Interaction of
            <i>Bacillus thuringiensis</i>
            Vegetative Insecticidal Protein with Ribosomal S2 Protein Triggers Larvicidal Activity in
            <i>Spodoptera frugiperda</i>

Singh, Gatikrushna; Sachdev, Bindiya; Sharma, Nathilal; Seth, Rakesh; Bhatnagar, Raj K.

doi:10.1128/aem.01552-10

Cited by 69 publications

(63 citation statements)

References 22 publications

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“…Silencing of the S2 gene reduced the toxicity of Vip3A to both Sf21 cells and fifth-instar S. litura larvae. Both S2 and Vip3Aa colocalized on the surface and in the cytoplasm of Sf21 cells, suggesting that the interaction takes place on the cell surface and, once pores are produced, that the Vip3-S2 complex internalizes (98). How this S2-Vip3A protein interaction could trigger the lysis of cells was not explained and remains unknown.…”

Section: Mode Of Actionmentioning

confidence: 99%

“…The first one was a 48-kDa protein from A. ipsilon with homology to a family of extracellular glycoproteins called tenascins, which could be associated with apoptotic processes (57). The second binding molecule was the S2 ribosomal protein from S. litura, identified as a Vip3A receptor in Sf21 cells (98). Silencing of the S2 gene reduced the toxicity of Vip3A to both Sf21 cells and fifth-instar S. litura larvae.…”

Section: Mode Of Actionmentioning

confidence: 99%

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Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

260

261

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SUMMARYEntomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no sequence similarity to Vip1 or Vip2 and is toxic to a wide variety of members of the Lepidoptera. Its mode of action has been shown to resemble that of the Cry proteins in terms of proteolytic activation, binding to the midgut epithelial membrane, and pore formation, although Vip3A proteins do not share binding sites with Cry proteins. The latter property makes them good candidates to be combined with Cry proteins in transgenic plants (Bacillus thuringiensis-treated crops [Bt crops]) to prevent or delay insect resistance and to broaden the insecticidal spectrum. There are commercially grown varieties of Bt cotton and Bt maize that express the Vip3Aa protein in combination with Cry proteins. For the most recently reported Vip4 family, no target insects have been found yet.

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Section: Mode Of Actionmentioning

confidence: 99%

Section: Mode Of Actionmentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

260

261

View full text Add to dashboard Cite

show abstract

“…In addition, some green fluorescence could be observed inside the epithelial cells, which could suggest internalization of Vip3Aa or a fragment of it. Results from a previous study with Sf21 insect cells also suggested that Vip3Aa internalized after binding to the cell membrane (37). Whether (2 g) was incubated with increasing amounts of 125 IVip3Aa for 90 min.…”

Section: Discussionmentioning

confidence: 99%

In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by ¹²⁵ I Radiolabeling

Chakroun

Ferré

2014

Appl Environ Microbiol

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Bacillus thuringiensis vegetative insecticidal proteins (Vip3A) have been recently introduced in important crops as a strategy to delay the emerging resistance to the existing Cry toxins. The mode of action of Vip3A proteins has been studied in Spodoptera frugiperda with the aim of characterizing their binding to the insect midgut. Immunofluorescence histological localization of Vip3Aa in the midgut of intoxicated larvae showed that Vip3Aa bound to the brush border membrane along the entire apical surface. The presence of fluorescence in the cytoplasm of epithelial cells seems to suggest internalization of Vip3Aa or a fragment of it. Successful radiolabeling and optimization of the binding protocol for the 125 I-Vip3Aa to S. frugiperda brush border membrane vesicles (BBMV) allowed the determination of binding parameters of Vip3A proteins for the first time. Heterologous competition using Vip3Ad, Vip3Ae, and Vip3Af as competitor proteins showed that they share the same binding site with Vip3Aa. In contrast, when using Cry1Ab and Cry1Ac as competitors, no competitive binding was observed, which makes them appropriate candidates to be used in combination with Vip3A proteins in transgenic crops.

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“…The synergistic interaction between antibiotics and ISR further increases resistance against pathogens (Jha et al 2011 ). The Bacillus thuringiensis , having the ability to produce insecticidal protein (Singh et al 2010a ), can be used as biocontrol agent.…”

Section: Biocontrol Activitymentioning

confidence: 99%

Plant–Microbe Interactions for Sustainable Agriculture: Fundamentals and Recent Advances

Nadeem

Naveed

Zahir

et al. 2013

Plant Microbe Symbiosis: Fundamentals and Advances

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Interaction of Bacillus thuringiensis Vegetative Insecticidal Protein with Ribosomal S2 Protein Triggers Larvicidal Activity in Spodoptera frugiperda

Cited by 69 publications

References 22 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by ¹²⁵ I Radiolabeling

Plant–Microbe Interactions for Sustainable Agriculture: Fundamentals and Recent Advances

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Interaction of Bacillus thuringiensis Vegetative Insecticidal Protein with Ribosomal S2 Protein Triggers Larvicidal Activity in Spodoptera frugiperda

Cited by 69 publications

References 22 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by 125 I Radiolabeling

Plant–Microbe Interactions for Sustainable Agriculture: Fundamentals and Recent Advances

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Product

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In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by ¹²⁵ I Radiolabeling