Wang Shichun, Wang Yawen, Cheng Congyang, Zhang Hongxing, Jin Junhua, Pang Xiaona, Song Xiaodong, Xie Yuanhong
Laboratory of Food Quality and Safety, Beijing Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticide Residue, College of Food Science and Engineering, Beijing University of Agriculture, Beijing, China.
Key Laboratory of Dairy Quality Digital Intelligence Monitoring Technology, State Administration for Market Regulation, Inner Mongolia Mengniu Dairy (Group) Co., Ltd., Hohhot, China.
Probiotics Antimicrob Proteins. 2025 Mar 19. doi: 10.1007/s12602-025-10518-1.
Plantaricin BM-1 exhibits antibacterial activity against Escherichia coli; however, the underlying mechanism remains unclear. This study aimed to investigate the function of PotF, a putrescine-binding protein, in regulating the antibacterial activity of plantaricin BM-1 against E. coli K12. The antibacterial activity of plantaricin BM-1 against E. coli K12 and JW0838 cells was assessed using growth curves. The differences in biofilm formation between the two E. coli strains were evaluated by crystal violet staining and confocal laser scanning microscopy. The effects of plantaricin BM-1 on E. coli morphology and cell membrane integrity were investigated by electron microscopy and lactate dehydrogenase release assays. Proteomics was used to screen for differentially expressed proteins (DEPs) that are potentially involved in regulating the antibacterial mechanism. The null mutation of potF enhanced the antibacterial effects of plantaricin BM-1 on E. coli, and caused a significant decrease (p < 0.05) in the biofilms of E. coli JW0838. The plantaricin disrupted the cell membrane of E. coli JW0838. Proteomic analysis revealed that potF mutation significantly affected several DEPs involved in biofilm formation. Plantaricin BM-1 exhibited significantly enhanced antibacterial activity against biofilm-associated gene mutants compared to wild-type E. coli K12. These findings enhance our understanding of the bacteriostasis of class IIa bacteriocins against Gram-negative microorganisms.
植物乳杆菌素BM-1对大肠杆菌具有抗菌活性；然而，其潜在机制仍不清楚。本研究旨在探讨腐胺结合蛋白PotF在调节植物乳杆菌素BM-1对大肠杆菌K12抗菌活性中的作用。通过生长曲线评估植物乳杆菌素BM-1对大肠杆菌K12和JW0838细胞的抗菌活性。通过结晶紫染色和共聚焦激光扫描显微镜评估两种大肠杆菌菌株在生物膜形成方面的差异。通过电子显微镜和乳酸脱氢酶释放试验研究植物乳杆菌素BM-1对大肠杆菌形态和细胞膜完整性的影响。蛋白质组学用于筛选可能参与调节抗菌机制的差异表达蛋白（DEP）。potF的无效突变增强了植物乳杆菌素BM-1对大肠杆菌的抗菌作用，并导致大肠杆菌JW0838生物膜显著减少（p < 0.05）。植物乳杆菌素破坏了大肠杆菌JW0838的细胞膜。蛋白质组学分析表明，potF突变显著影响了几个参与生物膜形成的DEP。与野生型大肠杆菌K12相比，植物乳杆菌素BM-1对生物膜相关基因突变体表现出显著增强的抗菌活性。这些发现增进了我们对IIa类细菌素对革兰氏阴性微生物抑菌作用的理解。
