Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers

The receptor binding step in the molecular mode of action of five δ‐endotoxins (Cry1Ab, Cry1Ac, Cry1C, Cry2A, and Cry9C) from Bacillus thuringiensis was examined to find toxins with different receptor sites in the midgut of the striped stem borer (SSB) Chilo suppressalis (Walker) and yellow stem bor...

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Main Authors: Alcantara, Edwin P., Aguda, Remedios M., Curtiss, April, Dean, Donald H., Cohen, Michael B.
Format: Journal Article
Language:Inglés
Published: Wiley 2004
Subjects:
Online Access:https://hdl.handle.net/10568/166803
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author Alcantara, Edwin P.
Aguda, Remedios M.
Curtiss, April
Dean, Donald H.
Cohen, Michael B.
author_browse Aguda, Remedios M.
Alcantara, Edwin P.
Cohen, Michael B.
Curtiss, April
Dean, Donald H.
author_facet Alcantara, Edwin P.
Aguda, Remedios M.
Curtiss, April
Dean, Donald H.
Cohen, Michael B.
author_sort Alcantara, Edwin P.
collection Repository of Agricultural Research Outputs (CGSpace)
description The receptor binding step in the molecular mode of action of five δ‐endotoxins (Cry1Ab, Cry1Ac, Cry1C, Cry2A, and Cry9C) from Bacillus thuringiensis was examined to find toxins with different receptor sites in the midgut of the striped stem borer (SSB) Chilo suppressalis (Walker) and yellow stem borer (YSB) Scirpophaga incertulas (Walker) (Lepidoptera: Pyralidae). Homologous competition assays were used to estimate binding affinities (Kcom) of 125I‐labelled toxins to brush border membrane vesicles (BBMV). The SSB BBMV affinities in decreasing order was: Cry1Ab = Cry1Ac > Cry9C > Cry2A > Cry1C. In YSB, the order of decreasing affinities was: Cry1Ac > Cry1Ab > Cry9C = Cry2A > Cry1C. The number of binding sites (Bmax) estimated by homologous competition binding among the Cry toxins did not affect toxin binding affinity (Kcom) to both insect midgut BBMVs. Results of the heterologous competition binding assays suggest that Cry1Ab and Cry1Ac compete for the same binding sites in SSB and YSB. Other toxins bind with weak (Cry1C, Cry2A) or no affinity (Cry9C) to Cry1Ab and Cry1Ac binding sites in both species. Cry2A had the lowest toxicity to 10‐day‐old SSB and Cry1Ab and Cry1Ac were the most toxic. Taken together, the results of this study show that Cry1Ab or Cry1Ac could be combined with either Cry1C, Cry2A, or Cry9C for more durable resistance in transgenic rice. Cry1Ab should not be used together with Cry1Ac because a mutation in one receptor site could diminish binding of both toxins. Arch. Insect Biochem. Physiol. 55:169–177, 2004. © 2004 Wiley‐Liss, Inc.
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spelling CGSpace1668032024-12-19T14:13:46Z Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers Alcantara, Edwin P. Aguda, Remedios M. Curtiss, April Dean, Donald H. Cohen, Michael B. bacillus thuringiensis transgenic rice chilo suppressalis scirpophaga incertulas endotoxins The receptor binding step in the molecular mode of action of five δ‐endotoxins (Cry1Ab, Cry1Ac, Cry1C, Cry2A, and Cry9C) from Bacillus thuringiensis was examined to find toxins with different receptor sites in the midgut of the striped stem borer (SSB) Chilo suppressalis (Walker) and yellow stem borer (YSB) Scirpophaga incertulas (Walker) (Lepidoptera: Pyralidae). Homologous competition assays were used to estimate binding affinities (Kcom) of 125I‐labelled toxins to brush border membrane vesicles (BBMV). The SSB BBMV affinities in decreasing order was: Cry1Ab = Cry1Ac > Cry9C > Cry2A > Cry1C. In YSB, the order of decreasing affinities was: Cry1Ac > Cry1Ab > Cry9C = Cry2A > Cry1C. The number of binding sites (Bmax) estimated by homologous competition binding among the Cry toxins did not affect toxin binding affinity (Kcom) to both insect midgut BBMVs. Results of the heterologous competition binding assays suggest that Cry1Ab and Cry1Ac compete for the same binding sites in SSB and YSB. Other toxins bind with weak (Cry1C, Cry2A) or no affinity (Cry9C) to Cry1Ab and Cry1Ac binding sites in both species. Cry2A had the lowest toxicity to 10‐day‐old SSB and Cry1Ab and Cry1Ac were the most toxic. Taken together, the results of this study show that Cry1Ab or Cry1Ac could be combined with either Cry1C, Cry2A, or Cry9C for more durable resistance in transgenic rice. Cry1Ab should not be used together with Cry1Ac because a mutation in one receptor site could diminish binding of both toxins. Arch. Insect Biochem. Physiol. 55:169–177, 2004. © 2004 Wiley‐Liss, Inc. 2004-04 2024-12-19T12:56:41Z 2024-12-19T12:56:41Z Journal Article https://hdl.handle.net/10568/166803 en Wiley Alcantara, Edwin P.; Aguda, Remedios M.; Curtiss, April; Dean, Donald H. and Cohen, Michael B. 2004. Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers. Arch Insect Biochem Physiol, Volume 55 no. 4 p. 169-177
spellingShingle bacillus thuringiensis
transgenic rice
chilo suppressalis
scirpophaga incertulas
endotoxins
Alcantara, Edwin P.
Aguda, Remedios M.
Curtiss, April
Dean, Donald H.
Cohen, Michael B.
Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title_full Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title_fullStr Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title_full_unstemmed Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title_short Bacillus thuringiensis delta-endotoxin binding to brush border membrane vesicles of rice stem borers
title_sort bacillus thuringiensis delta endotoxin binding to brush border membrane vesicles of rice stem borers
topic bacillus thuringiensis
transgenic rice
chilo suppressalis
scirpophaga incertulas
endotoxins
url https://hdl.handle.net/10568/166803
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