Asset Details
Do you wish to reserve the book?
Bacillus thuringiensis novel toxin Epp is toxic to mosquitoes and prodenia litura larvae
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Bacillus thuringiensis novel toxin Epp is toxic to mosquitoes and prodenia litura larvae
Do you wish to request the book?
Bacillus thuringiensis novel toxin Epp is toxic to mosquitoes and prodenia litura larvae
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Bacillus thuringiensis novel toxin Epp is toxic to mosquitoes and prodenia litura larvae
2020
Overview
As a pathogenic bacterium,
Bacillus thuringiensis
(
Bt
) has become an alternative to chemical insecticides in commercial agricultural to control forestry pests and mosquitoes. To prevent pest resistance, many novel
Bt
strains have been isolated. Strain S3580-1 (WGS: VHPX0000000) used in this research and originally isolated from Hainan Qixianling National Forest Park (China) showed significant toxicity to
Culex pipiens pallens
. Here, using whole genome sequencing, assembly, and bioinformatics analysis, the predicted S3580-1CG_5163 (GenBank Accession No. MK124137) gene-encoded protein was found to share low homology with known toxins designated by the
Bt
toxin nomenclature system. It was considered to be an ETX/MTX2-type toxin and was designated Epp. Bioinformatics analysis showed that the predicted S3580-1CG_5163 gene-encoded protein Epp shared low identity with other known toxic protein sequences containing Cry-ETX/MTX conserved domains at the amino acid level, but significant similarity at the structural level. In addition, bioassays showed that Epp was toxic against
Spodoptera litura
(LC
50
296.133 μg/mL; 95% FL 200.555–471.318 μg/mL) and
Cx. pipiens pallens
(LC
50
322.193 μg/mL; 95% FL 238.217–477.243 μg/mL). On pathological observation, the peritrophic membrane of
Cx. pipiens pallens
larvae was degraded causing the midgut structure to become incomplete, resulting in larval death. Further bioassays are required to fully elucidate the insecticidal spectrum of the ETX/MTX2-type toxin Epp, and thereby provide future research directions.
Publisher
Springer International Publishing,Springer Nature B.V
Subject
/ Animals
/ Bacillus thuringiensis - chemistry
/ Bacillus thuringiensis Toxins - classification
/ Bacillus thuringiensis Toxins - toxicity
/ Bacterial and Fungal Pathogenesis - Research Paper
/ Biomedical and Life Sciences
/ China
/ E coli
/ Enzymes
/ Forestry
/ Genomes
/ Homology
/ Larva
/ Larvae
/ Microbial Genetics and Genomics
/ Midgut
/ Mycology
/ Pest Control, Biological - methods
/ Pests
/ Proteins
/ Software
/ Toxicity
/ Toxins
/ Trees
