Open Access
| Issue |
Med Sci (Paris)
Volume 42, Number 1, Janvier 2026
L’antibiorésistance au prisme des trois santés
|
|
|---|---|---|
| Page(s) | 57 - 64 | |
| Section | M/S Revues | |
| DOI | https://doi.org/10.1051/medsci/2025252 | |
| Published online | 23 January 2026 | |
- Murray CJL, Ikuta KS, Sharara F, et al. Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis. Lancet 2022 ; 399 : 629–55. [CrossRef] [PubMed] [Google Scholar]
- Barbier F, Wolff M. Multirésistance chez Pseudomonas aeruginosa: Vers l’impasse thérapeutique ? Med Sci (Paris) 2010 ; 26 : 960–8. [Google Scholar]
- Sati H, Carrara E, Savoldi A, et al. The WHO bacterial priority pathogens list 2024: a prioritisation study to guide research, development, and public health strategies against antimicrobial resistance. Lancet Infect Dis 2025 ; S1473309925001185. [Google Scholar]
- Bertrand X, Slekovec C, Cholley P, et al. Épidémiologie des infections à Pseudomonas aeruginosa. Rev Francoph Lab 2011 ; 2011 : 35–40. [Google Scholar]
- Lyczak JB, Cannon CL, Pier GB. Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microbes Infect 2000 ; 2 : 1051–60. [Google Scholar]
- Singer M, Deutschman CS, Seymour CW, et al. The third international consensus definitions for sepsis and septic shock (sepsis-3). JAMA 2016 ; 315 : 801–10. [CrossRef] [PubMed] [Google Scholar]
- Gellatly SL, Hancock REW. Pseudomonas aeruginosa : new insights into pathogenesis and host defenses. Pathog Dis 2013; 67 : 159–73. [Google Scholar]
- Kaparakis M, Turnbull L, Carneiro L, et al. Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells. Cell Microbiol 2010 ; 12 : 372–85. [Google Scholar]
- Jarczak D, Kluge S, Nierhaus A. Sepsis: pathophysiology and therapeutic concepts. Front Med 2021 ; 8. [Google Scholar]
- Liu T, Zhang L, Joo D, et al. NF-κB signaling in inflammation. Signal Transduct TargetTher. 2017 ; 2 : 1–9. [Google Scholar]
- David L, Taieb F, Pénary M, et al. Outer membrane vesicles produced by pathogenic strains of Escherichia coli block autophagic flux and exacerbate inflammasome activation. Autophagy 2022 ; 18 : 2913–25. [Google Scholar]
- Goman A, Ize B, Jeannot K, et al. Uncovering a new family of conserved virulence factors that promote the production of host-damaging outer membrane vesicles in gram-negative bacteria. JEV 2025 ; 14. [Google Scholar]
- Gutu AD, Rodgers NS, Park J, et al. Pseudomonas aeruginosa high-level resistance to polymyxins and other antimicrobial peptides requires cprA, a gene that is disrupted in the PAO1 strain. Antimicrob Agents Chemother 2015 ; 59 : 5377–87. [Google Scholar]
- Murray JL, Kwon T, Marcotte EM, et al. Intrinsic antimicrobial resistance determinants in the superbug Pseudomonas aeruginosa. mBio 2015 ; 6 : e01603–15. [Google Scholar]
- Cianciulli Sesso A, Lilić B, Amman F, et al. Gene expression profiling of Pseudomonas aeruginosa upon exposure to colistin and tobramycin. Front Microbiol 2021 ; 12. [Google Scholar]
- McPhee JB, Bains M, Winsor G, et al. Contribution of the PhoP-PhoQ and PmrA-PmrB two-component regulatory systems to Mg2+-induced gene regulation in Pseudomonas aeruginosa. J Bacteriol 2006 ; 188 : 3995–4006. [Google Scholar]
- Gooderham WJ, Gellatly SL, Sanschagrin F, et al. The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa. Microbiology 2009 ; 155 : 699–711. [Google Scholar]
- Muller C, Plésiat P, Jeannot K. A two-component regulatory system interconnects resistance to polymyxins, aminoglycosides, fluoroquinolones, and β-lactams in Pseudomonas aeruginosa. Antimicrob Agents Chemother 2011 ; 55 : 1211–21. [Google Scholar]
