Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions
<i>Bacillus subtilis</i> spore display has become a field of increasing interest in the past two decades. To improve the efficiency of <i>B. subtilis</i> spore display, its directed modification was performed based on the cellulosome architecture by introducing onto them dive...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/4/1186 |
| _version_ | 1797395585624440832 |
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| author | He Wang Xiaomin Jiang Yongchang Qian Lianghong Yin |
| author_facet | He Wang Xiaomin Jiang Yongchang Qian Lianghong Yin |
| author_sort | He Wang |
| collection | DOAJ |
| description | <i>Bacillus subtilis</i> spore display has become a field of increasing interest in the past two decades. To improve the efficiency of <i>B. subtilis</i> spore display, its directed modification was performed based on the cellulosome architecture by introducing onto them divergent cohesin (Coh) modules that can specifically bind to the target enzyme bearing the matching dockerins (Doc). In this study, five different pairs of cohesins and dockerins, selected from four cellulolytic microbes, were examined for their capabilities in displaying a tetrameric enzyme β-galactosidase from <i>Bacillus stearothermophilus</i> IAM11001 on the surface of <i>B. subtilis</i> WB600 spores. Immunofluorescence microscopy, western blotting, dot blotting, and enzyme assay was applied to confirm its surface expression. All the resultant five Coh–Doc based spore display can hydrolyze <i>o</i>-nitrophenyl-β-D-galactopyranoside. Further, the optimized Coh–Doc based spore display exhibited the highest display efficiency. Overall, the results of current study may open new perspectives on the use of Coh–Doc interaction, which will find application in improving the efficiency of <i>B. subtilis</i> spore display. |
| first_indexed | 2024-03-09T00:37:38Z |
| format | Article |
| id | doaj.art-93f4b4dda2634d57bb4ec2e60564dcd8 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T00:37:38Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-93f4b4dda2634d57bb4ec2e60564dcd82023-12-11T18:04:05ZengMDPI AGMolecules1420-30492021-02-01264118610.3390/molecules26041186Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin InteractionsHe Wang0Xiaomin Jiang1Yongchang Qian2Lianghong Yin3School of Grain Science and Technology, Jiangsu University of Science and Technology, Zhenjiang 212100, ChinaSchool of Agricultural and Food Sciences, Zhejiang Agriculture and Forestry University, Hangzhou 311300, ChinaSchool of Forestry and Biotechnology, Zhejiang Agriculture and Forestry University, Hangzhou 311300, ChinaSchool of Forestry and Biotechnology, Zhejiang Agriculture and Forestry University, Hangzhou 311300, China<i>Bacillus subtilis</i> spore display has become a field of increasing interest in the past two decades. To improve the efficiency of <i>B. subtilis</i> spore display, its directed modification was performed based on the cellulosome architecture by introducing onto them divergent cohesin (Coh) modules that can specifically bind to the target enzyme bearing the matching dockerins (Doc). In this study, five different pairs of cohesins and dockerins, selected from four cellulolytic microbes, were examined for their capabilities in displaying a tetrameric enzyme β-galactosidase from <i>Bacillus stearothermophilus</i> IAM11001 on the surface of <i>B. subtilis</i> WB600 spores. Immunofluorescence microscopy, western blotting, dot blotting, and enzyme assay was applied to confirm its surface expression. All the resultant five Coh–Doc based spore display can hydrolyze <i>o</i>-nitrophenyl-β-D-galactopyranoside. Further, the optimized Coh–Doc based spore display exhibited the highest display efficiency. Overall, the results of current study may open new perspectives on the use of Coh–Doc interaction, which will find application in improving the efficiency of <i>B. subtilis</i> spore display.https://www.mdpi.com/1420-3049/26/4/1186spore display<i>Bacillus subtilis</i>cohesin dockerin interactionβ-galactosidasedisplay efficiency |
| spellingShingle | He Wang Xiaomin Jiang Yongchang Qian Lianghong Yin Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions Molecules spore display <i>Bacillus subtilis</i> cohesin dockerin interaction β-galactosidase display efficiency |
| title | Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions |
| title_full | Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions |
| title_fullStr | Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions |
| title_full_unstemmed | Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions |
| title_short | Constructing an Efficient <i>Bacillus subtilis</i> Spore Display by Using Cohesin−Dockerin Interactions |
| title_sort | constructing an efficient i bacillus subtilis i spore display by using cohesin dockerin interactions |
| topic | spore display <i>Bacillus subtilis</i> cohesin dockerin interaction β-galactosidase display efficiency |
| url | https://www.mdpi.com/1420-3049/26/4/1186 |
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