Responses of pseudomonas aeruginosa and other eskape pathogens to antimicrobial peptide dendrimers

Diplôme Thèse Responses of pseudomonas aeruginosa and other eskape pathogens to antimicrobial peptide dendrimers eng 2021-04-21 author Ben Jeddou Fatma 871739 director Van Delden Christian 24088 director Kohler Thilo 0000-0003-4889-9492 23327 10.13097/archive-ouverte/unige:152699 urn:nbn:ch:unige-1526999 Sc. Vie - Bioméd. 102 Antimicrobial peptides (AMPs) are one of the most diverse classes of antibiotics. A prominent example is polymyxin E (colistin), used as last-resort antibiotic against multidrug resistant (MDR) Gram-negative bacteria. However, the emergence of resistance and toxicity of colistin restrict its use. Dendrimer antimicrobial peptides are currently explored as an alternative to colistin, since they show low hemolytic activity and are active against MDR isolates of Pseudomonas aeruginosa and Acinetobacter baumannii. To unravel the mode of action and potential resistance mechanisms of dendrimer AMPs, spontaneous resistant mutants were selected on polymyxin B and the prototypical dendrimer G3KL in ESKAPE pathogens. We propose a model for decreased susceptibility to G3KL in P. aeruginosa that includes two modifications of the lipopolysaccharide resulting in decreased negative charges at the bacterial surface. We hypothesized that mechanisms leading to decreased susceptibility to G3KL may be different from those conferring polymyxin resistance and seem to be species-specific in Gram-negative bacteria. Pseudomonas aeruginosa AMP-dendrimers Two-component systems Antimicrobial peptides Dendrimers Two-component regulatory systems ESKAPE pathogens Dewey 616 56 Département de médecine 221 false c5614de3-4b40-4a10-b585-555ffc394c12 Thesis Public PhD_Thesis_Fatma_Ben_Jeddou.pdf 20688546 application/pdf openAccess Faculté de médecine / Section de médecine clinique / Département de médecine

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Responses of pseudomonas aeruginosa and other eskape pathogens to antimicrobial peptide dendrimers				2021	573	650

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Ben Jeddou, Fatma