The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules

Microbial Cell Factories

Research

Anna Zanfardino¹  Salvatore Fusco¹  Mario Varcamonti¹  Eugenio Notomista¹  Patrizia Contursi¹  Emilia Pedone²  Annarita Falanga²  Luciano Pirone³  Stefania Galdiero⁴ 

[1] Dipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy;Istituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy;Istituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy;C.I.R.C.M.S.B. (Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici), via Celso Ulpiani, 27, 70125, Bari, Italy;Istituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy;Department of Pharmacy and CiRPEB, University of Naples Federico II, 80100, Naples, Italy;

关键词: Sodium Dodecyl Sulphate;    Circular Dichroism;    Circular Dichroism Spectrum;    Bacterial Membrane;    Large Unilamellar Vesicle;   

DOI  :  10.1186/s12934-015-0302-9

 received in 2015-06-17, accepted in 2015-07-22,  发布年份 2015

来源: Springer

【 摘 要 】

BackgroundPathogenic bacteria easily develop resistance to conventional antibiotics so that even relatively new molecules are quickly losing efficacy. This strongly encourages the quest of new antimicrobials especially for the treatment of chronic infections. Cationic antimicrobial peptides (CAMPs) are small positively charged peptides with an amphipathic structure, active against Gram-positive and Gram-negative bacteria, fungi, as well as protozoa.ResultsA novel (CAMP)-like peptide (VLL-28) was identified in the primary structure of a transcription factor, Stf76, encoded by pSSVx, a hybrid plasmid–virus from the archaeon Sulfolobus islandicus. VLL-28 displays chemical, physical and functional properties typical of CAMPs. Indeed, it has a broad-spectrum antibacterial activity and acquires a defined structure in the presence of membrane mimetics. Furthermore, it exhibits selective leakage and fusogenic capability on vesicles with a lipid composition similar to that of bacterial membranes. VLL-28 localizes not only on the cell membrane but also in the cytoplasm of Escherichia coli and retains the ability to bind nucleic acids. These findings suggest that this CAMP-like peptide could exert its antimicrobial activity both on membrane and intra cellular targets.ConclusionsVLL-28 is the first CAMP-like peptide identified in the archaeal kingdom, thus pointing to archaeal microorganisms as cell factories to produce antimicrobial molecules of biotechnological interest. Furthermore, results from this work show that DNA/RNA-binding proteins could be used as sources of CAMPs.

【 授权许可】

CC BY   
© Notomista et al. 2015