Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Isolation of multiple subspecies of Bacillus thuringiensis from a population of the European sunflower moth, Homoeosoma nebulella

Article Abstract:

The larvae of a laboratory colony of the European sunflower moth Homoeosoma nebulella contain five subspecies (subspp.) of Bacillus thuringiensis that produce different insecticidal proteins. The subspp. thuringiensis produces spherical crystals, thompsoni produces pyramidal crystals while the other subspp. produce bipyramidal crystals. The thuringiensis, aizawai and kurstaki subspp. are toxic to H. nebulella and are potential agents for use against this insect.

Author: Itoua-Apoyolo, C., Drif, L., Vassal, J.M., DeBarjac, H., Bossy, J.P., Leclant, F., Frutos, R.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Binding of Cyt1Aa and Cry11Aa toxins of Bacillus thuringiensis serovar israelensis to brush border membrane vesicles of Tipula paludosa (Diptera: Nematocera) and subsequent pore formation

Article Abstract:

The binding of crystal proteins, including Cyt1Aa and Cry11Aa toxins of Bacillus thuringiensis serovar israelensis to brush border membrane vesicles of Tipula paludosa (Diptera: Nematocera) is being explained. The reaction leads to high efficiency of pore formation, exhibiting a reduced activity of the Cry11Aa substrate.

Author: Real, Maria Dolores, Oestergaard, Jesko, Ehlers, Ralf-Udo, Martinez-Ramirez, Amparo C.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Analysis, Physiological aspects, Nematocides

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


A binding site for Bacillus thuringiensis Cry1Ab toxin is lost during larval development in two forest pests

Article Abstract:

Two forest pests appear to become partially resistant to the insect toxins produced by Bacillus thuringiensis. Both Thaumetopoea pityocampa and Lymantria monacha lose binding sites for the Cry1Ab toxin during larval development.

Author: Rausell, Carolina, Martinez-Ramirez, Amparo Consuelo, Garcia-Robles, Inmaculada, Real, Maria Dolores
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Insects, Insecticide resistance, Microbial insecticides, Insect larvae

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Bacillus thuringiensis, Moths
Similar abstracts:
  • Abstracts: Synergistic effect of the Bacillus thuringiensis toxins CryIAa and CryIAc on the gypsy moth, Lymantria dispar
  • Abstracts: Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles. Single-site mutations in the conserved alternating-arginine region affect ionic channels formed by CryLAa, a Bacillus thuringiensis toxin
  • Abstracts: Determination of a 12 kb nucleotide sequence around the 76 degree region of the Bacillus subtilis chromosome. Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of Bacillu subtilis chromosome containing genes for trehalose metabolism and acetoin utilization
  • Abstracts: The assimilation of sulfur from multiple sources and its correlation with expression of the sulfate-starvation-induced stimulon in Pseudomonas putida S-313
  • Abstracts: Characterization of cry genes in a Mexican Bacillus thuringiensis strain collection. Identification of a putative Mexican strain of Serratia entomophila pathogenic against root-damaging larvae of scarabaeidae (Coleoptera)
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.