Publication: Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
1
Accepted Date
2014-07-18
Issued Date
2014-08-27
Copyright Date
2014
Resource Type
Language
eng
ISSN
1932-6203 (e)
Rights
Mahidol University
Rights Holder(s)
PLoS One
Bibliographic Citation
Godreuil S, Leban N, Padilla A, Hamel R, Luplertlop N, Chauffour A. et al. Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains. PLoS One. 2014 Aug 27;9(8):e105441.
Suggested Citation
Godreuil, Sylvain, Leban, Nadia, Padilla, Andre´, Hamel, Rodolphe, Natthanej Luplertlop, นัฏฐเนศวร์ ลับเลิศลบ, Chauffour, Aure´ lie, Vittecoq, Marion, Hoh, Franc¸ois, Thomas, Fre´de´ ric, Sougakoff, Wladimir, Lionne, Corinne, Yssel, Hans, Misse, Dorothe´e Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.. Godreuil S, Leban N, Padilla A, Hamel R, Luplertlop N, Chauffour A. et al. Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains. PLoS One. 2014 Aug 27;9(8):e105441.. doi:10.1371/journal.pone.0105441. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/842
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Title
Aedesin: structure and antimicrobial activity against multidrug resistant bacterial strains.
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Abstract
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.