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<p><i>Meloidogyne incognita</i> is one of the most widespread and destructive plant pathogenic nematodes in the world. Cytidine deaminase proteins (CDDs) belong to a family of enzymes that catalyse the deamination of cytidine to uridine in bacteria and fungi, and have an important role in the pyrimidine salvage pathway. A cDNA with homology to the CDDs family of <i>M. incognita</i> was identified in this study. We obtained the full-length sequence of <i>Mi-CDD1</i> from <i>M. incognita</i>, which is 595&#xa0;bp long and includes a 456&#xa0;bp ORF that encodes 151 amino acids. Multiple sequence alignment showed that <i>Mi</i>-CDD1 contains a conservative protein kinase C (PKC) phosphorylation site, the phylogenetic tree indicated that <i>Mi</i>-CDD1 had the closest relationship with <i>M. graminicola</i> CDD. <i>Mi-CDD1</i> mRNA was present in the intestine of <i>M. incognita</i> and targeted in the cytoplasm. The relative expression of <i>Mi-CDD1</i> was significantly highest in eggs than the other development stages, than in second-stage juveniles. The relative expression of <i>Mi-CDD1</i> was lowest after soaking with <i>Mi-CDD1</i> dsRNA in vitro for 72&#xa0;h than the other treatments using in vitro RNAi. The pathogenicity of <i>M. incognita</i> to pepper was significantly reduced after treatment with <i>Mi-CDD1</i> dsRNA in vitro for 72&#xa0;h, but the hatching rate of <i>M. incognita</i> eggs after soaking with <i>Mi-CDD1</i> dsRNA was not significantly different among <i>Mi-CDD1</i>, <i>GFP</i> dsRNA in vitro, and control treatments. The results help to understand the function of <i>Mi-</i>CDD1 in <i>M. incognita</i>.</p>

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Function analysis of the cytidine deaminases in root-knot nematode, Meloidogyne incognita

  • 期刊论文

  • 发表日期：

    2025年1月8日

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  • Dongwei Wang,
  • Jian Wang,
  • Yingmei Li,
  • Zhuo Zhang,
  • Jue Cheng,
  • Chunhui Zhu,
  • Zhixiang Zhao,
  • Xinqiu Tan,
  • Deyong Zhang,
  • Yong Liu,
  • Feixue Cheng

摘要

Meloidogyne incognita is one of the most widespread and destructive plant pathogenic nematodes in the world. Cytidine deaminase proteins (CDDs) belong to a family of enzymes that catalyse the deamination of cytidine to uridine in bacteria and fungi, and have an important role in the pyrimidine salvage pathway. A cDNA with homology to the CDDs family of M. incognita was identified in this study. We obtained the full-length sequence of Mi-CDD1 from M. incognita, which is 595 bp long and includes a 456 bp ORF that encodes 151 amino acids. Multiple sequence alignment showed that Mi-CDD1 contains a conservative protein kinase C (PKC) phosphorylation site, the phylogenetic tree indicated that Mi-CDD1 had the closest relationship with M. graminicola CDD. Mi-CDD1 mRNA was present in the intestine of M. incognita and targeted in the cytoplasm. The relative expression of Mi-CDD1 was significantly highest in eggs than the other development stages, than in second-stage juveniles. The relative expression of Mi-CDD1 was lowest after soaking with Mi-CDD1 dsRNA in vitro for 72 h than the other treatments using in vitro RNAi. The pathogenicity of M. incognita to pepper was significantly reduced after treatment with Mi-CDD1 dsRNA in vitro for 72 h, but the hatching rate of M. incognita eggs after soaking with Mi-CDD1 dsRNA was not significantly different among Mi-CDD1, GFP dsRNA in vitro, and control treatments. The results help to understand the function of Mi-CDD1 in M. incognita.