iTRAQ-coupled 2-D LC–MS/MS analysis of cytoplasmic protein profile in Escherichia coli incubated with apidaecin IB

• Published in: Journal of proteomics Vol. 75; no. 2; pp. 511 - 516
• Main Authors: Zhou, Yusi, Chen, Wei Ning
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier B.V 21.12.2011; Elsevier
• Subjects: Antibiotics; Antimicrobial Cationic Peptides - pharmacology; Antimicrobial peptides; Apidaecins; Biological and medical sciences; cells; Chaperones; Chaperonin 10 - biosynthesis; Chaperonin 60 - biosynthesis; Chaperonins; Chromatography, Liquid; Cofactors; Cytoplasm; Cytoplasm - metabolism; Diverse techniques; Drug development; Escherichia coli; Escherichia coli - drug effects; Escherichia coli - metabolism; Escherichia coli Proteins - biosynthesis; Fundamental and applied biological sciences. Psychology; Gene Expression Profiling; GroEL; GroES; Growth conditions; Heat-Shock Proteins - biosynthesis; HSP40 Heat-Shock Proteins - biosynthesis; HSP70 Heat-Shock Proteins - biosynthesis; humans; insects; iTRAQ; LC–MS/MS; mechanism of action; Molecular and cellular biology; proteins; proteomics; Tandem Mass Spectrometry; iTRAQ; GroES; GroEL; Apidaecins; LC–MS/MS; LC-MS/MS; Analysis; Escherichia coli; Bacteria; Profile; Protein; Enterobacteriaceae
• ISSN: 1874-3919; 1876-7737
• DOI: 10.1016/j.jprot.2011.08.015

Apidaecins refer to a series of proline-rich, 18- to 20-residue antimicrobial peptides produced by insects. Accumulating evidence that proline-rich antimicrobial peptides are not-toxic to human and animal cells makes them potential candidates for the development of novel antibiotic drugs. However, the mechanism of action was not fully understood. In this study, antibacterial mechanism of apidaecins was investigated. iTRAQ-coupled 2-D LC–MS/MS technique was utilized to identify altered cytoplasmic proteins of Escherichia coli incubated with one isoform of apidaecins — apidaecin IB. The production of the chaperonin GroEL and its cofactor GroES, which together form the only essential chaperone system in E. coli cytoplasm under all growth conditions, was decreased in cells incubated with apidaecin IB. The decreasing of the GroEL–GroES chaperone team was further found to be involved in a new antibacterial mechanism of apidaecins. Our findings therefore provide important new insights into the antibacterial mechanism of apidaecins and perhaps, by extension, for other proline-rich antimicrobial peptides. [Display omitted] ►Antimicrobial peptides apidaecins. ►Cytoplasmic proteome profile of bacterial cells in response to apidaecins. ►Chaperone proteins GroEL–GroES and apidaecins. ►New antibacterial mechanisms by apidaecins.