Immune functions of insect βGRPs and their potential application

Rao, Xiang‐Jun; Zhan, Ming-Yue; Pan, Yuemin; Liu, Su; Yang, Pei-Shan; Yang, Liling; Yu, Xiao‐Qiang

doi:10.1016/j.dci.2017.12.007

Cited by 37 publications

(27 citation statements)

References 92 publications

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“…The gram-negative bacteria-binding proteins (GNBPs) and β-1,3-glucan recognition proteins (βGRPs) belong to a subfamily of pattern recognition receptors and have strong affinities for the lipopolysaccharide of gram-negative bacteria and the β-1,3-glucan of fungi, but not for the PGN of gram-positive bacteria. Of the three GNBPs produced by D. melanogaster (GNBP1, GNBP2, and GNBP3), GNBP1 interacts with PGRP-SA to form a hydrolytic complex that activates the Toll pathway in response to gram-positive bacteria, while GNBP3 is required for detecting fungi and activating the Toll pathway ( Hughes, 2012 ; Rao et al, 2017 ). We identified one GNBP gene in the SPB transcriptome datasets.…”

Section: Resultsmentioning

confidence: 99%

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

Ran

Liu

et al. 2018

PeerJ

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RNA interference (RNAi) technology may be useful for developing new crop protection strategies against the soybean pod borer (SPB; Leguminivora glycinivorella), which is a critical soybean pest in northeastern Asia. Immune-related genes have been recently identified as potential RNAi targets for controlling insects. However, little is known about these genes or mechanisms underlying their expression in the SPB. In this study, we completed a transcriptome-wide analysis of SPB immune-related genes. We identified 41 genes associated with SPB microbial recognition proteins, immune-related effectors or signalling molecules in immune response pathways (e.g., Toll and immune deficiency pathways). Eleven of these genes were selected for a double-stranded RNA artificial feeding assay. The down-regulated expression levels of LgToll-5-1a and LgPGRP-LB2a resulted in relatively high larval mortality rates and abnormal development. Our data represent a comprehensive genetic resource for immune-related SPB genes, and may contribute to the elucidation of the mechanism regulating innate immunity in Lepidoptera species. Furthermore, two immune-related SPB genes were identified as potential RNAi targets, which may be used in the development of RNAi-mediated SPB control methods.

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Section: Resultsmentioning

confidence: 99%

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

Ran

Liu

et al. 2018

PeerJ

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“…Binding ability of BmBGRP and PiBGRP to alkaline-treated BG were also observed either in solid phase or liquid phase. Even the alkaline-treated BGs partially possess helical conformation in the solution [11]. BmBGRP and PiBGRP may bind to the scattering helical portion remaining in the AT-SPG and AT-laminarin.…”

Section: Discussionmentioning

confidence: 99%

“…The triple-helical conformation can be transiently converted to single-strand random coiled or single-helical form, in other words partially opened triple helix, by serial treatment with alkaline and neutralization [10]. It is hypothesized that the innate immune system is able to recognize the structural diversity of the BGs [11]. Therefore, we have isolated four kinds of BGRPs from different insects and examined the binding specificity towards structure-differed BGs in this study.…”

Section: Introductionmentioning

confidence: 99%

N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan

Adachi

Ishii

Kanno

et al. 2019

IJMS

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Recognition of (1→3)-β-d-glucans (BGs) by invertebrate β-1,3-d-glucan recognition protein (BGRP) plays a significant role in the activation of Toll pathway and prophenoloxidase systems in insect host defense against fungal invasion. To examine the structure diversity of BGRPs for the recognition of physiochemically different BGs, the binding specificity of BGRPs cloned from four different insects to structure different BGs was characterized using ELISA. Recombinant BGRPs expressed as Fc-fusion proteins of human IgG1 bound to the solid phase of BGs. Based on the binding specificities, the BGRPs were categorized into two groups with different ultrastructures and binding characters; one group specifically binds BGs with triple-helical conformation, while the other group recognizes BGs with disordered conformations like single-helical or partially opened triple helix. The BGRPs from the silkworm and the Indian meal moth bound to the BGs with a triple-helical structure, whereas BGRPs from the red flour beetle and yellow mealworm beetle showed no binding to triple-helical BGs, but bound to alkaline-treated BGs that have a partially opened triple-helical conformation. This evidence suggests that the insect BGRPs can distinguish between different conformations of BGs and are equipped for determining the diversity of BG structures.

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“…For example, partially opened triple helix can be converted through serial treatment with alkaline-and-neutralization [8]. It is hypothesized that the innate immune system is able to recognize the structural diversity of BGs [9]. Therefore, in this study we have isolated four kinds of BGRPs from different insects and examined their binding specificity to different structures of BGs.…”

Section: Of 13mentioning

confidence: 99%

N-Terminal (1→3)-β-D-glucan Recognition Proteins from Insects Recognize the Difference in ultra-Structures of (1→3)-β-D-glucan

Adachi

Ishii

Kanno

et al. 2019

Preprint

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The recognition of (1→3)-β-D-glucans (BGs) by β-1,3-D-glucan recognition protein (BGRP) found in invertebrates plays a significant role in the activation of toll pathway and pro-phenol oxidase system in insect host defense against fungal invasion. To examine the structural diversity of BGs in BGRP interaction, the binding specificity of BGRPs cloned from four different insectswas characterized using ELISA. Recombinant BGRPs expressed as Fc-fusion proteins of human IgG1 bound to solid phase BGs. Because of the binding specificities, the BGRPs were categorized into two different ultrastructure- binding characters. The BGRPs from Silkworm and Indian meal moth bound to BGs containing triple-helical structure. Other BGRPs from red flour beetle and yellow mealworm beetle showed no binding to triple-helical BGs, but to alkaline-treated BGs, which have partially opened helical conformation. These evidences suggest that the innate immune system distinguishes different BG conformations and it is equipped for the diversity of BG structures.

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Immune functions of insect βGRPs and their potential application

Cited by 37 publications

References 92 publications

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan

N-Terminal (1→3)-β-D-glucan Recognition Proteins from Insects Recognize the Difference in ultra-Structures of (1→3)-β-D-glucan

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Immune functions of insect βGRPs and their potential application

Cited by 37 publications

References 92 publications

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

RNA interference-mediated silencing of genes involved in the immune responses of the soybean pod borer Leguminivora glycinivorella (Lepidoptera: Olethreutidae)

N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan

N-Terminal (1&rarr;3)-&beta;-D-glucan Recognition Proteins from Insects Recognize the Difference in ultra-Structures of (1&rarr;3)-&beta;-D-glucan

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N-Terminal (1→3)-β-D-glucan Recognition Proteins from Insects Recognize the Difference in ultra-Structures of (1→3)-β-D-glucan