Fibroblast Growth Factor Receptor, a Novel Receptor for Vegetative Insecticidal Protein Vip3Aa

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Abstract

Vegetative insecticidal proteins (Vips), which are secreted by some Bacillus thuringiensis strains during vegetative growth, exhibit high virulence to many pests. Vip3A proteins have been used commercially both in some bio-insecticides and in transgenic crops; however, compared with insecticidal crystal proteins, the mechanism of action of Vip3A is still unclear. In this work, we indicated that the fibroblast growth factor receptor-like protein (Sf-FGFR) from the membrane of Sf9 cells could bind to Vip3Aa. The interaction between Vip3Aa and Sf-FGFR was confirmed by pull-down assays and dot blotting experiment in vitro. The binding affinity between Vip3Aa and extracellular regions of Sf-FGFR (GST-FGFR-N) was determined by microscale thermophoresis assay (MST). Moreover, Vip3Aa-Flag could be co-immunoprecipitated with Sf-FGFR-V5 ex vivo. Furthermore, knockdown of Sf-FGFR gene in Sf9 cells resulted in reducing the mortality of those cells to Vip3Aa. In summary, our data indicated that Sf-FGFR is a novel receptor for Vip3Aa.

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Protein-binding assays in biological liquids using microscale thermophoresis.

Christoph J Wienken, Philipp Baaske, Ulrich Rothbauer … (2010)

Protein interactions inside the human body are expected to differ from the situation in vitro. This is crucial when investigating protein functions or developing new drugs. In this study, we present a sample-efficient, free-solution method, termed microscale thermophoresis, that is capable of analysing interactions of proteins or small molecules in biological liquids such as blood serum or cell lysate. The technique is based on the thermophoresis of molecules, which provides information about molecule size, charge and hydration shell. We validated the method using immunologically relevant systems including human interferon gamma and the interaction of calmodulin with calcium. The affinity of the small-molecule inhibitor quercetin to its kinase PKA was determined in buffer and human serum, revealing a 400-fold reduced affinity in serum. This information about the influence of the biological matrix may allow to make more reliable conclusions on protein functionality, and may facilitate more efficient drug development.

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Role of receptors in Bacillus thuringiensis crystal toxin activity.

Craig R Pigott, David J Ellar (2007)

Bacillus thuringiensis produces crystalline protein inclusions with insecticidal or nematocidal properties. These crystal (Cry) proteins determine a particular strain's toxicity profile. Transgenic crops expressing one or more recombinant Cry toxins have become agriculturally important. Individual Cry toxins are usually toxic to only a few species within an order, and receptors on midgut epithelial cells have been shown to be critical determinants of Cry specificity. The best characterized of these receptors have been identified for lepidopterans, and two major receptor classes have emerged: the aminopeptidase N (APN) receptors and the cadherin-like receptors. Currently, 38 different APNs have been reported for 12 different lepidopterans. Each APN belongs to one of five groups that have unique structural features and Cry-binding properties. While 17 different APNs have been reported to bind to Cry toxins, only 2 have been shown to mediate toxin susceptibly in vivo. In contrast, several cadherin-like proteins bind to Cry toxins and confer toxin susceptibility in vitro, and disruption of the cadherin gene has been associated with toxin resistance. Nonetheless, only a small subset of the lepidopteran-specific Cry toxins has been shown to interact with cadherin-like proteins. This review analyzes the interactions between Cry toxins and their receptors, focusing on the identification and validation of receptors, the molecular basis for receptor recognition, the role of the receptor in resistant insects, and proposed models to explain the sequence of events at the cell surface by which receptor binding leads to cell death.

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Integrative molecular profiling of triple negative breast cancers identifies amplicon drivers and potential therapeutic targets

Nicholas Turner, Maryou Lambros, Hugo Horlings … (2010)

Triple negative breast cancers (TNBCs) have a relatively poor prognosis and cannot be effectively treated with current targeted therapies. We searched for genes that have the potential to be therapeutic targets by identifying genes consistently over-expressed when amplified. Fifty-six TNBCs were subjected to high-resolution microarray-based comparative genomic hybridisation (aCGH), of which 24 were subjected to genome-wide gene expression analysis. TNBCs were genetically heterogeneous; no individual focal amplification was present at high frequency, although 78.6% of TNBCs harboured at least one focal amplification. Integration of aCGH and expression data revealed 40 genes significantly overexpressed when amplified, including the known oncogenes and potential therapeutic targets, FGFR2 (10q26.3), BUB3 (10q26.3), RAB20 (13q34), PKN1 (19p13.12), and NOTCH3 (19p13.12). We identified two TNBC cell lines with FGFR2 amplification, which both had constitutive activation of FGFR2. Amplified cell lines were highly sensitive to FGFR inhibitor PD173074, and to RNAi silencing of FGFR2. Treatment with PD173074 induced apoptosis resulting partly from inhibition of PI3K-AKT signalling. Independent validation using publicly available aCGH datasets revealed FGFR2 gene was amplified in 4% (6/165) of TNBC, but not in other subtypes (0/214, p=0.0065). Our analysis demonstrates that TNBCs are heterogeneous tumours with amplifications of FGFR2 in a subgroup of tumours.

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Author and article information

Journal

Journal ID (nlm-ta): Toxins (Basel)

Journal ID (iso-abbrev): Toxins (Basel)

Journal ID (publisher-id): toxins

Title: Toxins

Publisher: MDPI

ISSN (Electronic): 2072-6651

Publication date (Electronic): 18 December 2018

Publication date Collection: December 2018

Volume: 10

Issue: 12

Electronic Location Identifier: 546

Affiliations

[1 ]Department of Microbiology, College of Life Sciences, Nankai University, Tianjin 300071, China; jiangkun@ 123456sdu.edu.cn (K.J.); xiaoyuehou@ 123456mail.nankai.edu.cn (X.H.); luhan0325@ 123456mail.nankai.edu.cn (L.H.); tantongtong@ 123456mail.nankai.edu.cn (T.T.); caozhanglei@ 123456mail.nankai.edu.cn (Z.C.)

[2 ]State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China

[3 ]Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin 300071, China

[4 ]Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin 300071, China

Author notes

[* ]Correspondence: caijun@ 123456nankai.edu.cn

[†]

These authors contributed equally to this work.

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Jun Cai https://orcid.org/0000-0002-5194-3629

Article

Publisher ID: toxins-10-00546

DOI: 10.3390/toxins10120546

PMC ID: 6315849

PubMed ID: 30567360

SO-VID: 668080b3-e7c3-4c63-a40c-9e551fbe4f87

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Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Fibroblast Growth Factor Receptor, a Novel Receptor for Vegetative Insecticidal Protein Vip3Aa

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Most cited references 17

Protein-binding assays in biological liquids using microscale thermophoresis.

Role of receptors in Bacillus thuringiensis crystal toxin activity.

Integrative molecular profiling of triple negative breast cancers identifies amplicon drivers and potential therapeutic targets

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