Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.

Multidrug resistance, which is acquired by both Gram-positive and Gram-negative bacteria, causes infections that are associated with significant morbidity and mortality in many clinical settings around the world. Because of the rapidly increasing incidence of pathogens that have become resistant to...

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Autores principales: Sylvain Godreuil, Nadia Leban, André Padilla, Rodolphe Hamel, Natthanej Luplertlop, Aurélie Chauffour, Marion Vittecoq, François Hoh, Frédéric Thomas, Wladimir Sougakoff, Corinne Lionne, Hans Yssel, Dorothée Missé
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Publicado: Public Library of Science (PLoS) 2014
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spelling oai:doaj.org-article:7723da698a064d01a3e61df7fd398c822021-11-25T06:03:04ZAedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.1932-620310.1371/journal.pone.0105441https://doaj.org/article/7723da698a064d01a3e61df7fd398c822014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25162372/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Multidrug resistance, which is acquired by both Gram-positive and Gram-negative bacteria, causes infections that are associated with significant morbidity and mortality in many clinical settings around the world. Because of the rapidly increasing incidence of pathogens that have become resistant to all or nearly all available antibiotics, there is a need for a new generation of antimicrobials with a broad therapeutic range for specific applications against infections. Aedesin is a cecropin-like anti-microbial peptide that was recently isolated from dengue virus-infected salivary glands of the Aedes aegypti mosquito. In the present study, we have refined the analysis of its structural characteristics and have determined its antimicrobial effects against a large panel of multidrug resistant bacterial strains, directly isolated from infected patients. Based the results from nuclear magnetic resonance spectroscopy analysis, Aedesin has a helix-bend-helix structure typical for a member of the family of α-helix anti-microbial peptides. Aedesin efficiently killed Gram-negative bacterial strains that display the most worrisome resistance mechanisms encountered in the clinic, including resistance to carbapenems, aminoglycosides, cephalosporins, 4th generation fluoroquinolones, folate inhibitors and monobactams. In contrast, Gram-positive strains were insensitive to the lytic effects of the peptide. The anti-bacterial activity of Aedesin was found to be salt-resistant, indicating that it is active under physiological conditions encountered in body fluids characterized by ionic salt concentrations. In conclusion, because of its strong lytic activity against multidrug resistant Gram-negative bacterial strains displaying all types of clinically relevant resistance mechanisms known today, Aedesin might be an interesting candidate for the development of alternative treatment for infections caused by these types of bacteria.Sylvain GodreuilNadia LebanAndré PadillaRodolphe HamelNatthanej LuplertlopAurélie ChauffourMarion VittecoqFrançois HohFrédéric ThomasWladimir SougakoffCorinne LionneHans YsselDorothée MisséPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 8, p e105441 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Sylvain Godreuil
Nadia Leban
André Padilla
Rodolphe Hamel
Natthanej Luplertlop
Aurélie Chauffour
Marion Vittecoq
François Hoh
Frédéric Thomas
Wladimir Sougakoff
Corinne Lionne
Hans Yssel
Dorothée Missé
Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
description Multidrug resistance, which is acquired by both Gram-positive and Gram-negative bacteria, causes infections that are associated with significant morbidity and mortality in many clinical settings around the world. Because of the rapidly increasing incidence of pathogens that have become resistant to all or nearly all available antibiotics, there is a need for a new generation of antimicrobials with a broad therapeutic range for specific applications against infections. Aedesin is a cecropin-like anti-microbial peptide that was recently isolated from dengue virus-infected salivary glands of the Aedes aegypti mosquito. In the present study, we have refined the analysis of its structural characteristics and have determined its antimicrobial effects against a large panel of multidrug resistant bacterial strains, directly isolated from infected patients. Based the results from nuclear magnetic resonance spectroscopy analysis, Aedesin has a helix-bend-helix structure typical for a member of the family of α-helix anti-microbial peptides. Aedesin efficiently killed Gram-negative bacterial strains that display the most worrisome resistance mechanisms encountered in the clinic, including resistance to carbapenems, aminoglycosides, cephalosporins, 4th generation fluoroquinolones, folate inhibitors and monobactams. In contrast, Gram-positive strains were insensitive to the lytic effects of the peptide. The anti-bacterial activity of Aedesin was found to be salt-resistant, indicating that it is active under physiological conditions encountered in body fluids characterized by ionic salt concentrations. In conclusion, because of its strong lytic activity against multidrug resistant Gram-negative bacterial strains displaying all types of clinically relevant resistance mechanisms known today, Aedesin might be an interesting candidate for the development of alternative treatment for infections caused by these types of bacteria.
format article
author Sylvain Godreuil
Nadia Leban
André Padilla
Rodolphe Hamel
Natthanej Luplertlop
Aurélie Chauffour
Marion Vittecoq
François Hoh
Frédéric Thomas
Wladimir Sougakoff
Corinne Lionne
Hans Yssel
Dorothée Missé
author_facet Sylvain Godreuil
Nadia Leban
André Padilla
Rodolphe Hamel
Natthanej Luplertlop
Aurélie Chauffour
Marion Vittecoq
François Hoh
Frédéric Thomas
Wladimir Sougakoff
Corinne Lionne
Hans Yssel
Dorothée Missé
author_sort Sylvain Godreuil
title Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
title_short Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
title_full Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
title_fullStr Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
title_full_unstemmed Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
title_sort aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/7723da698a064d01a3e61df7fd398c82
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