scholarly journals Development of a Bacillus subtilis expression system using the improved Pglv promoter

2010 ◽  
Vol 9 (1) ◽  
pp. 55 ◽  
Author(s):  
Yang M Ming ◽  
Zhang W Wei ◽  
Chen Y Lin ◽  
Gong Y Sheng
2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Xi Kong ◽  
Mei Yang ◽  
Hafiz Muhammad Khalid Abbas ◽  
Jia Wu ◽  
Mengge Li ◽  
...  

2020 ◽  
Vol 21 (22) ◽  
pp. 8722
Author(s):  
Jiale Li ◽  
Samiul Islam ◽  
Pengfei Guo ◽  
Xiaoqing Hu ◽  
Wubei Dong

Antimicrobial genes are distributed in all forms of life and provide a primary defensive shield due to their unique broad-spectrum resistance activities. To better isolate these genes, we used the Bacillus subtilis expression system as the host cells to build Oryza rufipogon Griff cDNA libraries and screen potential candidate genes from the library at higher flux using built-in indicator bacteria. We observed that the antimicrobial peptides OrR214 and OrR935 have strong antimicrobial activity against a variety of Gram-positive and Gram-negative bacteria, as well as several fungal pathogens. Owing to their high thermal and enzymatic stabilities, these two peptides can also be used as field biocontrol agents. Furthermore, we also found that the peptide OrR214 (MIC 7.7–10.7 μM) can strongly inhibit bacterial growth compared to polymyxin B (MIC 5–25 μM) and OrR935 (MIC 33–44 μM). The cell flow analysis, reactive oxygen burst, and electron microscopy (scanning and transmission electron microscopy) observations showed that the cell membranes were targeted by peptides OrR214 and OrR935, which revealed the mode of action of bacteriostasis. Moreover, the hemolytic activity, toxicity, and salt sensitivity experiments demonstrated that these two peptides might have the potential to be used for clinical applications. Overall, OrR214 and OrR935 antimicrobial peptides have a high-throughput bacteriostatic activity that acts as a new form of antimicrobial agent and can be used as a raw material in the field of drug development.


2013 ◽  
Vol 64 (2) ◽  
pp. 879-882 ◽  
Author(s):  
Reza Panahi ◽  
Ebrahim Vasheghani-Farahani ◽  
Seyed Abbas Shojaosadati ◽  
Bijan Bambai

Microbiology ◽  
2000 ◽  
Vol 146 (10) ◽  
pp. 2583-2594 ◽  
Author(s):  
Christina L. Jensen ◽  
Keith Stephenson ◽  
Steen T. Jørgensen ◽  
Colin Harwood

2021 ◽  
Vol 28 ◽  
Author(s):  
Chutchanun Trakulnaleamsai ◽  
Boonhiang Promdonkoy ◽  
Sumarin Soonsanga

Background: Mtx2 is a mosquitocidal toxin produced during the vegetative growth of Lysinibacillus sphaericus. The protein shows synergism with other toxins against mosquito larvae; hence it could be used in mosquito control formulations. The protein expression system is needed for Mtx2 development as a biocontrol agent. Objective: The objective of the study was to set up a Bacillus subtilis system to produce Mtx2 as a secreted protein since the protein contains a putative signal peptide. Methods: Initially, four different promoters (P43, Pspac, PxylA, and PyxiE) were compared for their strength using GFP as a reporter in B. subtilis. Subsequently, six different signal peptides (SacB, Epr, AmyE, AprE, LipA, and Vip3A)were tested in conjunction with the selected promoter and mtx2 to evaluate levels of Mtx2 secreted by B. subtilis WB800, an extracellular protease-deficient strain. Results: The promoter PyxiE showed the highest GFP intensity and was selected for further study. Mtx2 was successfully produced as a secreted protein from signal peptides LipA and AmyE, and exhibited larvicidal activity against Aedesaegypti. Conclusion: B. subtilis was successfully developed as a host for the production of secreted Mtx2 and the protein retained its larvicidal activity. Although the Mtx2 production level still needs improvement, the constructed plasmids could be used to produce other soluble proteins.


Sign in / Sign up

Export Citation Format

Share Document