- Fernández L, Jenssen H, Bains M, et al. The two-component system CprRS senses cationic peptides and triggers adaptive resistance in Pseudomonas aeruginosa independently of ParRS. Antimicrob Agents Chemother 2012 ; 56 : 6212–22. [Google Scholar]
- McPhee JB, Lewenza S, Hancock REW. Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa. Mol Microbiol 2003 ; 50 : 205–17. [Google Scholar]
- Olaitan AO, Morand S, Rolain J-M. Mechanisms of polymyxin resistance: acquired and intrinsic resistance in bacteria. Front Microbiol. 2014 ; 5 : 643. [Google Scholar]
- MacDonald IA, Kuehn MJ. Stress-induced outer membrane vesicle production by Pseudomonas aeruginosa. J Bacteriol 2013 ; 195 : 2971–81. [Google Scholar]
- Burt M, Angelidou G, Mais CN, et al. Lipid A in outer membrane vesicles shields bacteria from polymyxins. J Extracell Vesicles 2024 ; 13 : e12447. [Google Scholar]
- Chen Z, Liu Y, Jiang L, et al. Bacterial outer membrane vesicles increase polymyxin resistance in Pseudomonas aeruginosa while inhibiting its quorum sensing. J Hazard Mater 2024 ; 478 : 135588. [Google Scholar]
- Kulkarni HM, Nagaraj R, Jagannadham MV. Protective role of E. coli outer membrane vesicles against antibiotics. Microbiol Res 2015 ; 181 : 1–7. [Google Scholar]
- Joubert PE, Grégoire IP, Meiffren G, et al. Autophagie et pathogènes : « Bon appétit Messieurs ! ». Med Sci (Paris) 2011 ; 27 : 41–7. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]
- Junkins RD, Shen A, Rosen K, et al. Autophagy enhances bacterial clearance during P. aeruginosa lung infection. PLoS One 2013 ; 8 : e72263. [Google Scholar]
- Mohankumar V, Ramalingam S, Chidambaranathan GP, et al. Autophagy induced by type III secretion system toxins enhances clearance of Pseudomonas aeruginosa from human corneal epithelial cells. Biochem Biophys Res Commun 2018 ; 503 : 1510–5. [Google Scholar]
- Vanaja SK, Russo AJ, Behl B, et al. Bacterial outer membrane vesicles mediate cytosolic localization of LPS and caspase-11 activation. Cell 2016 ; 165 : 1106–19. [Google Scholar]
- Biasizzo M, Kopitar-Jerala N. Interplay between NLRP3 inflammasome and autophagy. Front Immunol 2020 ; 11 : 591803. [Google Scholar]
- Lapaquette P, Thi Thu Nguyen H, Faure M. L’autophagie garante de l’immunité et de l’inflammation: « Tout est bien, tout va bien, tout va pour le mieux qu’il soit possible ». Med Sci (Paris) 2017 ; 33 : 305–11. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]
- Neupane AS, Willson M, Chojnacki AK, et al. Patrolling alveolar macrophages conceal bacteria from the immune system to maintain homeostasis. Cell 2020 ; 183 : 110–125.e11. [Google Scholar]
- Finethy R, Luoma S, Orench-Rivera N, et al. Inflammasome activation by bacterial outer membrane vesicles requires guanylate binding proteins. mBio 2017 ; 8 : e01188–17. [Google Scholar]
- Santos JC, Dick MS, Lagrange B, et al. LPS targets host guanylate-binding proteins to the bacterial outer membrane for non-canonical inflammasome activation. EMBO 2018 ; 37 : e98089. [Google Scholar]
- Shah B, Sullivan CJ, Lonergan NE, et al. Circulating bacterial membrane vesicles cause sepsis in rats. Shock Augusta Ga 2012 ; 37 : 621–8. [Google Scholar]
- Hotchkiss RS, Moldawer LL, Opal SM, et al. Sepsis and septic shock. Nat Rev Dis Primer 2016 ; 2 : 16045. [Google Scholar]
- Deng M, Tang Y, Li W, et al. The endotoxin delivery protein HMGB1 mediates caspase-11-dependent lethality in sepsis. Immunity 2018 ; 49 : 740–753.e7. [CrossRef] [PubMed] [Google Scholar]
- Liu D, Huang S-Y, Sun J-H, et al. Sepsis-induced immunosuppression: mechanisms, diagnosis and current treatment options. Mil Med Res 2022 ; 9 : 56. [Google Scholar]
- Moskowitz SM, Ernst RK, Miller SI. PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A. J Bacteriol 2004 ; 186 : 575–9. [Google Scholar]
