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

BACKGROUND: Pathogenic bacteria easily develop resistance to c onventional 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 (CAMP...

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Autores principales: Notomista, Eugenio, Falanga, Annarita, Fusco, Salvatore, Pirone, Luciano, Zanfardino, Anna, Galdiero, Stefania, Varcamonti, Mario, Pedone, Emilia, Contursi, Patrizia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4559164/
https://www.ncbi.nlm.nih.gov/pubmed/26338197
http://dx.doi.org/10.1186/s12934-015-0302-9
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author Notomista, Eugenio
Falanga, Annarita
Fusco, Salvatore
Pirone, Luciano
Zanfardino, Anna
Galdiero, Stefania
Varcamonti, Mario
Pedone, Emilia
Contursi, Patrizia
author_facet Notomista, Eugenio
Falanga, Annarita
Fusco, Salvatore
Pirone, Luciano
Zanfardino, Anna
Galdiero, Stefania
Varcamonti, Mario
Pedone, Emilia
Contursi, Patrizia
author_sort Notomista, Eugenio
collection PubMed
description BACKGROUND: Pathogenic bacteria easily develop resistance to c onventional 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. RESULTS: A 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. CONCLUSIONS: VLL-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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-015-0302-9) contains supplementary material, which is available to authorized users.
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spelling pubmed-45591642015-09-04 The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules Notomista, Eugenio Falanga, Annarita Fusco, Salvatore Pirone, Luciano Zanfardino, Anna Galdiero, Stefania Varcamonti, Mario Pedone, Emilia Contursi, Patrizia Microb Cell Fact Research BACKGROUND: Pathogenic bacteria easily develop resistance to c onventional 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. RESULTS: A 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. CONCLUSIONS: VLL-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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-015-0302-9) contains supplementary material, which is available to authorized users. BioMed Central 2015-09-04 /pmc/articles/PMC4559164/ /pubmed/26338197 http://dx.doi.org/10.1186/s12934-015-0302-9 Text en © Notomista et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Notomista, Eugenio
Falanga, Annarita
Fusco, Salvatore
Pirone, Luciano
Zanfardino, Anna
Galdiero, Stefania
Varcamonti, Mario
Pedone, Emilia
Contursi, Patrizia
The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title_full The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title_fullStr The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title_full_unstemmed The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title_short The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
title_sort identification of a novel sulfolobus islandicus camp-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4559164/
https://www.ncbi.nlm.nih.gov/pubmed/26338197
http://dx.doi.org/10.1186/s12934-015-0302-9
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