Location of the dipteran specificity region in a Lepidopteran-Dipteran crystal protein from Bacillus thuringiensis

Two highly related crystal protein genes from Bacillus thuringiensis subsp. kurstaki HD-1, designated cryIIA and cryIIB (previously named cryB1 and cryB2, respectively), were used to study host range specificity. Their respective gene products are 87% identical but exhibit different toxicity spectra...

Full description

Saved in:
Bibliographic Details
Published in:Journal of Bacteriology 1990-06, Vol.172 (6), p.2826-2832
Main Authors: Widner, W.R. (University of Washington, Seattle, WA), Whiteley, H.R
Format: Article
Language:English
Subjects:
amino acid sequence
Animals
BACILLUS THURINGIENSIS
Bacillus thuringiensis - analysis
Bacillus thuringiensis kurstaki
Bacterial Proteins - analysis
Bacterial Proteins - genetics
Bacterial Proteins - toxicity
Bacterial Toxins - analysis
Bacterial Toxins - toxicity
Bacteriology
Biological and medical sciences
biological control
Cloning, Molecular
Cricetinae
CryII protein
crystals
DIPTERA
Diptera - drug effects
Endotoxins
Fundamental and applied biological sciences. Psychology
GENE
Gene Expression
GENES
Genes, Bacterial
Hemolysin Proteins
LARVAS
LARVE
LEPIDOPTERA
Lepidoptera - drug effects
Microbiology
PARASITISME
PARASITISMO
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
PROTEINAS
PROTEINE
Structure-Activity Relationship
TOXICIDAD
TOXICITE
toxins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Two highly related crystal protein genes from Bacillus thuringiensis subsp. kurstaki HD-1, designated cryIIA and cryIIB (previously named cryB1 and cryB2, respectively), were used to study host range specificity. Their respective gene products are 87% identical but exhibit different toxicity spectra; CryIIA is toxic to both mosquito and tobacco hornworm larvae, whereas CryIIB is toxic only to the latter. Hybrids of the cryIIA and cryIIB genes were generated, and their resultant gene products were assayed for toxicity. A short segment of CryIIA corresponding to residues 307 through 382 was shown to be sufficient for altering host range specificity--i.e., when this region replaced the corresponding segment of CryIIB, the resulting hybrid protein acquired toxicity against mosquitoes. The CryIIA and CryIIB polypeptides differ by only 18 amino acids in this region, indicating that very few amino acid changes can have a substantial effect on the toxicity spectra of these proteins
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.172.6.2826-2832.1990