Resistance of Trichoplusia ni to Bacillus thuringiensis Toxin Cry1Ac Is Independent of Alteration of the Cadherin-Like Receptor for Cry Toxins

Autor: Lihua Huang, Ping Wang, Wendy Kain, Kasorn Tiewsiri, Xin Zhang
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Insecticides
Agricultural Biotechnology
Applied Microbiology
ATP-binding cassette transporter
Genes
Insect
Plant Science
Gene mutation
Moths
Biochemistry
Insecticide Resistance
Hemolysin Proteins
Bacillus thuringiensis
Trichoplusia
Cloning
Molecular
Plant Pests
Multidisciplinary
biology
Genetically Modified Organisms
Agriculture
Cadherins
Larva
Medicine
Insect Proteins
Agrochemicals
Research Article
Biotechnology
DNA
Complementary
Science
Molecular Sequence Data
Receptors
Cell Surface
Integrated Control
Bacterial Proteins
Animals
Amino Acid Sequence
RNA
Messenger
Pesticides
Pest Control
Biological
Gene
Biology
Transgenic Plants
Bacillus thuringiensis Toxins
Base Sequence
Cadherin
fungi
Proteins
Midgut
Plant Pathology
biology.organism_classification
Molecular biology
Endotoxins
Cry1Ac
Plant Biotechnology
Pest Control
Zoology
Entomology
Zdroj: PLoS ONE
PLoS ONE, Vol 7, Iss 5, p e35991 (2012)
ISSN: 1932-6203
Popis: Alteration of binding sites for Bacillus thuringiensis (Bt) toxins in insect midgut is the major mechanism of high-level resistance to Bt toxins in insects. The midgut cadherin is known to be a major binding protein for Bt Cry1A toxins and linkage of Bt-resistance to cadherin gene mutations has been identified in lepidopterans. The resistance to Bt toxin Cry1Ac evolved in greenhouse populations of Trichoplusia ni has been identified to be associated with the down-regulation of an aminopeptidase N (APN1) gene by a trans-regulatory mechanism and the resistance gene has been mapped to the locus of an ABC transporter (ABCC2) gene. However, whether cadherin is also involved with Cry1Ac-resistance in T. ni requires to be understood. Here we report that the Cry1Ac-resistance in T. ni is independent of alteration of the cadherin. The T. ni cadherin cDNA was cloned and the cadherin sequence showed characteristic features known to cadherins from Lepidoptera. Various T. ni cadherin gene alleles were identified and genetic linkage analysis of the cadherin alleles with Cry1Ac-resistance showed no association of the cadherin gene with the Cry1Ac-resistance in T. ni. Analysis of cadherin transcripts showed no quantitative difference between the susceptible and Cry1Ac-resistant T. ni larvae. Quantitative proteomic analysis of midgut BBMV proteins by iTRAQ-2D-LC-MS/MS determined that there was no quantitative difference in cadherin content between the susceptible and the resistant larvae and the cadherin only accounted for 0.0014% (mol%) of the midgut BBMV proteins, which is 1/300 of APN1 in molar ratio. The cadherin from both the susceptible and resistant larvae showed as a 200-kDa Cry1Ac-binding protein by toxin overlay binding analysis, and nano-LC-MS/MS analysis of the 200-kDa cadherin determined that there is no quantitative difference between the susceptible and resistant larvae. Results from this study indicate that the Cry1Ac-resistance in T. ni is independent of cadherin alteration.
Databáze: OpenAIRE
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