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铜/锌超氧化物歧化酶同源物参与抗病毒反应。

Cu/Zn superoxide dismutase homologs participate in antiviral responses.

作者信息

Wang Haijuan, Zhang Jidan, Meng Zhuo, Sun Zhenqi, Liu Dongyang, Li Bin, Yan Fangfang, Jia Chongyi, Zhou Hongyou, Zhao Mingmin

机构信息

College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.

Sichuan Province Company of Tobacco Corporation in China, Chengdu, China.

出版信息

Front Microbiol. 2025 Jul 18;16:1561731. doi: 10.3389/fmicb.2025.1561731. eCollection 2025.

DOI:10.3389/fmicb.2025.1561731
PMID:40756210
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12313585/
Abstract

Superoxide dismutases (SODs) serve as the first line of defense against reactive oxygen species. Copper-zinc superoxide dismutase () is an enzyme whose activity depends on copper availability. induction is shown to be involved in the antioxidative and antiviral activity of acetylsalicylic acid in hepatitis C virus (HCV)-expressing cells. Here, RNA sequencing (RNA-seq) analysis identified SOD homologs (three , four , and two ) that were differentially expressed in during tobacco vein mottling virus (TVMV) infection. was cloned from and subsequently characterized. Encoding sequence and structural analyses of the protein confirmed a conserved SOD enzyme domain, GFHLHEfGDtT, indicating that it is SOD-dependent and phylogenetically related to in (XP 016486719.1). was primarily localized in the cytoplasm. The transient expression of led to a reduced accumulation of TVMV and PVY-Rosea1 (PVY-Ros1). In summary, our results suggest that homologs participate in plant antiviral responses.

摘要

超氧化物歧化酶(SODs)作为抵御活性氧的第一道防线。铜锌超氧化物歧化酶( )是一种其活性依赖于铜可用性的酶。已表明 的诱导参与了乙酰水杨酸在丙型肝炎病毒(HCV)表达细胞中的抗氧化和抗病毒活性。在此,RNA测序(RNA-seq)分析鉴定出在烟草脉斑驳病毒(TVMV)感染期间在 中差异表达的SOD同源物(三个 、四个 和两个 )。 从 中克隆出来并随后进行了表征。对 蛋白的编码序列和结构分析证实了一个保守的SOD酶结构域,GFHLHEfGDtT,表明它是SOD依赖性的,并且在系统发育上与 中的 (XP 016486719.1)相关。 主要定位于细胞质中。 的瞬时表达导致TVMV和PVY - Rosea1(PVY - Ros1)的积累减少。总之,我们的结果表明 同源物参与植物抗病毒反应。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/39468e5fe84f/fmicb-16-1561731-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/0af019956225/fmicb-16-1561731-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/29c443198016/fmicb-16-1561731-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/41cdc563174c/fmicb-16-1561731-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/f96b1cd4afcd/fmicb-16-1561731-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/88ebf4dd5ebe/fmicb-16-1561731-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/39468e5fe84f/fmicb-16-1561731-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/0af019956225/fmicb-16-1561731-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/29c443198016/fmicb-16-1561731-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/41cdc563174c/fmicb-16-1561731-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/f96b1cd4afcd/fmicb-16-1561731-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/88ebf4dd5ebe/fmicb-16-1561731-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e219/12313585/39468e5fe84f/fmicb-16-1561731-g006.jpg

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