An immune-responsive PGRP-S1 regulates the expression of antibacterial peptide genes in diamondback moth, Plutella xylostella (L.)

Zhang, Zhantao; Kong, Jinrong; Mandal, Surajit De; Li, Shuzhong; Zheng, Zhihua; Jin, Fengliang; Xu, Xi

doi:10.1016/j.ijbiomac.2019.09.081

Cited by 16 publications

(10 citation statements)

References 39 publications

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“…In addition, SlGRP‐LB possessed a signal peptide in the N‐terminal, indicating it is a secreted protein. In Drosophila , the short‐form GRPs are small secreted proteins consisting of the GRP domain and a signal peptide sequence, while the long‐form proteins also contain transmembrane domains (Zhang et al, 2020). Interestingly, the 3‐D structural of SlGRP‐LB analysis suggested that it contains three α‐helices, six β‐helices and a zinc ion binding site.…”

Section: Discussionmentioning

confidence: 99%

“…We believed that injected bacteria directly entered the S. litura hemolymph activates the host immune response. In Plutella xylostella, E. coli , and S. aureus stimulated the expression of PxGRP‐S1 after 6 h postinfection in the midgut; while in hemocytes and fat body PxGRP‐S1 expression was increased by E. coli and S. aureus after 3 h postinfection, respectively (Zhang et al, 2020). These results suggested that SlGRP‐LB could be induced by various pathogens.…”

Section: Discussionmentioning

confidence: 99%

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Functional analysis of a peptidoglycan recognition protein involved in the immune response in the common cutworm, Spodoptera litura

Wang

Zhang

2021

Arch Insect Biochem Physiol

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Peptidoglycan recognition proteins (GRPs) are family of pattern recognition receptors (PRRs), which can recognize the peptidoglycan and trigger the innate immune system against the microorganisms in insects. In this study, we identified a GRP‐LB from Spodoptera litura genome database and named SlGRP‐LB, which contained a complete open reading frame (ORF) of 639 bp, encoding a protein of 212 amino acids with a signal peptide and GRP domain. Phylogenetic tree analysis suggested that the SlGRP‐LB has a close relationship with Helicoverpa armigera GRP‐LB (HaGRP‐LB). Tissue expression analysis revealed that SlGRP‐LB had a high expression level in the fat body. The expression levels of SlGRP‐LB were significantly upregulated in the hemolymph, fat body, and midgut from 3 to 12 h after injection of Escherichia coli and Staphylococcus aureus, while the expression levels were not downregulated at 24 h postinfection. Knockdown of SlGRP‐LB expression by RNA interference reduced the expression of antibacterial peptide‐related genes in the fat body and midgut, while their expression levels were upregulated in the hemolymph. In addition, the recombinant SlGRP‐LB was expressed by using E. coli expression system, and it exhibited binding activity to E. coli. Taken together, the data suggest that S. litura GRP‐LB might play a crucial role in regulating immune response in S. litura.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Functional analysis of a peptidoglycan recognition protein involved in the immune response in the common cutworm, Spodoptera litura

Wang

Zhang

2021

Arch Insect Biochem Physiol

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“…Following the misuse of insecticides in the field, P. xylostella has developed such severe resistance to most pesticides through multiple mechanisms that it is difficult to control 14,15 . Although RNAi was reported to be less efficient in lepidoptera 16 , RNAi in P. xylostella through dsRNA injection or oral administration demonstrated that this approach is for this species 17,18 . Therefore, the control and resistance management of P. xylostella may be achieved by dsRNA ingestion and interference with specific target genes.…”

Section: Introductionmentioning

confidence: 99%

BacterialPxRdl2dsRNA increased the insecticidal activities of GABAR-targeting compounds againstPlutella xylostella

Wang

et al. 2021

Preprint

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BACKGROUND: The application of RNAi to control pests has attracted the attention of researchers. Our results indicated that knockout of PxRdl2 can decrease resistance to fipronil in Plutella xylostella, providing a suitable target gene for RNAi-based pest control. RESULTS: The differences in the sensitivity of two established homozygous knockout strains of P. xylostella. (Rdl1KO and Rdl2KO) and susceptible P. xylostella to a series of compounds were evaluated. Quinazolines and isoxazolines both showed stronger efficacy in the Rdl2KO strain. Therefore, we proposed a method based on the knockdown of the P. xylostella Rdl2 gene as a tactic to enhance the toxicity of quinazolines and isoxazolines. To reduce costs and protect dsRNA against degradation, we applied a bacterial expression system using the L4440 vector to express PxRdl2 dsRNA in HT115 Escherichia coli. Transformed bacteria (dsRNA-Bac) fed through leaves combined with quinazoline and isoxazolines proved to be more effective in both the susceptible and fipronil-resistant P. xylostella. CONCLUSION: Our results provide a strategy for the development of novel insecticide spray formulations containing dsRNA-Bac, which synergize with insecticide toxins by suppressing PxRdl2, reducing the use of pesticides in the field.

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“…PGRP1 together with microbe binding protein leads to hemolymph protease‐14 precursor autoactivation (Hu et al, 2019; Sumathipala & Jiang, 2010; Y. Wang & Jiang, 2017). Plutella xylostella PGRP‐S1 serves as a bacterial PRR and triggers the expression of AMPs (Zhang et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Structure–function analysis of PGRP‐S1 from the oriental armyworm, Mythimna separata

Liu

Yang

et al. 2021

Arch Insect Biochem Physiol

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Peptidoglycan recognition proteins (PGRPs) are well known for their abilities to recognize or hydrolyze peptidoglycan (PGN), one of the major bacterial cell wall components. However, much less is known about their antifungal activities. PGRP‐S1 was previously identified from a crop pest, Mythimna separata (Walker) (Lepidoptera: Noctuidae). PGRP‐S1 showed bacteriolytic activities against Gram‐positive and Gram‐negative bacteria. In this study, tissue expression analysis showed that PGRP‐S1 was mainly expressed in the midgut of naïve larvae. The induction analysis showed that it was significantly induced in the larval midgut 12 h post the injection of Beauveria bassiana conidia. To identify the key residues that are related to its microbicidal activities, the structure of PGPR‐S1 was predicted for structural comparison and molecular docking analysis. Six residues (H61, H62, Y97, H171, T175, and C179) were mutated to Ala individually by site‐directed mutagenesis. The recombinant wild‐type (WT) and mutant proteins were expressed and purified. The recombinant proteins bound to different polysaccharides, PGNs, and bacteria. H61A, Y97A, H171A, and C179A lost amidase activity. Accordingly, antibacterial assay and scanning electron microscopy confirmed that only H62A and T175A retained bacteriolytic activities. The germination of B. bassiana conidia was significantly inhibited by WT, H61A, Y97A, T175A, and C179A mutants. Electron microscopy showed that some conidia became ruptured after treatment. The growth of hyphae was inhibited by the WT, H61A, H62A, and T175A. In summary, our data showed that different residues of PGRP‐S1 are involved in the antibacterial and antifungal activities.

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An immune-responsive PGRP-S1 regulates the expression of antibacterial peptide genes in diamondback moth, Plutella xylostella (L.)

Cited by 16 publications

References 39 publications

Functional analysis of a peptidoglycan recognition protein involved in the immune response in the common cutworm, Spodoptera litura

Functional analysis of a peptidoglycan recognition protein involved in the immune response in the common cutworm, Spodoptera litura

BacterialPxRdl2dsRNA increased the insecticidal activities of GABAR-targeting compounds againstPlutella xylostella

Structure–function analysis of PGRP‐S1 from the oriental armyworm, Mythimna separata

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