A screening of five Bacillus thuringiensis Vip3A proteins for their activity against lepidopteran pests

Escudero, Íñigo Ruiz de; Banyuls, Núria; Bel, Yolanda; Maeztu, Mireya; Escriche, Baltasar; Muñoz, Delia; Caballero, Primitivo; Ferré, Juan

doi:10.1016/j.jip.2014.01.006

Cited by 73 publications

(49 citation statements)

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“…The N terminus of Vip3 is highly conserved, while the C-terminal region is highly variable (16,50,53) (Fig. 7); thus, the C-terminal region was proposed to be involved in target specificity (53).…”

Section: Protein Structure and Functionmentioning

confidence: 99%

“…On the other hand, other species susceptible to Cry proteins, such as Ostrinia nubilalis (Lepidoptera: Crambidae), Culex quinquefasciatus (Diptera: Culicidae), and Chironomus tepperi (Diptera: Chironomidae), are marginally or not susceptible to any Vip3A protein tested (15,55,65,66). With Vip3 proteins, depending on the Vip3 protein and the insect species being considered, it is not uncommon to find that while mortality is reached with a high concentration of Vip3 protein, strong growth inhibition (or even complete growth arrest) is observed with lower concentrations (16,62,(67)(68)(69). Therefore, "functional mortality" (dead insects plus those remaining at larval instar L1) better represents the effectiveness of the Vip3 protein in these cases (16,70,71).…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…With Vip3 proteins, depending on the Vip3 protein and the insect species being considered, it is not uncommon to find that while mortality is reached with a high concentration of Vip3 protein, strong growth inhibition (or even complete growth arrest) is observed with lower concentrations (16,62,(67)(68)(69). Therefore, "functional mortality" (dead insects plus those remaining at larval instar L1) better represents the effectiveness of the Vip3 protein in these cases (16,70,71). Table 2 summarizes the results that have been reported on the insecticidal activity of proteins of the Vip3Aa subfamily.…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…Only the values for the protoxin form are given, since there are no reports indicating relevant differences in the insecticidal activities of the protoxin and the activated forms (16), with the exceptions of the activities of Vip3Aa16 against S. exigua and Vip3Af1 against Spodoptera frugiperda (Lepidoptera: Noctuidae) (71,72). Despite the very small differences among Vip3Aa sequences, some proteins may exhibit significant differences in toxicity to the same insect species (16,59,73).…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…Figure 2 shows a dendrogram with the hierarchy of the Vip proteins based on their degree of amino acid identity. Vip1 and Vip2 act as binary toxins for some members of the Coleoptera and Hemiptera (7,(11)(12)(13)(14), and Vip3 is active against a wide range of species of Lepidoptera (15,16). No target insects have as yet been found for Vip4.…”

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confidence: 99%

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Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

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243

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: Protein Structure and Functionmentioning

confidence: 99%

Section: Insecticidal Activitymentioning

confidence: 99%

Section: Insecticidal Activitymentioning

confidence: 99%

Section: Insecticidal Activitymentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

Self Cite

243

261

View full text Add to dashboard Cite

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Bacillus thuringiensis vegetative insecticidal protein family Vip3A and mode of action against pest Lepidoptera

Chakrabarty

Jin

et al. 2020

Pest Management Science

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Vip3A proteins are widely used for controlling pest Lepidoptera. Different binding sites with different receptors in the insect midgut membrane and lack of cross‐resistance with crystal (Cry) proteins enhance their applicability, as both single proteins and proteins pyramided with Cry proteins in transgenic Bt crops. Vip3A proteins are effective but there is relatively little information about their structure, function, activation, specificity, and mode of action. In addition, the mechanism of insect resistance to these proteins is unknown. Phylogenetic analysis and multiple sequence alignment showed that Vip3A proteins are genetically distant from Cry proteins. The mode of action and insecticidal activity of Vip3A proteins are discussed in this review. This review also provides detailed information about the Vip3A protein family that may aid in the design of more efficient pest management strategies in response to insect resistance to insecticidal proteins. © 2020 Society of Chemical Industry

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