表位中积累突变并逃避CTL。
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