Combined analysis of supernatant-based feeding bioassays and PCR as a first-tier screening strategy for Vip -derived activities in Bacillus thuringiensis strains effective against tropical fall armyworm

Loguercio, Leandro Lopes; Barreto, Marlen; Rocha, T. L.; Santos, Carlos; Teixeira, F. F.; Paiva, Edílson

doi:10.1046/j.1365-2672.2002.01694.x

Cited by 30 publications

(42 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…vip3 genes are ϳ2.4 kb in length, and they are normally carried on large plasmids (43,45), although in some cases, they have been proposed to be located in the bacterial chromosome (46). Many strategies for screening of B. thuringiensis isolates have been performed with the aim of isolating new vip3 genes (19,20,25,42,(46)(47)(48)(49)(50)(51)(52). At the time of writing of this review, there have been 54 vip3Aa, 2 vip3Ab, 1 vip3Ac, 4 vip3Ad, 1 vip3Ae, 3 vip3Af, 15 vip3Ag, 1 vip3Ah, 1 vip3Ai, 2 vip3Ba, 3 vip3Bb, and 4 vip3Ca genes reported (9).…”

Section: The Vip3 Lepidopteran-active Proteinmentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

254

261

View full text Add to dashboard Cite

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.

show abstract

Section: The Vip3 Lepidopteran-active Proteinmentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

254

261

View full text Add to dashboard Cite

show abstract

“…A massa molecular das pró-toxinas Cry está compreendida entre 130 e 135 kDa (Lightwood et al, 2000), enquanto a das pró-toxinas Vip3A é de 88,5 kDa (Loguercio et al, 2002 vip3Aa,vip3Ae,vip3Af,cry1Aa,cry1Ab,cry1Ac, cry1Ca e cry1Ea. MM, marcador de massa molecular (kDa).…”

Section: Resultsunclassified

Interação de proteínas Cry1 e Vip3A de Bacillus thuringiensis para controle de lepidópteros-praga

Crialesi-Legori

Davolos

Lemes

et al. 2014

Pesq. agropec. bras.

View full text Add to dashboard Cite

Resumo -O objetivo deste trabalho foi avaliar a suscetibilidade das lagartas Anticarsia gemmatalis (Lepidoptera: Erebidae) e Chrysodeixis includens (Lepidoptera: Noctuidae) às proteínas Cry1 e Vip3A, bem como determinar se há a interação entre essas proteínas no controle das duas espécies. Bioensaios com as proteínas isoladas e em combinações foram realizados, e as concentrações letais CL 50 e CL 90 foram estimadas para cada condição. As proteínas Cry1Aa, Cry1Ac e Vip3Af foram as mais efetivas no controle de A. gemmatalis, enquanto Cry1Ac, Vip3Aa e Vip3Af foram mais efetivas no de C. includens. As proteínas Cry1Ac e Cry1Ca causaram maior inibição do desenvolvimento das larvas sobreviventes à CL 50 , em ambas as espécies. Combinações entre Vip3A e Cry1 apresentam efeito sinérgico no controle das espécies e a combinação Vip3Aa+Cry1Ea destaca-se no controle de A. gemmatalis e C. includens. Essas proteínas combinadas são promissoras na construção de plantas piramidadas, para o controle simultâneo das pragas.Termos para indexação: Anticarsia gemmatalis, Chrysodeixis includens, manejo da resistência, piramidação de genes, sinergismo, soja transgênica. Interaction of Cry1 and Vip3A proteins of Bacillus thuringiensis for the control of lepidopteran insect pestsAbstract -The objective of this work was to evaluate the susceptibility of Anticarsia gemmatalis (Lepidoptera: Erebidae) and Chrysodeixis includens (Lepidoptera: Noctuidae) caterpillars to Cry1 and Vip3A proteins, as well as to determine if there is any interaction between these proteins on the control of the two species. Bioassays with both isolated and combined proteins were carried out, and lethal concentrations LC 50 and LC 90 were estimated for each condition. Cry1Aa, Cry1Ac, and Vip3Af were the more effective proteins for the control of A. gemmatalis, while Cry1Ac, Vip3Aa, and Vip3Af were more effective for the control of C. includens. Cry1Ac and Cry1Ca proteins caused the highest inhibition to the development of larvae that survived the LC 50 dose in both species. Different combinations of Vip3A and Cry1 have synergistic effect in the control of both species, and the combination Vip3Aa + Cry1Ea showed an outstanding control of A. gemmatalis and C. includens. These proteins are promising for building pyramided plants for the simultaneous control of the pests.

show abstract

“…Há evidências de que as proteínas Vip3Aa ligam-se a receptores diferentes dos das proteínas Cry1, na membrana epitelial do intestino médio dos insetos-praga (Sena et al, 2009;Hamadou-Charfi et al, 2013). Esta é uma informação relevante para o manejo da resistência, uma vez que alterações que diminuem a ligação das proteínas com os receptores estão associadas a elevados níveis de resistência às toxinas Cry (Ferré & Van Rie, 2002 Loguercio et al (2002). A segunda linhagem é considerada padrão para vários genes cry1A e cry2, além de também possuir o gene vip3Aa33 -acesso número GU073128 GenBank (2014a), cuja sequência foi submetida por Sauka et al (2012).…”

Section: Introductionunclassified

Relação entre toxicidade de proteínas Vip3Aa e sua capacidade de ligação a receptores intestinais de lepidópteros-praga

Marucci

Figueiredo

Tezza

et al. 2015

Pesq. agropec. bras.

View full text Add to dashboard Cite

Relationship between toxicity of Vip3Aa proteins and their binding capacity to intestine receptors of lepidopteran pestsAbstract -The objective of this work was to evaluate the toxicity of new Vip3Aa proteins and their binding capacity to brush-border membrane vesicles (BBMV) in the intestine of Spodoptera frugiperda, Anticarsia gemmatalis, and Heliothis virescens neonate larvae. The proteins expressed by the genes vip3Aa42 and vip3Aa43 showed toxicity to S. frugiperda (LC 50 of 78.2 and 113 ng cm -2, respectively) and A. gemmatalis (LC 50 of 239.2 and 57.5 ng cm -2 , respectively), but they showed low toxicity to H. virescens (LC 50 >5,000 ng cm -2 ). BBMV binding assays showed that the proteins bind effectively to the receptors on vesicles of the evaluated species, but this binding capacity is only effective on the activation of toxicity to the evaluated populations of S. frugiperda and A. gemmatalis.

show abstract

Combined analysis of supernatant-based feeding bioassays and PCR as a first-tier screening strategy for Vip -derived activities in Bacillus thuringiensis strains effective against tropical fall armyworm

Cited by 30 publications

References 19 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Interação de proteínas Cry1 e Vip3A de Bacillus thuringiensis para controle de lepidópteros-praga

Relação entre toxicidade de proteínas Vip3Aa e sua capacidade de ligação a receptores intestinais de lepidópteros-praga

Contact Info

Product

Resources

About