Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 135

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Mechanism of staphylococcal resistance to clinically relevant antibiotics

Brdová, Daniela, Ruml, Tomáš, Viktorová, Jitka·2024·Drug Resistance Updates

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.drup.2024.101147

Cites

7 of 7 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 7 references

Research works printed but not linked: 204

  1. Lai, 2022, Overcoming the rising incidence and evolving mechanisms of antibiotic resistance by novel drug delivery approaches – an overview, Adv. Drug Deliv. Rev., 181, 10.1016/j.addr.2021.114078 · DOI
  2. Davies, 2010, Origins and evolution of antibiotic resistance, Microbiol. Mol. Biol. Rev., 74, 417, 10.1128/MMBR.00016-10 · DOI · Paper page
  3. Ratia, 2022, Gold-derived molecules as new antimicrobial agents, Front. Microbiol., 13, 10.3389/fmicb.2022.846959 · DOI
  4. Jensen, 2009, Genetics of antimicrobial resistance in Staphylococcus aureus, Future Microbiol., 4, 565, 10.2217/fmb.09.30 · DOI · Paper page
  5. Gaynes, 2017, The discovery of penicillin—new insights after more than 75 years of clinical use, Emerg. Infect. Dis., 23, 849, 10.3201/eid2305.161556 · DOI · Paper page
  6. Rammelkamp, 1942, Resistance of Staphylococcus aureus to the Action of Penicillin. Proceedings of the Society for, Exp. Biol. Med., 51, 386, 10.3181/00379727-51-13986 · DOI · Paper page
  7. Peacock, 2015, Mechanisms of methicillin resistance in Staphylococcus aureus, Annu. Rev. Biochem., 84, 577, 10.1146/annurev-biochem-060614-034516 · DOI · Paper page
  8. Barber, 1961, Methicillin-resistant Staphylococci, J. Clin. Pathol., 14, 385, 10.1136/jcp.14.4.385 · DOI · Paper page
  9. Bishara, 2012, Healthcare-associated vs. hospital-acquired Staphylococcus aureus bacteremia, Int. J. Infect. Dis., 16, e457, 10.1016/j.ijid.2012.02.009 · DOI
  10. Tsuji, 2007, Community- and health care-associated methicillin-resistant Staphylococcus aureus: a comparison of molecular epidemiology and antimicrobial activities of various agents, Diagn. Microbiol. Infect. Dis., 58, 41, 10.1016/j.diagmicrobio.2006.10.021 · DOI
  11. Newman, 2015, Chapter 5 - Natural Products as Pharmaceuticals and Sources for Lead Structures, 101
  12. Guo, 2020, Prevalence and therapies of antibiotic-resistance in Staphylococcus aureus, Front. Cell. Infect. Microbiol., 10, 10.3389/fcimb.2020.00107 · DOI · Paper page
  13. Lade, 2022, Molecular basis of non-β-lactam antibiotics resistance in Staphylococcus aureus, Antibiot. (Basel), 11
  14. Kahlmeter, 2019, Point-counterpoint: differences between the european committee on antimicrobial susceptibility testing and clinical and laboratory standards institute recommendations for reporting antimicrobial susceptibility results, J. Clin. Microbiol., 57, 10.1128/JCM.01129-19 · DOI
  15. Costa, 2017, Evolution of antimicrobial resistance in Europe: a factual review, J. Allergy Ther., 8, 1
  16. Fernández, 2011, Creeping baselines and adaptive resistance to antibiotics, Drug Resist. Updates, 14, 1, 10.1016/j.drup.2011.01.001 · DOI · Paper page
  17. Ramirez, 2010, Aminoglycoside modifying enzymes, Drug Resist. Updates, 13, 151, 10.1016/j.drup.2010.08.003 · DOI · Paper page
  18. Douglas, 2023, Staph wars: the antibiotic pipeline strikes back, Microbiol. (Read. ), 169
  19. Chen, 2023, A review of current antibiotic resistance and promising antibiotics with novel modes of action to combat antibiotic resistance, Arch. Microbiol., 205, 356, 10.1007/s00203-023-03699-2 · DOI
  20. Navratna, 2010, Molecular basis for the role of Staphylococcus aureus Penicillin Binding Protein 4 in Antimicrobial Resistance, J. Bacteriol., 192, 134, 10.1128/JB.00822-09 · doi:10.1128/jb.00822-09
  21. Berti, 2013, β-lactam antibiotics targeting PBP1 selectively enhance daptomycin activity against Methicillin-Resistant Staphylococcus aureus, Antimicrob. Agents Chemother., 57, 5005, 10.1128/AAC.00594-13 · DOI
  22. Pinho, 2000, Cloning, characterization, and inactivation of the gene pbpC, encoding penicillin-binding protein 3 of Staphylococcus aureus, J. Bacteriol., 182, 1074, 10.1128/JB.182.4.1074-1079.2000 · DOI
