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.
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http://dx.doi.org/10.1128/AEM.71.10.6276-6281.2005 | DOI Listing |
Int J Mol Sci
December 2024
Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Developing simple and efficient multi-gene expression systems is crucial for multi-trait improvement or bioproduction in transgenic plants. In previous research, an -based bicistronic system from the nonpathogenic fungus efficiently expressed multiple enzyme proteins in yeast and maize, and the heterologous enzymes successfully performed their catalytic activity to reconstruct the biosynthetic pathway in the host organism. Unlike enzyme proteins, some heterologous functional proteins (such as insecticidal proteins) are dose-dependent and they need to express sufficient levels to perform their biological functions.
View Article and Find Full Text PDFPLoS Pathog
December 2024
Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México.
Int J Mol Sci
November 2024
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon 73170, Nakhon Pathom, Thailand.
Cry toxins from are effective biopesticides that kill lepidopteran pests, replacing chemical pesticides that indiscriminately attack both target and non-target organisms. However, resistance in susceptible pests is an emerging problem. also produces vegetative insecticidal protein (Vip3A), which can kill insect targets in the same group as Cry toxins but using different host receptors, making the combined application of Cry and Vip3A an exciting possibility.
View Article and Find Full Text PDFPest Manag Sci
January 2025
Institute of Insect Sciences, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou, China.
Background: Vegetative insecticidal proteins (Vip3) from Bacillus thuringiensis (Bt) have been utilized for control of lepidopteran insect pests. The majority of known Vip3 proteins possess exceptional high toxicity against Noctuid insects such as the fall armyworm (FAW, Spodoptera frugiperda), beet armyworm (BAW, Spodoptera exigua) and cotton bollworm (CBW, Helicoverpa armigera), but generally have relatively low or even no activity against some very important pest insects, such as Asian corn borer (ACB, Ostrinia furnacalis), European corn borer (ECB, Ostrinia nubilalis), rice stem borer (RSB, Chilo suppressalis) and oriental armyworm (OAW, Mythimna separata).
Results: Here, we report mutant Vip3Af with a single amino acid mutation, Vip3Af-T686R, which gains significantly higher insecticidal activity against ACB, OAW and BAW, while retaining high activity against FAW, CBW and RSB.
Gene
January 2025
ICAR-National Institute for Plant Biotechnology, PUSA Campus, New Delhi 110012, India. Electronic address:
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