数字农科院2.0

Discovery of an SQS-PSY Domain-Containing Protein in Meloidogyne incognita Reveals Its Function in Parasitism

文献类型： 外文期刊

作者： Junru Lu;Runmao Lin;Yunlong Ma;Xin Sun;Yang Jiao;Xinyue Cheng;Bingyan Xie

作者机构：

关键词： differentially expressed genes (DEGs);experimentally functional analysis;gene expression pattern;heterologous expression;host-induced gene silencing (HIGS);in situ hybridization;nematode-plant interaction;parasitism;root-knot nematode

期刊名称： International Journal of Molecular Sciences

ISSN： 1422-0067

年卷期： 2025 年 26 卷 18 期

页码：

收录情况： SCIE（2025版）

摘要： Proteins containing the SQS-PSY domain, which include squalene synthetase (SQS), phytoene synthetase (PSY), and NDUFAF6, are functionally important and widely distributed in plants and animals. However, they have not been previously reported in nematodes. In this study, we identified a gene (Minc31999) encoding an SQS-PSY domain-containing protein in the root-knot nematode Meloidogyne incognita. In silico comparison and enzymatic assays of the recombinant protein indicated that this nematode protein is a putative NDUFAF6 homolog. Phylogenetic analysis revealed that this protein is evolutionarily conserved within the Nematoda phylum. RT-qPCR analysis showed that Minc31999 is highly expressed during the early infection stage of M. incognita. Targeting the nematode gene Minc31999 via host-induced gene silencing (HIGS) significantly hindered nematode development and virulence. In contrast, heterologous expression of Minc31999 in Arabidopsis thaliana disrupted normal plant development and increased host susceptibility to nematode infection. Transcriptomic profiling (RNA-seq) of these transgenic plants prior to infections showed a widespread differential expression of genes across multiple metabolic pathways. We propose that this nematode SQS-PSY domain-containing protein may function as an effector that rewires host secondary metabolism to establish a parasitic relationship. Our study elucidates a novel strategy in nematode–plant interactions and advances our understanding of the functional evolution of SQS-PSY domain-containing proteins.

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