Equine ANP32 proteins support influenza A virus RNA polymerase activity

文献类型： 外文期刊

第一作者： Zhang, Yuan

作者： Zhang, Yuan;Guo, Xing;Yu, Mengmeng;Sun, Liuke;Qu, Yuxing;Guo, Kui;Hu, Zhe;Liu, Diqiu;Wang, Xiaojun;Zhang, Haili;Zhang, Haili

作者机构：

关键词： Equine influenza virus (EIV); Equine ANP32A; Equine ANP32B; RNA polymerase activity; N -Cap domain

期刊名称：VIROLOGICA SINICA （ 影响因子：5.5； 五年影响因子：4.9 ）

ISSN： 1674-0769

年卷期： 2023 年 38 卷 6 期

页码：

收录情况： SCI

摘要： Host ANP32 family proteins are crucial for maintaining the activity of influenza RNA polymerase and play an important role in the cross-species transmission of influenza viruses. To date, the molecular properties of equine ANP32 (eqANP32) protein are poorly understood, particularly the mechanisms that affect equine influenza virus (EIV) RNA polymerase activity. Here, we found that there are six alternative splicing variants of equine ANP32A (eqANP32A) with different levels of expression. Further studies showed that these six splicing variants of eqANP32A supported the activity of EIV RNA polymerase to varying degrees, with the variant eqANP32A_X2 having the highest expression abundance and exhibiting the highest support of polymerase activity. Sequence analysis demonstrated that the differences in the N-Cap regions of the six splicing variants significantly affected their N-terminal conformation, but did not affect their ability to bind RNA polymerase. We also demonstrated that there is only one transcript of eqANP32B, and that this transcript showed only very low support to the EIV RNA polymerase. This functional defect in eqANP32B is caused by the sequence of the 110-259 amino acids at its C -terminus. Our results indicated that it is the eqANP32A_X2 protein that mainly determines the efficiency of the EIV replication in horses. In conclusion, our study parsed the molecular properties of eqANP32 family proteins and revealed the sequence features of eqANP32A and eqANP32B, suggesting for the first time that the N-Cap region of ANP32A protein also plays an important role in supporting the activity of the influenza virus polymerase.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序