当前位置: X-MOL 学术Bioprocess Biosyst. Eng. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Heterologous expression of the novel α-helical hybrid peptide PR-FO in Bacillus subtilis.
Bioprocess and Biosystems Engineering ( IF 3.8 ) Pub Date : 2020-04-29 , DOI: 10.1007/s00449-020-02353-1
Licong Zhang 1 , Dandan Wei 1 , Na Zhan 1 , Taotao Sun 1 , Bingdong Shan 1 , Anshan Shan 1
Affiliation  

PR-FO is a novel α-helical hybrid antimicrobial peptide (AMP) with strong antimicrobial activities and high stability, and the potential to develop into a new generation of antimicrobial agents. In this study, the encoded gene sequence of SMT3-PR-FO was designed and transformed into B. subtilis WB800N. Fusion proteins with concentrations of 16 mg L-1 (SPamyQ) and 23 mg L-1 (SPsacB) were obtained after purification by a Ni-NTA resin column. A total of 3 mg (SPamyQ) and 4 mg (SPsacB) of PR-FO with a purity of 90% was obtained from 1 L fermentation cultures. Recombinant PR-FO exhibited high inhibition activities against both gram-negative bacteria and gram-positive bacteria, and low haemolytic activity against human red blood cells. These results indicated that the rSMT3-PR-FO could be expressed under the guidance of SPamyQ and SPsacB, and the maltose-induced expression strategy might be a safe and efficient method for the soluble peptides production in B. subtilis.

中文翻译:

新型α-螺旋杂合肽PR-FO在枯草芽孢杆菌中的异源表达。

PR-FO是一种新型的α-螺旋杂合抗菌肽(AMP),具有强大的抗菌活性和很高的稳定性,并有可能发展为新一代抗菌剂。在这项研究中,设计了SMT3-PR-FO的编码基因序列,并将其转化到枯草芽孢杆菌WB800N中。通过Ni-NTA树脂柱纯化后,获得浓度分别为16 mg L-1(SPamyQ)和23 mg L-1(SPsacB)的融合蛋白。从1 L发酵培养物中获得了总计3 mg(SPamyQ)和4 mg(SPsacB)的PR-FO,纯度为90%。重组PR-FO对革兰氏阴性菌和革兰氏阳性菌均表现出高抑制活性,而对人红细胞的溶血活性低。这些结果表明,rSMT3-PR-FO可以在SPamyQ和SPsacB的指导下表达,
更新日期:2020-04-29
down
wechat
bug