Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner
Bacillus thuringiensis Berliner based biopesticides have been successfully used world over for the control of agricultural pests and vectors of human diseases. Currently there are more than 200 B. thuringiensis strains with differing insecticidal activities are available as biocontrol agents and for...
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| Format: | Article |
| Language: | English |
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Malaysian Society for Microbiology
2007-01-01
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| Series: | Malaysian Journal of Microbiology |
| Subjects: | |
| Online Access: | http://web.usm.my/mjm/issues/vol3no2/research1.pdf |
| _version_ | 1811310804813742080 |
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| author | Xavier, R. Reena Josephine, C. M. Sreeramanan, S. |
| author_facet | Xavier, R. Reena Josephine, C. M. Sreeramanan, S. |
| author_sort | Xavier, R. |
| collection | DOAJ |
| description | Bacillus thuringiensis Berliner based biopesticides have been successfully used world over for the control of agricultural pests and vectors of human diseases. Currently there are more than 200 B. thuringiensis strains with differing insecticidal activities are available as biocontrol agents and for developing transgenic plants. However, two major disadvantages are the development of insect resistance and high target specificity (narrow host range). Globally there is a continuous search for new B. thuringiensis strains with novel insecticidal activities. The present study aims to study the environmental distribution of B. thuringiensis and their toxic potential against insect pests. Soil and grain samples were collected from different environments and were processed by a modified acetate selection method. Initially B. thuringiensis isolates were screened on the basis of colony morphology and phase contrast microscopy for the presence of parasporal crystal inclusions. The population dynamics showed that B. thuringiensis is abundant in sericulture environment compared to other niches. Relative abundance of B. thuringiensis strains in sericulture environment shows the persistent association of B. thuringiensis with Bombyx mori (silk worm) as insect pathogen. The protein profiles of the selected strains were studied by SDS-PAGE. The protein profiles of majority of B. thuringiensis isolates from grain storage facilities predominantly showing the 130 kDa and 68 kDa proteins, which is characteristics of lepidopteran active B. thuringiensis. However, one isolate BTRX-4 has 80-85 kDa protein, which is novel in that, this strain also exhibits antilepidopteran activity, which is normally presented by B. thuringiensis strains having 130 kDa and 68 kDa proteins. The protein profile of B. thuringiensis isolates from sericulture environment shows two different protein profiles. B. thuringiensis isolates BTRX-16 to BTRX-22 predominantly show 130 kDa protein, however, the B. thuringiensis isolates BTRX-23 to BTRX-30 have two distinct protein profiles corresponding to 130 kDa and 68 kDa. These results show that there may be more than one B. thuringiensis strain that can infect Bombyx mori. The preliminary bioassay against second instar larvae of Heliothis armigera showed varying mortality rate. In conclusion, despite the ubiquitous presence of B. thuringiensis strains in different environments, specifically the sericulture environment supports B. thuringiensis in a significant manner compared to other environments. Further the ICPs produced by different strains of B. thuringiensis are unique in terms of the protein profile and hence may also differ in their insecticidal activities. |
| first_indexed | 2024-04-13T10:05:36Z |
| format | Article |
| id | doaj.art-921b16f0af694a06bcd432f0179306fa |
| institution | Directory Open Access Journal |
| issn | 1823-8262 2231-7538 |
| language | English |
| last_indexed | 2024-04-13T10:05:36Z |
| publishDate | 2007-01-01 |
| publisher | Malaysian Society for Microbiology |
| record_format | Article |
| series | Malaysian Journal of Microbiology |
| spelling | doaj.art-921b16f0af694a06bcd432f0179306fa2022-12-22T02:51:06ZengMalaysian Society for MicrobiologyMalaysian Journal of Microbiology1823-82622231-75382007-01-013216Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis BerlinerXavier, R.Reena Josephine, C. M.Sreeramanan, S.Bacillus thuringiensis Berliner based biopesticides have been successfully used world over for the control of agricultural pests and vectors of human diseases. Currently there are more than 200 B. thuringiensis strains with differing insecticidal activities are available as biocontrol agents and for developing transgenic plants. However, two major disadvantages are the development of insect resistance and high target specificity (narrow host range). Globally there is a continuous search for new B. thuringiensis strains with novel insecticidal activities. The present study aims to study the environmental distribution of B. thuringiensis and their toxic potential against insect pests. Soil and grain samples were collected from different environments and were processed by a modified acetate selection method. Initially B. thuringiensis isolates were screened on the basis of colony morphology and phase contrast microscopy for the presence of parasporal crystal inclusions. The population dynamics showed that B. thuringiensis is abundant in sericulture environment compared to other niches. Relative abundance of B. thuringiensis strains in sericulture environment shows the persistent association of B. thuringiensis with Bombyx mori (silk worm) as insect pathogen. The protein profiles of the selected strains were studied by SDS-PAGE. The protein profiles of majority of B. thuringiensis isolates from grain storage facilities predominantly showing the 130 kDa and 68 kDa proteins, which is characteristics of lepidopteran active B. thuringiensis. However, one isolate BTRX-4 has 80-85 kDa protein, which is novel in that, this strain also exhibits antilepidopteran activity, which is normally presented by B. thuringiensis strains having 130 kDa and 68 kDa proteins. The protein profile of B. thuringiensis isolates from sericulture environment shows two different protein profiles. B. thuringiensis isolates BTRX-16 to BTRX-22 predominantly show 130 kDa protein, however, the B. thuringiensis isolates BTRX-23 to BTRX-30 have two distinct protein profiles corresponding to 130 kDa and 68 kDa. These results show that there may be more than one B. thuringiensis strain that can infect Bombyx mori. The preliminary bioassay against second instar larvae of Heliothis armigera showed varying mortality rate. In conclusion, despite the ubiquitous presence of B. thuringiensis strains in different environments, specifically the sericulture environment supports B. thuringiensis in a significant manner compared to other environments. Further the ICPs produced by different strains of B. thuringiensis are unique in terms of the protein profile and hence may also differ in their insecticidal activities.http://web.usm.my/mjm/issues/vol3no2/research1.pdfBacillus thuringiensisBiopesticidesInsecticidal crystal proteins |
| spellingShingle | Xavier, R. Reena Josephine, C. M. Sreeramanan, S. Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner Malaysian Journal of Microbiology Bacillus thuringiensis Biopesticides Insecticidal crystal proteins |
| title | Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner |
| title_full | Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner |
| title_fullStr | Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner |
| title_full_unstemmed | Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner |
| title_short | Environmental Distribution and Diversity of Insecticidal Proteins of Bacillus thuringiensis Berliner |
| title_sort | environmental distribution and diversity of insecticidal proteins of bacillus thuringiensis berliner |
| topic | Bacillus thuringiensis Biopesticides Insecticidal crystal proteins |
| url | http://web.usm.my/mjm/issues/vol3no2/research1.pdf |
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