. doi: 10.1016/j.virs.2023.12.006
Citation: Xincheng Ni, Kai Wang, Yinze Han, Jian Lei. Structural analysis of conformational changes in the mpox virus A7 protein .VIROLOGICA SINICA, 2024, 39(2) : 331-334.  http://dx.doi.org/10.1016/j.virs.2023.12.006

猴痘病毒A7蛋白构象变化的结构分析

  • 通讯作者: 雷剑, leijian@scu.edu.cn
  • 收稿日期: 2023-09-14
    录用日期: 2023-12-22
  • 自2022年5月以来,猴痘病毒(MPXV)在世界范围内爆发,严重威胁着人们的公共卫生安全。对病毒关键蛋白的深入研究有助于探索新的抗病毒药物靶点。新月膜(crescent membranes)在MPXV病毒粒子形态发生中起关键作用。该膜由多种病毒蛋白介导形成,这些蛋白被统称为病毒膜组装蛋白(VMAP),其中,A7是最大的VMAP组分。A7由N-端结构域A7N121(含N端121个氨基酸)和C-端结构域A7C组成。本次研究中,我们证明了A7具有磷脂结合能力,并先后解析了A7N121和A7N137的晶体结构。基于对A7N137的结构分析,我们发现连接区域(122-137氨基酸)呈现出明显的构象摆动,导致A7的N端和C端结构域之间产生不同的空间相对取向。随后,通过B-factor分析及分子动力学模拟实验,我们进一步表征了A7连接区域的构象变化特征。最后,基于上述研究结果,我们提出了A7全长的结构模型,并讨论了A7构象变化的潜在生物学意义。总之,该研究扩展了对MPXV A7蛋白的现有认知,并为下一步研究提供了新的方向。

Structural analysis of conformational changes in the mpox virus A7 protein

  • Corresponding author: Jian Lei, leijian@scu.edu.cn
  • Received Date: 14 September 2023
    Accepted Date: 22 December 2023
  • Highlights
    1. Phospholipid-binding abilities of mpox virus A7 protein and its truncations are investigated.
    2. The structures of the N-terminal truncations of A7 protein (A7N121 and A7N137) are determined.
    3. Conformational changes of the conserved linking helix in A7 are illustrated.
    4. A structural model of the full-length A7 protein is proposed.

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    Structural analysis of conformational changes in the mpox virus A7 protein

      Corresponding author: Jian Lei, leijian@scu.edu.cn
    • National Clinical Research Center for Geriatrics, and State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, 610041, China

    Abstract: Highlights
    1. Phospholipid-binding abilities of mpox virus A7 protein and its truncations are investigated.
    2. The structures of the N-terminal truncations of A7 protein (A7N121 and A7N137) are determined.
    3. Conformational changes of the conserved linking helix in A7 are illustrated.
    4. A structural model of the full-length A7 protein is proposed.

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