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Applied and Environmental Microbiology, May 1999, p. 1900-1903, Vol. 65, No. 5
Department of Genetics, Universitat de
València, 46100-Burjassot (València),
Spain,1 and DLO-Centre for Plant
Breeding and Reproduction Research, 6700 AA Wageningen, The
Netherlands2
Received 5 November 1998/Accepted 9 February 1999
The toxic fragment of Bacillus thuringiensis crystal
proteins consists of three distinct structural domains. There is
evidence that domain I is involved in pore formation and that domain II is involved in receptor binding and specificity. It has been found that, in some cases, domain III is also important in determining specificity. Furthermore, involvement of domain III in binding has also
been reported recently. To investigate the role of toxin domains in the
diamondback moth (Plutella xylostella), we used hybrid
toxins with domain III substitutions among Cry1C, Cry1E, and Cry1Ab.
Neither Cry1E nor G27 (a hybrid with domains I and II from Cry1E and
domain III from Cry1C) was toxic, whereas Cry1C and F26 (the reciprocal
hybrid) were equally toxic. H04 (a hybrid with domains I and II from
Cry1Ab and domain III from Cry1C) showed toxicity that was of a similar
level as that of Cry1Ab and significantly higher than that of Cry1C.
Binding assays with 125I-Cry1C showed that Cry1C and F26
competed for the same binding sites on midgut membrane vesicles,
whereas Cry1E, G27, and H04 did not bind to these sites. Our results
show that, in contrast to findings in other insects for the toxins and
hybrids used here, toxin specificity as well as specificity of binding
to membrane vesicles in the diamondback moth is mediated by domain II
(and/or I) and not by domain III.
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Role of Bacillus thuringiensis Toxin
Domains in Toxicity and Receptor Binding in the Diamondback
Moth
*
Corresponding author. Mailing address: Department of
Genetics, Universitat de València, Av. Dr. Moliner 50, 46100-Burjassot (València), Spain. Phone: 34-96-386-4506. Fax:
34-96-398-3029. E-mail: Juan.Ferre{at}uv.es.
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