Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

Joel Gonzátlez-Cabrera, Baltasar Escriche, Bruce E Tabashnik, Juan Ferré

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1Ac, and Cry1Ja bound to a common binding site that was not shared by the other toxins tested. Reciprocal competition experiments with Cry1Ab, Cry1Ac, and Cry1Ja showed that these toxins do not bind to any additional binding sites. In the resistant strain, binding of 125I-Cry1Ac was not significantly affected; however, 125I-Cry1Ab did not bind to the BBMV. This result, along with previous data from this strain, shows that the resistance fits the "mode 1" pattern of resistance described previously in Plutella xylostella, Plodia interpunctella, and Heliothis virescens.

Original languageEnglish (US)
Pages (from-to)929-935
Number of pages7
JournalInsect Biochemistry and Molecular Biology
Volume33
Issue number9
DOIs
StatePublished - Sep 1 2003

Fingerprint

Pectinophora gossypiella
Bacillus thuringiensis
Bacilli
Brushes
Microvilli
toxins
Membranes
Cotton
brush border membrane vesicles
Binding Sites
Genetically Modified Plants
binding sites
cotton
Insects
pests
Plodia interpunctella
Experiments
Heliothis virescens
Plutella xylostella
microvilli

Keywords

  • Bacillus thuringiensis
  • Binding
  • Cotton
  • Cry toxins
  • Pectinophora gossypiella
  • Resistance

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry

Cite this

Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella). / Gonzátlez-Cabrera, Joel; Escriche, Baltasar; Tabashnik, Bruce E; Ferré, Juan.

In: Insect Biochemistry and Molecular Biology, Vol. 33, No. 9, 01.09.2003, p. 929-935.

Research output: Contribution to journalArticle

@article{b986fb272a484f76a33f9e84dca80d49,
title = "Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)",
abstract = "Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1Ac, and Cry1Ja bound to a common binding site that was not shared by the other toxins tested. Reciprocal competition experiments with Cry1Ab, Cry1Ac, and Cry1Ja showed that these toxins do not bind to any additional binding sites. In the resistant strain, binding of 125I-Cry1Ac was not significantly affected; however, 125I-Cry1Ab did not bind to the BBMV. This result, along with previous data from this strain, shows that the resistance fits the {"}mode 1{"} pattern of resistance described previously in Plutella xylostella, Plodia interpunctella, and Heliothis virescens.",
keywords = "Bacillus thuringiensis, Binding, Cotton, Cry toxins, Pectinophora gossypiella, Resistance",
author = "Joel Gonz{\'a}tlez-Cabrera and Baltasar Escriche and Tabashnik, {Bruce E} and Juan Ferr{\'e}",
year = "2003",
month = "9",
day = "1",
doi = "10.1016/S0965-1748(03)00099-7",
language = "English (US)",
volume = "33",
pages = "929--935",
journal = "Insect Biochemistry and Molecular Biology",
issn = "0965-1748",
publisher = "Elsevier Limited",
number = "9",

}

TY - JOUR

T1 - Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

AU - Gonzátlez-Cabrera, Joel

AU - Escriche, Baltasar

AU - Tabashnik, Bruce E

AU - Ferré, Juan

PY - 2003/9/1

Y1 - 2003/9/1

N2 - Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1Ac, and Cry1Ja bound to a common binding site that was not shared by the other toxins tested. Reciprocal competition experiments with Cry1Ab, Cry1Ac, and Cry1Ja showed that these toxins do not bind to any additional binding sites. In the resistant strain, binding of 125I-Cry1Ac was not significantly affected; however, 125I-Cry1Ab did not bind to the BBMV. This result, along with previous data from this strain, shows that the resistance fits the "mode 1" pattern of resistance described previously in Plutella xylostella, Plodia interpunctella, and Heliothis virescens.

AB - Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1Ac, and Cry1Ja bound to a common binding site that was not shared by the other toxins tested. Reciprocal competition experiments with Cry1Ab, Cry1Ac, and Cry1Ja showed that these toxins do not bind to any additional binding sites. In the resistant strain, binding of 125I-Cry1Ac was not significantly affected; however, 125I-Cry1Ab did not bind to the BBMV. This result, along with previous data from this strain, shows that the resistance fits the "mode 1" pattern of resistance described previously in Plutella xylostella, Plodia interpunctella, and Heliothis virescens.

KW - Bacillus thuringiensis

KW - Binding

KW - Cotton

KW - Cry toxins

KW - Pectinophora gossypiella

KW - Resistance

UR - http://www.scopus.com/inward/record.url?scp=0042740454&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0042740454&partnerID=8YFLogxK

U2 - 10.1016/S0965-1748(03)00099-7

DO - 10.1016/S0965-1748(03)00099-7

M3 - Article

C2 - 12915184

AN - SCOPUS:0042740454

VL - 33

SP - 929

EP - 935

JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

SN - 0965-1748

IS - 9

ER -