Identification of Bombyx mori midgut receptor for Bacillus thuringiensis insecticidal CryIA(a) toxin

As part of a study of the mechanism by which Bacillus thuringiensis insecticidal crystal protein acts, a Bombyx mori receptor to the CryIA(a) toxin specific for lepidopterans was examined. Histological examination showed that the toxin acted on the brush-border membrane of the midgut columnar cells...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998-04, Vol.62 (4), p.718-726
Main Authors: Nagamatsu, Y. (Hiroshima Univ., Fukuyama (Japan). Faculty of Applied Biological Science), TOda, S, Yamaguchi, F, Ogo, M, Kogure, M, Nakamura, M, Shibata, Y, Katsumoto, T
Format: Article
Language:English
Subjects:
Animals
ANTIBODIES
ANTICORPS
ANTICUERPOS
Antitoxins - immunology
BACILLUS THURINGIENSIS
Bacillus thuringiensis - metabolism
Bacterial Proteins - metabolism
Bacterial Toxins
Biological and medical sciences
Biological control
biopesticide
Bombyx - metabolism
BOMBYX MORI
Control
Densitometry
Digestive System - enzymology
Digestive System - metabolism
Digestive System - ultrastructure
Electrophoresis, Polyacrylamide Gel
Endotoxins - metabolism
Fundamental and applied biological sciences. Psychology
GLICOPROTEINAS
GLYCOPROTEINE
GLYCOPROTEINS
Hemolysin Proteins
IDENTIFICACION
IDENTIFICATION
Immunoblotting
IMMUNOLOGICAL TECHNIQUES
Insect Proteins
INSECTICIDAS
INSECTICIDE
INSECTICIDES
Insecticides - metabolism
INTESTIN
INTESTINES
INTESTINOS
Iodine Radioisotopes
Lectins
Membrane Proteins - metabolism
Microbiology
MICROSCOPIA
MICROSCOPIE
MICROSCOPY
Microscopy, Electron
Microvilli - metabolism
Microvilli - ultrastructure
Mycology
Pathogenicity, host-agent relations, miscellaneous strains, epidemiology
Phytopathology. Animal pests. Plant and forest protection
Protein Binding
Protozoa. Invertebrates
receptor
Receptors, Cell Surface - metabolism
silkworm
TECHNIQUE IMMUNOLOGIQUE
TECNICAS INMUNOLOGICAS
toxin
TOXINAS
TOXINE
TOXINS
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Summary:As part of a study of the mechanism by which Bacillus thuringiensis insecticidal crystal protein acts, a Bombyx mori receptor to the CryIA(a) toxin specific for lepidopterans was examined. Histological examination showed that the toxin acted on the brush-border membrane of the midgut columnar cells and broke its infolding structure, causing cell lysis. The membrane vesicles were purified, and a 175-kDa protein binding the toxin was found that accounted for some 0.015% of membrane proteins. The protein, designated BtR175, was a glycoprotein that reacted with concanavalin A. Anti-BtR antibodies inhibited the binding of toxin to membrane vesicles in vitro and decreased the effect of the toxin to silkworms in vivo. BtR175, although found in the gut, was not found in fat bodies, integument, or silk glands. These results indicated that BtR175 was the receptor protein for the insecticidal toxin. Proteins (137 and 107 kDa) binding the CryIA(a) toxin also were found in the gut membranes of Tenebrio moritor larvae, a coleopteran not sensitive to the toxin. The specificity of the toxin could not be explained only in term of the existence of its binding protein
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.62.718