@article{fdi:010062822,
  title = {{A}edesin : structure and antimicrobial activity against multidrug resistant bacterial strains},
  author = {{G}odreuil, {S}. and {L}eban, {N}. and {P}adilla, {A}. and {H}amel, {R}odolphe and {L}uplertlop, {N}. and {C}hauffour, {A}. and {V}ittecoq, {M}. and {H}oh, {F}. and {T}homas, {F}. and {S}ougakoff, {V}. and {L}ionne, {C}. and {Y}ssel, {H}. and {M}iss{\'e}, {D}oroth{\'e}e},
  editor = {},
  language = {{ENG}},
  abstract = {{M}ultidrug resistance, which is acquired by both {G}ram-positive and {G}ram-negative bacteria, causes infections that are associated with significant morbidity and mortality in many clinical settings around the world. {B}ecause 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. {A}edesin is a cecropin-like anti-microbial peptide that was recently isolated from dengue virus-infected salivary glands of the {A}edes aegypti mosquito. {I}n 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. {B}ased the results from nuclear magnetic resonance spectroscopy analysis, {A}edesin has a helix-bend-helix structure typical for a member of the family of α-helix anti-microbial peptides. {A}edesin efficiently killed {G}ram-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. {I}n contrast, {G}ram-positive strains were insensitive to the lytic effects of the peptide. {T}he anti-bacterial activity of {A}edesin was found to be salt-resistant, indicating that it is active under physiological conditions encountered in body fluids characterized by ionic salt concentrations. {I}n conclusion, because of its strong lytic activity against multidrug resistant {G}ram-negative bacterial strains displaying all types of clinically relevant resistance mechanisms known today, {A}edesin might be an interesting candidate for the development of alternative treatment for infections caused by these types of bacteria.},
  keywords = {{INFECTION} ; {BACTERIE} ; {MEDICAMENT} ; {ANTIBIOTIQUE} ; {SENSIBILITE} {RESISTANCE} ; {ANALYSE} {STRUCTURALE} ; {SPECTROSCOPIE} ; {MICROSCOPIE} {ELECTRONIQUE} ; {ETUDE} {EXPERIMENTALE} ; {PEPTIDE} ; {MONDE}},
  booktitle = {},
  journal = {{PL}o{S} {O}ne},
  volume = {9},
  numero = {8},
  pages = {e105441 [9  en ligne]},
  ISSN = {1932-6203},
  year = {2014},
  DOI = {10.1371/journal.pone.0105441},
  URL = {https://www.documentation.ird.fr/hor/fdi:010062822},
}