Identification of novel antimicrobial peptides from rice planthopper, Nilaparvata lugens. (October 2019)

• Record Type: Journal Article
• Authors: Zhou, Xiang; Peng, Lu-Yao; Wang, Zhe-Chao; Wang, Wei; Zhu, Zhen; Huang, Xiao-Hui; Chen, Li-Bo; Song, Qi-Sheng; Bao, Yan-Yuan
• Is Part Of: Insect biochemistry and molecular biology. Volume 113(2019)
• Publication Date: 2019-10
• Subjects: Nilaparvata lugens -- Lugensin -- PGRP-LC -- Antibacterial activity; Insect biochemistry -- Periodicals; Insects -- Physiology -- Periodicals; Insects -- Molecular aspects -- Periodicals; Biochemistry -- Periodicals; Insectes -- Biochimie -- Périodiques; Insectes -- Composition -- Périodiques; Insectes -- Physiologie -- Périodiques; Insectes -- Aspect moléculaire -- Périodiques; Biochimie -- Périodiques; Biochemistry; Insect biochemistry; Insects -- Molecular aspects; Insects -- Physiology; Periodicals; 572.8157
• DOI: 10.1016/j.ibmb.2019.103215
• Languages: English
• ISSNs: 0965-1748

Abstract

Abstract: In this study, two novel antibacterial peptide genes, termed lugensin A and B were identified and characterized from a rice sap-sucking hemipteran insect pest, the brown planthopper, Nilaparvata lugens . Lugensin gene expression was significantly induced by Gram-negative and Gram-positive bacterial stains under the regulation of a signal receptor, the long peptidoglycan recognition protein (PGRP-LC) in the IMD pathway. Knockdown of PGRP-LC by RNAi eliminated bacterium induced Lugensin gene expression. Lugensins had the apparent antibacterial activities against Escherichia coli K12, Bacillus subtilis and the rice bacterial brown stripe pathogen Acidovorax avenae subsp. avenae ( Aaa ) strain RS-1. Lugensins inhibited bacterial proliferation by disrupting the integrity of the bacterial membranes. Scanning electron microscopy revealed abnormal membrane morphology of the recombinant Lugensin-treated bacteria. Lugensins induced complete cell disruption of E. coli K12 and B. subtilis strains while formed the holes on the cell surface of Aaa RS-1 strain. Immunofluorescence showed that Lugensins localized in the cell membrane of E. coli K12 while accumulated in the cytosol of B. subtilis . Differently, Lugensins remained in both the cell membrane and the cytosol of Aaa RS-1 strain, suggesting different action modes of Lugensins to different microbes. This is the first report of the novel antibacterial peptides found in the rice sap-sucking hemipteran insect species. Graphical abstract: Image 1 Highlights: Two novel antibacterial peptides, Lugensins were found in a phloem-sucking insect, N. lugens . Gram-negative and -positive bacteria activated Lugensin gene expression. PGRP-LC, a signal receptor in the Imd pathway, regulated Lugensin gene expression. Lugensins had antibacterial activities against Gram-negative and -positive bacteria strains. Lugensins displayed the different action models on the membranes of the bacteria strains.