Related Experiment Video
Updated: May 9, 2026
Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae,
Lijie Xia1, Fuchun Zhang, Zhongyuan Liu
1Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, Xinjiang 830046, P.R. China ;
Abstract:
Insect antimicrobial peptides (AMPs) have a broad antimicrobial spectrum. To aid the characterization of the gene function and further applications, we cloned the gene of cecropinXJ into the prokaryotic expression vector pET32a and expressed cecropinXJ in Escherichia coli BL2l (DE3). Following induction by isopropyl-β-D-thiogalactoside (IPTG), a 25 kDa fusion peptide of cecropinXJ with a tagged thioredoxin (Trx) protein was highly expressed in E. coli. The yield was 10 mg/l culture medium following purification on nickel-nitrilotriacetic acid (Ni-NTA) metal affinity chromatography matrices. The purified recombinant antibacterial peptide, cecropinXJ, retained a high stability against Staphylococcus aureus over a temperature range from 4 to 100°C and a pH range from pH 2.0 to 12.0. The minimum inhibitory concentration (MIC) of the fusion protein against S. aureus was 0.4 μM. The recombinant cecropinXJ is also cytotoxic to several types of human cancer cells.
