title: Identification of Bombyx mori midgut receptor for Bacillus thuringiensis insecticidal CryIA(a) toxin.
abstract: 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.
authors.affiliation: Department of Applied Biochemistry, Faculty of Applied Biological Science, Hiroshima University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Nagamatsu
authors.forename: S
authors.initials: S
authors.lastname: Toda
authors.forename: F
authors.initials: F
authors.lastname: Yamaguchi
authors.forename: M
authors.initials: M
authors.lastname: Ogo
authors.forename: M
authors.initials: M
authors.lastname: Kogure
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: Y
authors.initials: Y
authors.lastname: Shibata
authors.forename: T
authors.initials: T
authors.lastname: Katsumoto
mesh_terms: D000818:Animals; D000992:Antitoxins / Q000276:immunology; D001413:Bacillus thuringiensis / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism*; D001427:Bacterial Toxins; D012831:Bombyx / Q000378:metabolism*; D003720:Densitometry; D004064:Digestive System / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D004731:Endotoxins / Q000378:metabolism*; D006460:Hemolysin Proteins; D015151:Immunoblotting; D019476:Insect Proteins; D007306:Insecticides / Q000378:metabolism*; D007457:Iodine Radioisotopes; D037102:Lectins; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D008871:Microvilli / Q000378:metabolism / Q000648:ultrastructure; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism*
chemical_list: D000992:Antitoxins; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; C095416:Cry toxin receptors; D004731:Endotoxins; D006460:Hemolysin Proteins; D019476:Insect Proteins; D007306:Insecticides; D007457:Iodine Radioisotopes; D037102:Lectins; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; C030956:insecticidal crystal protein, Bacillus Thuringiensis