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Applied and Environmental Microbiology, October 2005, p. 6276-6281, Vol. 71, No. 10
0099-2240/05/$08.00+0 doi:10.1128/AEM.71.10.6276-6281.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Patricia Gil,1
Nathalie Neisner,1
Jeroen Van Rie,1 and
Roger Frutos2*
Bayer BioScience N.V., Technologiepark 38, 9052 Gent, Belgium,1 CIRAD, TA 30/D, Campus International de Baillarguet, 34398 Montpellier Cedex 5, France2
Received 11 February 2005/ Accepted 18 May 2005
A novel vip3-related gene was identified in Bacillus thuringiensis. This novel gene is 2,406 bp long and codes for a 91-kDa protein (801 amino acids). This novel protein exhibits between 61 and 62% similarity with Vip3A proteins and is designated Vip3Ba1. Vip3Ba1 has several specific features. Differences between Vip3Ba1 and the Vip3A proteins are spread throughout the sequence but are more frequent in the C-terminal part from amino acid 456 onward. The regions containing the two proteolytic processing sites, which are highly conserved among the Vip3A toxins, are markedly different in Vip3Ba1. The pattern DCCEE (Asp Cys Cys Glu Glu) is repeated four times between position 463 and 483 in Vip3Ba1, generating the sequence 463-DCCEEDCCEEDCCEEDCCEE-483. This sequence, which is rich in negatively charged amino acids, also contains 73% of the cysteines present in Vip3Ba1. This repeated sequence is not present in Vip3A proteins. The Vip3Ba1protein was produced in Escherichia coli and tested against Ostrinia nubilalis and Plutella xylostella, and it generated significant growth delays but had no larvicidal effect, indicating that its host range might be different than that of Vip3A proteins.
Supplemental material for this article may be found at http://aem.asm.org/.
Present address: UR 1199, Laboratoire de Protéomique, INRA, 2 Place Viala, 34060 Montpellier Cedex 1, France.
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