Overexpression of Resistance-Nodulation-Division Efflux Pump Genes Contributes to Multidrug Resistance in Aeromonas hydrophila Clinical Isolates

Author(s):  
Chung-Cheng Lo ◽  
Wan-Yu Liao ◽  
Miao-Chen Chou ◽  
Yu-Yi Wu ◽  
Tzu-Hui Yeh ◽  
...  
2010 ◽  
Vol 30 (7) ◽  
pp. 632-638 ◽  
Author(s):  
Tyree H Kiser ◽  
Marilee D Obritsch ◽  
Rose Jung ◽  
Robert MacLaren ◽  
Douglas N Fish

2008 ◽  
Vol 52 (4) ◽  
pp. 1559-1563 ◽  
Author(s):  
Mathieu Hernould ◽  
Séverine Gagné ◽  
Michel Fournier ◽  
Claudine Quentin ◽  
Corinne Arpin

ABSTRACT Gene inactivation and complementation experiments showed that the tripartite AheABC efflux pump of Aeromonas hydrophila extruded at least 13 substrates, including nine antibiotics. The use of phenylalanine-arginine-β-naphthylamide (PAβN) revealed an additional system(s) contributing to intrinsic resistance. This is the first analysis of the role of multidrug efflux systems in Aeromonas spp.


2018 ◽  
Vol 11 (4) ◽  
pp. 371-378 ◽  
Author(s):  
In-Sun Choi ◽  
Choon-Mee Kim ◽  
Sook-Jin Jang

AbstractBackgroundUnderstanding the contribution of efflux pumps to the resistance of antibiotics is useful when considering strategies for antimicrobial therapy.ObjectivesTo assess the role of efflux activity on the resistance of antibiotics commonly used in hospitals.MethodsWe analyzed the efflux activity of 120 clinical isolates of Acinetobacter baumannii using an Hoechst 33342 (H33342) dye-accumulation assay. We compared the indicators for efflux activity of susceptible and non-susceptible groups of each of 16 tested antibiotics. To determine the role of efflux activity on resistance to an antibiotic, we used 3 criteria based on the results of the H33342-accumulation assay.ResultsThe evaluation suggests that efflux activity contributed to resistance to the following 11 antibiotics: cefepime, cefotaxime, ceftazidime, ciprofloxacin, gentamicin, imipenem, meropenem, piperacillin, piperacillin/tazobactam, ticarcillin/ clavulanic acid, and tigecycline. However, ampicillin/sulbactam, minocycline, and trimethoprim/sulfamethoxazole did not meet the criteria, suggesting resistance may not be mediated by efflux activity. A significant difference in efflux activity was observed between bacteria belonging to the multidrug-resistant Acinetobacter baumannii (MDRAB) group and those belonging to the non-MDRAB group.ConclusionsEfflux activity may contribute to multidrug resistance and particularly resistance to numerous antibiotics used in hospitals. These antibiotics would be good candidates for combination therapeutic regimens consisting of an antibiotic and an efflux pump inhibitor as an adjuvant to combat drug efflux.


2020 ◽  
Vol 23 (1) ◽  
pp. 45
Author(s):  
Ji Ae Choi ◽  
Choon-Mee Kim ◽  
Sook-Jin Jang ◽  
Seong-Sik Cho ◽  
Chul Ho Jang ◽  
...  

2015 ◽  
Vol 59 (7) ◽  
pp. 4067-4073 ◽  
Author(s):  
Yi-Tsung Lin ◽  
Yi-Wei Huang ◽  
Shiang-Jiuun Chen ◽  
Chia-Wei Chang ◽  
Tsuey-Ching Yang

ABSTRACTThe resistance-nodulation-division (RND)-type efflux pump is one of the causes of the multidrug resistance ofStenotrophomonas maltophilia. The roles of the RND-type efflux pump in physiological functions and virulence, in addition to antibiotic extrusion, have attracted much attention. In this study, the contributions of the constitutively expressed SmeYZ efflux pump to drug resistance, virulence-related characteristics, and virulence were evaluated.S. maltophiliaKJ is a clinical isolate of multidrug resistance. ThesmeYZisogenic deletion mutant, KJΔYZ, was constructed by a gene replacement strategy. The antimicrobial susceptibility, virulence-related physiological characteristics, susceptibility to human serum and neutrophils, andin vivovirulence between KJ and KJΔYZ were comparatively assessed. The SmeYZ efflux pump contributed resistance to aminoglycosides and trimethoprim-sulfamethoxazole. Inactivation ofsmeYZresulted in attenuation of oxidative stress susceptibility, swimming, flagella formation, biofilm formation, and secreted protease activity. Furthermore, loss of SmeYZ increased susceptibility to human serum and neutrophils and decreasedin vivovirulence in a murine model. These findings suggest the possibility of attenuation of the resistance and virulence ofS. maltophiliawith inhibitors of the SmeYZ efflux pump.


2010 ◽  
Vol 55 (2) ◽  
pp. 921-924 ◽  
Author(s):  
Michelle C. Swick ◽  
Sonia K. Morgan-Linnell ◽  
Kimberly M. Carlson ◽  
Lynn Zechiedrich

ABSTRACTIn a single quantitative study, we measuredacrA,acrB,tolC,mdfA, andnorEexpression inEscherichia coliclinical isolates by using real-time PCR.acrAandacrBoverexpression strongly correlated with fluoroquinolone and multidrug resistance;tolC,mdfA, andnorEexpression did not. The order of abundance of efflux pump transcripts in all fluoroquinolone-susceptible isolates wastolC(highest), thenacrAandacrB, and thenmdfAandnorE.Our findings suggestacrABoverexpression is an indicator of multidrug resistance.


2021 ◽  
Vol 52 (1) ◽  
Author(s):  
Yuhao Dong ◽  
Qing Li ◽  
Jinzhu Geng ◽  
Qing Cao ◽  
Dan Zhao ◽  
...  

AbstractThe TonB system is generally considered as an energy transporting device for the absorption of nutrients. Our recent study showed that deletion of this system caused a significantly increased sensitivity of Aeromonas hydrophila to the macrolides erythromycin and roxithromycin, but had no effect on other classes of antibiotics. In this study, we found the sensitivity of ΔtonB123 to all macrolides tested revealed a 8- to 16-fold increase compared with the wild-type (WT) strain, but this increase was not related with iron deprivation caused by tonB123 deletion. Further study demonstrated that the deletion of tonB123 did not damage the integrity of the bacterial membrane but did hinder the function of macrolide efflux. Compared with the WT strain, deletion of macA2B2, one of two ATP-binding cassette (ABC) types of the macrolide efflux pump, enhanced the sensitivity to the same levels as those of ΔtonB123. Interestingly, the deletion of macA2B2 in the ΔtonB123 mutant did not cause further increase in sensitivity to macrolide resistance, indicating that the macrolide resistance afforded by the MacA2B2 pump was completely abrogated by tonB123 deletion. In addition, macA2B2 expression was not altered in the ΔtonB123 mutant, indicating that any influence of TonB on MacA2B2-mediated macrolide resistance was at the pump activity level. In conclusion, inactivation of the TonB system significantly compromises the resistance of A. hydrophila to macrolides, and the mechanism of action is related to the function of MacA2B2-mediated macrolide efflux.


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