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Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

Authors

  • Y. Zhou,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
    3. Key Laboratory of Plant Resource Conservation and Sustainable Utilization, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China
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    • These authors contributed equally.
  • X.-W. Lin,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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    • These authors contributed equally.
  • Y.-R. Zhang,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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  • Y.-J. Huang,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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  • C.-H. Zhang,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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  • Q. Yang,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
    3. Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Nanjing, Jiangsu, China
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  • H.-Y. Li,

    1. Institute of Biotechnology, Zhejiang University, Hangzhou, Zhejiang, China
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  • J.-Q. Yuan,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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  • J.-A. Cheng,

    1. State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
    2. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
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  • R. Xu,

    1. Department of Medicine, State University of New York at Stony Brook, Stony Brook, NY, USA
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  • C. Mao,

    Corresponding author
    • Department of Medicine, State University of New York at Stony Brook, Stony Brook, NY, USA
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  • Z.-R. Zhu

    Corresponding author
    1. Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
    • State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China
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Correspondence: Zeng-Rong Zhu, Institute of Insect Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, Zhejiang 310058, China. Tel.: 86 571 88982355; fax: 86 571 88982355; e-mail: zrzhu@zju.edu.cn or Cungui Mao, Department of Medicine, State University of New York at Stony Brook, Stony Brook, NY 11790-8155, USA. Tel.: 631 444 7726; fax: 631 444 6313; e-mail: cungui.mao@stonybrookmedicine.edu

Abstract

Ceramidases are a group of enzymes that catalyse hydrolysis of ceramides to generate fatty acid and sphingosine. In this study, we report the cloning and characterization of the rice small brown planthopper Laodelphax striatellus neutral ceramidase (nCDase), LsnCer. LsnCer was identified by sequencing the transcriptome of L. striatellus and is a protein of 717 amino acids with a predicted molecular weight of 79.3 kDa. Similarly to other known nCDases, the optimum pH for LsnCer is 8.0 and the optimum temperature is 37 °C for its in vitro activity. LsnCer activity is inhibited by Zn2+ significantly and Fe2+ slightly. LsnCer has broad substrate specificity with a preference for ceramides with a medium acyl-chain or a monounsaturated long acyl-chain. Infection with rice strip virus (RSV) or treatment with insecticides significantly increased LsnCer mRNA expression and its enzymatic activity in L. striatellus. These results suggest that LsnCer is a bona fide nCDase that may have a role in adaption of L. striatellus to environmental stresses.

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