- Kapel N, Caballero JD, MacLean RC. Localized pmrB hypermutation drives the evolution of colistin heteroresistance. Cell Rep 2022 ; 39 : 110929. [Google Scholar]
- Bricio-Moreno L, Sheridan VH, Goodhead I, et al. Evolutionary trade-offs associated with loss of PmrB function in host-adapted Pseudomonas aeruginosa. Nat Commun 2018 ; 9 : 2635. [Google Scholar]
- Hasan CM, Pottenger S, Green AE, et al. Pseudomonas aeruginosa utilizes the host-derived polyamine spermidine to facilitate antimicrobial tolerance. JCI Insight 2022 ; 7 : e158879. [Google Scholar]
- Phuong MS, Hernandez RE, Wolter DJ, et al. Impairment in inflammasome signaling by the chronic Pseudomonas aeruginosa isolates from cystic fibrosis patients results in an increase in inflammatory response. Cell Death Dis. 2021 ; 12 : 1–14. [Google Scholar]
- Wolf AJ, Liu GY, Underhill DM. Inflammatory properties of antibiotic-treated bacteria. J Leukoc Biol 2017 ; 101 : 127–34. [Google Scholar]
- Wong CS, Jelacic S, Habeeb RL, et al. The risk of the hemolytic-uremic syndrome after antibiotic treatment of Escherichia coli O157:H7 infections. N Engl J Med 2000 ; 342 : 1930–6. [Google Scholar]
- Ikuta KS. Global mortality associated with 33 bacterial pathogens in 2019: a systematic analysis for the Global Burden of Disease Study 2019. Lancet 2022 ; 400 : 2221–48. [Google Scholar]
- Tamma PD, Heil EL, Justo JA, et al. Infectious diseases society of america 2024 guidance on the treatment of antimicrobial-resistant gram-negative infections. Clin Infect Dis 2024. [Google Scholar]
- Rudd KE, Johnson SC, Agesa KM, et al. Global, regional, and national sepsis incidence and mortality, 1990-2017: analysis for the Global Burden of Disease Study. Lancet 2020 ; 395 : 200–11. [CrossRef] [PubMed] [Google Scholar]
- Niederman MS. Use of broad-spectrum antimicrobials for the treatment of pneumonia in seriously ill patients: maximizing clinical outcomes and minimizing selection of resistant organisms. Clin Infect Dis 2006 ; 42 : S72–S81. [Google Scholar]
- Pea F, Viale P, Furlanut M. Antimicrobial therapy in critically ill patients: a review of pathophysiological conditions responsible for altered disposition and pharmacokinetic variability. Clin Pharmacokinet 2005 ; 44 : 1009–34. [Google Scholar]
- Zhang Y, Ning B. Signaling pathways and intervention therapies in sepsis. Signal Transduct Target Ther 2021 ; 6 : 407. [Google Scholar]
- Vincent JL, Mongkolpun W. Non-antibiotic therapies for sepsis: an update. Expert Rev Anti Infect Ther 2019 ; 17 : 169–75. [Google Scholar]
- Miao R, Huang J. MCC950 improves lipopolysaccharide-induced systemic inflammation in mice by relieving pyroptosis in blood neutrophils. Exp Ther Med 2023 ; 26 : 417. [Google Scholar]
- Li H, Guan Y, Liang B, et al. Therapeutic potential of MCC950, a specific inhibitor of NLRP3 inflammasome. Eur J Pharmacol 2022 ; 928 : 175091. [Google Scholar]
- Harris TL, Worthington RJ, Hittle LE, et al. Small molecule downregulation of PmrAB reverses lipid A modification and breaks colistin resistance. ACS Chem Biol 2014 ; 9 : 122–7. [Google Scholar]
- Furniss RCD, Kostrzewa M, Mavridou DAI, et al. The clue is in the lipid A: Rapid detection of colistin resistance. PLoS Pathog 2020 ; 16 : e1008331. [Google Scholar]
- Knopp M, Babina AM, Gudmundsdóttir JS, et al. A novel type of colistin resistance genes selected from random sequence space. PLoS Genet 2021 ; 17 : e1009227. [Google Scholar]
- Camus L, Vandenesch F, Moreau K. From genotype to phenotype: adaptations of Pseudomonas aeruginosa to the cystic fibrosis environment. Microb Genomics 2021 ; 7 : mgen000513. [Google Scholar]
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.
