<i>Aedes aegypti</i> Galectin Competes with Cry11Aa for Binding to ALP1 To Modulate Cry Toxicity

Zhang, Lingling; Hu, Xiaohua; Wu, Songqing; Batool, Khadija; Chowdhury, Mridula; Lin, Yongjun; Zhang, Jie; Gill, Sarjeet S.; Guan, Xiong; Yu, Xiao‐Qiang

doi:10.1021/acs.jafc.8b04665

Cited by 19 publications

(32 citation statements)

References 43 publications

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“…However, bacteria loading was not influenced by MaGal2 knockdown, which indicated that bacteria loading does not normally occur in J IV . In addition, galectins both mediate recognition and effector function in innate immunity, and also mediate developmental processes (Rao et al ., 2016; Zhang et al ., 2018a). However, MaGal2 may also have additional roles in Monochamus beetles, and should therefore be further studied.…”

Section: Discussionmentioning

confidence: 99%

A new bacteria‐free strategy induced by MaGal2 facilitates pinewood nematode escape immune response from its vector beetle

et al. 2020

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Symbiotic microbes play a crucial role in regulating parasite-host interactions; however, the role of bacterial associates in parasite-host interactions requires elucidation. In this study, we showed that, instead of introducing numerous symbiotic bacteria, dispersal of 4th-stage juvenile (J IV ) pinewood nematodes (PWNs), Bursaphelenchus xylophilus, only introduced few bacteria to its vector beetle, Monochamus alternatus (Ma). J IV showed weak binding ability to five dominant bacteria species isolated from the beetles' pupal chamber. This was especially the case for binding to the opportunistic pathogenic species Serratia marcescens; the nematodes' bacteria binding ability at this critical stage when it infiltrates Ma for dispersal was much weaker compared with Caenorhabditis elegans, Diplogasteroides asiaticus, and propagative-stage PWN. The associated bacterium S. marcescens, which was isolated from the beetles' pupal chambers, was unfavorable to Ma, because it caused a higher mortality rate upon injection into tracheae. In addition, S. marcescens in the tracheae caused more immune effector disorders compared with PWN alone. Ma_Galectin2 (MaGal2), a pattern-recognition receptor, was up-regulated following PWN loading. Recombinant MaGal2 protein formed aggregates with five dominant associated bacteria in vitro. Moreover, MaGal2 knockdown beetles had up-regulated prophenoloxidase gene expression, increased phenoloxidase activity, and decreased PWN loading. Our study revealed a previously unknown strategy for immune evasion of this plant pathogen inside its vector, and provides novel insights into the role of bacteria in parasite-host interactions.

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Section: Discussionmentioning

confidence: 99%

A new bacteria‐free strategy induced by MaGal2 facilitates pinewood nematode escape immune response from its vector beetle

et al. 2020

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“…Three-dimensional (3D) structures of Cry1Ab1 toxic core and Cry-binding proteins were predicted by PHYRE2. GRAMM-X Protein-Protein Docking Web Server v.1.2.0 was used to predict the molecular docking of Cry1Ab1 toxic core and Cry-binding proteins, and then the docking results was analyzed and showed in the Discovery Studio 2.5 (Kang et al 2017;Zhang et al 2018). The functional domain of Crybinding proteins was acquired from the UniProt database.…”

Section: Molecular Docking and Binding Sites Analysismentioning

confidence: 99%

“…Zhao et al found that Cry41-realted interacted with Cathepsin B and enhanced its activity, causing acceleration of apoptosis of aphid cells (Zhao et al 2020). Additionally, galectin-14 was reported to compete with Cry11Aa for binding to BBMVs and ALP1 in Aedes aegypti to prevent effective binding of the toxin to receptors (Zhang et al 2018). Hence, the mechanisms for Cry toxins against insects are believed to be much more complicated than before.…”

Section: Introductionmentioning

confidence: 99%

Indications for the potential of Cry1Ab1 for inhibiting aphid development and virus transmission

Jin

Zhang

Zhao

et al. 2022

Preprint

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Cry1A-type toxins are insecticidal proteins from Bacillus thuringiensis that are widely used to control Lepidoptera pests, and they are believed to be useless for the control of Hemiptera pests. In this paper, the purified Cry1Ab1 toxic core rarely killed peach aphids (Myzus persicae), as its Lethal Concentration 50 (LC50) was up to 1308.6 μg/ml, as measured using the membrane-encapsulation method. We then identified the proteins that bind to the Cry1Ab1 toxic core in M. persicae using pull-down assays and liquid chromatography−tandem mass spectrometry (LC-MS/MS), and then analyzed the associated functions of these proteins using the STRING database. GPN-loop GTPase 2, beta-actin, ATP synthase subunit alpha and an unknown and annotated protein, which are mainly involved in cell phagocytosis, RNA polymerase, cellular oxidative phosphorylation and other related functions, were the proteins that bound to the Cry1Ab1 toxic core. Indications from docking showed that Cry1Ab1 toxic core, ATP synthase subunit alpha and beta-actin or Cry1Ab1 toxic core, ATP synthase subunit alpha and GPN-loop GTPase 2 being a complex to exert effects. Based on the identification of Cry1Ab1-binding proteins from M.persicae, we presented here the molecular clues that Cry1A exert a negative effect on aphid growth and development, and we also proposed that Cry protein had the ability to disturb virus transmission by aphid. The two indications will result in new insights for aphid-effective Cry evaluation and improvement.

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“…Many animal lectins are glycosylated, but the galectin family seems to be an exception [55,56]. Galectins have been reported in a few insects, including D. melanogaster, A. gambiae, A. aegypti, and the sand fly Phlebotomus papatasi [57][58][59][60][61]. Galectins expressed in the insect gut have been shown to participate in the neutralization of bacterial toxins [57,58].…”

Section: Insect Lectinsmentioning

confidence: 99%

Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?

Chen

Schutter

Damme

et al. 2021

Insects

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Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions. Many plant lectins were identified as exogenous stimuli of vertebrate immunity. Despite being the largest and most diverse taxon on earth, the study of lectins and their functions in insects is lagging behind. In insects, research on lectins and their biological importance has mainly focused on the C-type lectin (CTL) family, limiting our global understanding of the function of insect lectins and their role in insect immunity. In contrast, plant lectins have been well characterized and the immunomodulatory effects of several plant lectins have been documented extensively in vertebrates. This information could complement the missing knowledge on endogenous insect lectins and contribute to understanding of the processes and mechanisms by which lectins participate in insect immunity. This review summarizes existing studies of immune responses stimulated by endogenous or exogenous lectins. Understanding how lectins modulate insect immune responses can provide insight which, in turn, can help to elaborate novel ideas applicable for the protection of beneficial insects and the development of novel pest control strategies.

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Aedes aegypti Galectin Competes with Cry11Aa for Binding to ALP1 To Modulate Cry Toxicity

Cited by 19 publications

References 43 publications

A new bacteria‐free strategy induced by MaGal2 facilitates pinewood nematode escape immune response from its vector beetle

A new bacteria‐free strategy induced by MaGal2 facilitates pinewood nematode escape immune response from its vector beetle

Indications for the potential of Cry1Ab1 for inhibiting aphid development and virus transmission

Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?

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