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Molecular characterization and gene silencing of Laccase 1 in the grain aphid, Sitobion avenae.
Arch Insect Biochem Physiol. 2018 Apr; 97(4)AI

Abstract

Laccase 1 (Lac1), a polyphenol oxidase, has been proposed to be involved in insect iron metabolism and immunity responses. However, little information is available on the roles of Lac 1 in insect-plant interactions. The grain aphid Sitobion avenae is one of the most destructive pests of cereal, directly drawing phloem sap and transmitting viruses. In the present study, we first cloned the open reading frame (ORF) of Lac 1 from S. avenae, and the putative protein sequence was predicted to have a carboxyl-terminal transmembrane domain. We found that SaLac1 had higher expression levels in the fourth and adult stages using reverse transcription real-time quantitative PCR (RT-qPCR). SaLac 1 was highly expressed in the salivary gland and midgut and also in wingless compared with winged morphs. After feeding on aphid-resistant wheat with a high total phenol content, the expression level of SaLac 1 increased significantly. RNA interference (RNAi) by oral feeding successfully inhibited the transcript levels of SaLac 1, and the knockdown of Lac 1 significantly decreased the survival rate of S. avenae on aphid-resistant wheat. Our study demonstrated that S. avenae Lac1 was involved in the detoxification of phenolic compounds in wheat and was essential for the aphid to adapt to resistant plants.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Zhang Y
State Key Laboratory of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China. Functional and Evolutionary Entomology, Gembloux Agro-Bio Tech, University of Liège, Liege, Belgium.
Fan J
State Key Laboratory of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China.
Francis F
Functional and Evolutionary Entomology, Gembloux Agro-Bio Tech, University of Liège, Liege, Belgium.
Chen J
State Key Laboratory of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China.

MeSH

Amino Acid SequenceAnimalsAphidsBase SequenceGene SilencingHerbivoryInsect VectorsLaccasePhylogenySequence Analysis, DNATriticum

Pub Type(s)

Journal Article

Language

eng

PubMed ID

29323436

Citation

Zhang, Yong, et al. "Molecular Characterization and Gene Silencing of Laccase 1 in the Grain Aphid, Sitobion Avenae." Archives of Insect Biochemistry and Physiology, vol. 97, no. 4, 2018.
Zhang Y, Fan J, Francis F, et al. Molecular characterization and gene silencing of Laccase 1 in the grain aphid, Sitobion avenae. Arch Insect Biochem Physiol. 2018;97(4).
Zhang, Y., Fan, J., Francis, F., & Chen, J. (2018). Molecular characterization and gene silencing of Laccase 1 in the grain aphid, Sitobion avenae. Archives of Insect Biochemistry and Physiology, 97(4). https://doi.org/10.1002/arch.21446
Zhang Y, et al. Molecular Characterization and Gene Silencing of Laccase 1 in the Grain Aphid, Sitobion Avenae. Arch Insect Biochem Physiol. 2018;97(4) PubMed PMID: 29323436.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization and gene silencing of Laccase 1 in the grain aphid, Sitobion avenae. AU - Zhang,Yong, AU - Fan,Jia, AU - Francis,Frédéric, AU - Chen,Julian, Y1 - 2018/01/11/ PY - 2018/1/13/pubmed PY - 2018/4/3/medline PY - 2018/1/12/entrez KW - RNAi KW - RT-qPCR KW - Sitobion avenae KW - aphid-wheat interactions KW - laccase 1 JF - Archives of insect biochemistry and physiology JO - Arch Insect Biochem Physiol VL - 97 IS - 4 N2 - Laccase 1 (Lac1), a polyphenol oxidase, has been proposed to be involved in insect iron metabolism and immunity responses. However, little information is available on the roles of Lac 1 in insect-plant interactions. The grain aphid Sitobion avenae is one of the most destructive pests of cereal, directly drawing phloem sap and transmitting viruses. In the present study, we first cloned the open reading frame (ORF) of Lac 1 from S. avenae, and the putative protein sequence was predicted to have a carboxyl-terminal transmembrane domain. We found that SaLac1 had higher expression levels in the fourth and adult stages using reverse transcription real-time quantitative PCR (RT-qPCR). SaLac 1 was highly expressed in the salivary gland and midgut and also in wingless compared with winged morphs. After feeding on aphid-resistant wheat with a high total phenol content, the expression level of SaLac 1 increased significantly. RNA interference (RNAi) by oral feeding successfully inhibited the transcript levels of SaLac 1, and the knockdown of Lac 1 significantly decreased the survival rate of S. avenae on aphid-resistant wheat. Our study demonstrated that S. avenae Lac1 was involved in the detoxification of phenolic compounds in wheat and was essential for the aphid to adapt to resistant plants. SN - 1520-6327 UR - https://www.unboundmedicine.com/medline/citation/29323436/Molecular_characterization_and_gene_silencing_of_Laccase_1_in_the_grain_aphid_Sitobion_avenae_ DB - PRIME DP - Unbound Medicine ER -