Shared binding sites in lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A toxins

被引:30
作者
Herrero, S
González-Cabrera, J
Tabashnik, BE
Ferré, J
机构
[1] Univ Valencia, Dept Genet, E-46100 Burjassot, Valencia, Spain
[2] Univ Arizona, Dept Entomol, Tucson, AZ 85721 USA
关键词
D O I
10.1128/AEM.67.12.5729-5734.2001
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth (Plutella xylostella) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that Cry1Ja shares binding sites with Cry1A toxins. We tested this hypothesis in six moth and butterfly species, each from a different family: Cacyreas marshalli (Lycaenidae), Lobesia botrana (Tortricidae), Manduca sexta (Sphingidae), Pectinophora gossypiella (Gelechiidae), P. xylostella (Plutellidae), and Spodoptera exigua (Noctuidae). Although the extent of competition varied among species, experiments with biotinylated Cry1Ja and radiolabeled Cry1Ac showed that Cry1Ja and Cry1Ac competed for binding sites in all six species. A recent report also indicates shared binding sites for Cry1Ja and Cry1A toxins in Heliothis virescens (Noctuidae). Thus, shared binding sites for Cry1Ja and Cry1A occur in all lepidopteran species tested so far.
引用
收藏
页码:5729 / 5734
页数:6
相关论文
共 49 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]  
Ballester V, 1999, APPL ENVIRON MICROB, V65, P1413
[3]  
Ballester V, 1999, APPL ENVIRON MICROB, V65, P1900
[4]   LACK OF CROSS-RESISTANCE TO OTHER BACILLUS-THURINGIENSIS CRYSTAL PROTEINS IN A POPULATION OF PLUTELLA-XYLOSTELLA HIGHLY RESISTANT TO CRYIA(B) [J].
BALLESTER, V ;
ESCRICHE, B ;
MENSUA, JL ;
RIETHMACHER, GW ;
FERRE, J .
BIOCONTROL SCIENCE AND TECHNOLOGY, 1994, 4 (04) :437-443
[5]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[6]   A new aminopeptidase from diamondback moth provides evidence for a gene duplication event in Lepidoptera [J].
Chang, WXZ ;
Gahan, LJ ;
Tabashnik, BE ;
Heckel, DG .
INSECT MOLECULAR BIOLOGY, 1999, 8 (02) :171-177
[7]   Bacillus thuringiensis toxin-mediated insect resistance in plants [J].
de Maagd, RA ;
Bosch, D ;
Stiekema, W .
TRENDS IN PLANT SCIENCE, 1999, 4 (01) :9-13
[8]   Domain III of the Bacillus thuringiensis delta-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N [J].
de Maagd, RA ;
Bakker, PL ;
Masson, L ;
Adang, MJ ;
Sangadala, S ;
Stiekema, W ;
Bosch, D .
MOLECULAR MICROBIOLOGY, 1999, 31 (02) :463-471
[9]   Cloning and characterization of Manduca sexta and Plutella xylostella midgut aminopeptidase N enzymes related to Bacillus thuringiensis toxin-binding proteins [J].
Denolf, P ;
Hendrickx, K ;
VanDamme, J ;
Jansens, S ;
Peferoen, M ;
Degheele, D ;
VanRie, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 248 (03) :748-761
[10]  
Donovan W. P., 1994, U.S. Patent, Patent No. [5322687, 6, 322, 687]