Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae)

Carmen Sara Hernández-Rodríguez, Sergio Pérez-Guerrero, Hani K Aldebis, Enrique Vargas-Osuna, Juan Ferré

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larvae showed specific binding sites for Cry1Ac that are shared, with low affinity, by Cry1Ca and Cry1Fa.
Original languageEnglish
Pages (from-to)131-133
Number of pages3
JournalJournal of Invertebrate Pathology
Volume100
Issue number2
DOIs
Publication statusPublished - 2009

Fingerprint

Prays oleae
Yponomeutidae
Bacillus thuringiensis
moth
moths
instars
Lepidoptera
insect
insect proteins
brush border membrane vesicles
larva
protein
crop losses
larvae
groves
vesicle
midgut
insect pests
rearing
insecticide

Cite this

Hernández-Rodríguez, C. S., Pérez-Guerrero, S., Aldebis, H. K., Vargas-Osuna, E., & Ferré, J. (2009). Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae). Journal of Invertebrate Pathology, 100(2), 131-133. https://doi.org/10.1016/j.jip.2008.11.005

Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae). / Hernández-Rodríguez, Carmen Sara; Pérez-Guerrero, Sergio; Aldebis, Hani K; Vargas-Osuna, Enrique; Ferré, Juan.

In: Journal of Invertebrate Pathology, Vol. 100, No. 2, 2009, p. 131-133.

Research output: Contribution to journalArticle

Hernández-Rodríguez, CS, Pérez-Guerrero, S, Aldebis, HK, Vargas-Osuna, E & Ferré, J 2009, 'Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae)', Journal of Invertebrate Pathology, vol. 100, no. 2, pp. 131-133. https://doi.org/10.1016/j.jip.2008.11.005
Hernández-Rodríguez, Carmen Sara ; Pérez-Guerrero, Sergio ; Aldebis, Hani K ; Vargas-Osuna, Enrique ; Ferré, Juan. / Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae). In: Journal of Invertebrate Pathology. 2009 ; Vol. 100, No. 2. pp. 131-133.
@article{93da8c35dc094857b8e22283833b7a69,
title = "Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae)",
abstract = "The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larvae showed specific binding sites for Cry1Ac that are shared, with low affinity, by Cry1Ca and Cry1Fa.",
author = "Hern{\'a}ndez-Rodr{\'i}guez, {Carmen Sara} and Sergio P{\'e}rez-Guerrero and Aldebis, {Hani K} and Enrique Vargas-Osuna and Juan Ferr{\'e}",
year = "2009",
doi = "10.1016/j.jip.2008.11.005",
language = "English",
volume = "100",
pages = "131--133",
journal = "Journal of Invertebrate Pathology",
issn = "0022-2011",
publisher = "Elsevier Academic Press Inc",
number = "2",

}

TY - JOUR

T1 - Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera Yponomeutidae)

AU - Hernández-Rodríguez, Carmen Sara

AU - Pérez-Guerrero, Sergio

AU - Aldebis, Hani K

AU - Vargas-Osuna, Enrique

AU - Ferré, Juan

PY - 2009

Y1 - 2009

N2 - The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larvae showed specific binding sites for Cry1Ac that are shared, with low affinity, by Cry1Ca and Cry1Fa.

AB - The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larvae showed specific binding sites for Cry1Ac that are shared, with low affinity, by Cry1Ca and Cry1Fa.

UR - http://www.scopus.com/inward/record.url?scp=58649115807&partnerID=8YFLogxK

UR - http://dx.doi.org/10.1016/j.jip.2008.11.005

U2 - 10.1016/j.jip.2008.11.005

DO - 10.1016/j.jip.2008.11.005

M3 - Article

VL - 100

SP - 131

EP - 133

JO - Journal of Invertebrate Pathology

JF - Journal of Invertebrate Pathology

SN - 0022-2011

IS - 2

ER -