title: iTRAQ-Based Quantitative Proteomic Analysis of the Antimicrobial Mechanism of Peptide F1 against Escherichia coli.
abstract: Antimicrobial peptides have received increasing attention in the agricultural and food industries due to their potential to control pathogens. However, to facilitate the development of novel peptide-based antimicrobial agents, details regarding the molecular mechanisms of these peptides need to be elucidated. The aim of this study was to investigate the antimicrobial mechanism of peptide F1, a bacteriocin found in Tibetan kefir, against Escherichia coli at protein levels using iTRAQ-based quantitative proteomic analysis. In response to treatment with peptide F1, 31 of the 280 identified proteins in E. coli showed alterations in their expression, including 10 down-regulated proteins and 21 up-regulated proteins. These 31 proteins all possess different molecular functions and are involved in different molecular pathways, as is evident in referencing the Kyoto Encyclopedia of Genes and Genomes pathways. Specifically, pathways that were significantly altered in E. coli in response to peptide F1 treatment include the tricarboxylic acid cycle, oxidative phosphorylation, glycerophospholipid metabolism, and the cell cycle-caulobacter pathways, which was also associated with inhibition of the cell growth, induction of morphological changes, and cell death. The results provide novel insights into the molecular mechanisms of antimicrobial peptides.
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.|§Department of Food Science, University of Massachusetts, Amherst, Massachusetts 01003, United States.
authors.forename: Jianyin
authors.initials: J
authors.lastname: Miao
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Feilong
authors.initials: F
authors.lastname: Chen
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Shan
authors.initials: S
authors.lastname: Duan
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Xiangyang
authors.initials: X
authors.lastname: Gao
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Guo
authors.initials: G
authors.lastname: Liu
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Yunjiao
authors.initials: Y
authors.lastname: Chen
authors.affiliation: §Department of Food Science, University of Massachusetts, Amherst, Massachusetts 01003, United States.
authors.forename: William
authors.initials: W
authors.lastname: Dixon
authors.affiliation: §Department of Food Science, University of Massachusetts, Amherst, Massachusetts 01003, United States.
authors.forename: Hang
authors.initials: H
authors.lastname: Xiao
authors.affiliation: †College of Food Science, South China Agricultural University, Guangzhou 510642, People's Republic of China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Cao
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D004926:Escherichia coli / Q000737:chemistry* / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020869:Gene Expression Profiling; D040901:Proteomics
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D029968:Escherichia coli Proteins
keywords: Escherichia coli; antimicrobial mechanism; antimicrobial peptide F1; iTRAQ; proteomic analysis