  23. Henze, 1995, Staphylococcus aureus penicillin-binding protein 4 and intrinsic beta-lactam resistance, Antimicrob. Agents Chemother., 39, 2415, 10.1128/AAC.39.11.2415 · DOI
  24. Fisher, 2016, β-lactam resistance mechanisms: gram-positive bacteria and Mycobacterium tuberculosis, Cold Spring Harb. Perspect. Med., 6, 10.1101/cshperspect.a025221 · DOI
  25. da Costa, 2018, PBP4: a new perspective on Staphylococcus aureus β-Lactam Resistance, Microorg. (Basel), 6, 57, 10.3390/microorganisms6030057 · DOI
  26. Ferrer-González, 2017, β-lactam antibiotics with a high affinity for PBP2 act Synergistically with the FtsZ-Targeting Agent TXA707 against Methicillin-Resistant Staphylococcus aureus, Antimicrob. Agents Chemother., 61, e00863, 10.1128/AAC.00863-17 · DOI
  27. Foster, 2017, Antibiotic resistance in Staphylococcus aureus. Current status and future prospects, FEMS Microbiol. Rev., 41, 430, 10.1093/femsre/fux007 · DOI · Paper page
  28. Lowy, 2003, Antimicrobial resistance: the example of Staphylococcus aureus, J. Clin. Investig., 111, 1265, 10.1172/JCI18535 · DOI · Paper page
  29. Alexander, 2023, Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureus, Nat. (Lond. ), 613, 375, 10.1038/s41586-022-05583-3 · DOI
  30. Hartman, 1984, Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus, J. Bacteriol., 158, 513, 10.1128/jb.158.2.513-516.1984 · DOI · Paper page
  31. Utsui, 1985, Role of an altered penicillin-binding protein in methicillin- and cephem-resistant Staphylococcus aureus, Antimicrob. Agents Chemother., 28, 397, 10.1128/AAC.28.3.397 · DOI · Paper page
  32. Strynadka, 2002, Structural basis for the β lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus, Nat. Struct. Biol., 9, 870
  33. Zuniga, 2020, Expression of genes encoding resistance in Staphylococcus spp. isolated from bovine subclinical mastitis in Brazil, J. Infect. Dev. Ctries., 14, 772, 10.3855/jidc.12611 · doi:10.3855/jidc.12611
  34. Uddin, 2017, Associations between resistance phenotype and gene expression in response to serial exposure to oxacillin and ciprofloxacin in Staphylococcus aureus, Lett. Appl. Microbiol., 65, 462, 10.1111/lam.12808 · doi:10.1111/lam.12808
  35. Rosato, 2003, mecA-blaZ corepressors in clinical Staphylococcus aureus isolates, Antimicrob. Agents Chemother., 47, 1460, 10.1128/AAC.47.4.1460-1463.2003 · DOI
  36. Paterson, 2013, The emergence of mecC methicillin-resistant Staphylococcus aureus, Trends Microbiol. (Regul. Ed. ), 22, 42, 10.1016/j.tim.2013.11.003 · doi:10.1016/j.tim.2013.11.003
  37. McClure, 2020, A novel assay for detection of methicillin-resistant Staphylococcus aureus directly from clinical samples, Front. Microbiol., 11
  38. Lozano, 2020, Human mecC-Carrying MRSA: clinical implications and risk factors, Microorg. (Basel), 8, 1615, 10.3390/microorganisms8101615 · DOI
  39. Hryniewicz, 2017, Borderline oxacillin-resistant Staphylococcus aureus (BORSA) - a more common problem than expected?, J. Med. Microbiol., 66, 10.1099/jmm.0.000585 · doi:10.1099/jmm.0.000585
  40. Nomura, 2020, A class A β-lactamase produced by borderline oxacillin-resistant Staphylococcus aureus hydrolyses oxacillin, J. Glob. Antimicrob. Resist., 22, 244, 10.1016/j.jgar.2020.03.002 · DOI
  41. Gitman, 2021, Modified methicillin-resistant Staphylococcus aureus detected in neonatal intensive care patients, J. Antimicrob. Chemother., 76, 2774, 10.1093/jac/dkab266 · doi:10.1093/jac/dkab266
  42. Memmi, 2008, Staphylococcus aureus PBP4 is essential for beta-lactam resistance in community-acquired methicillin-resistant strains, Antimicrob. Agents Chemother., 52, 3955, 10.1128/AAC.00049-08 · DOI · Paper page
  43. Hamilton, 2017, High-level resistance of Staphylococcus aureus to β-Lactam Antibiotics Mediated by Penicillin-binding Protein 4 (PBP4), Antimicrob. Agents Chemother., 61, 10.1128/AAC.02727-16 · DOI
  44. Argudín, 2018, Genetic diversity among staphylococcus aureus isolates showing oxacillin and/or cefoxitin resistance not linked to the presence of mec Genes, Antimicrob. Agents Chemother., 62, 10.1128/AAC.00091-18 · DOI · Paper page
  45. Chatterjee, 2017, PBP4 Mediates β-lactam resistance by altered function, Antimicrob. Agents Chemother., 61, 10.1128/AAC.00932-17 · DOI
  46. Duplessis, 2011, Ceftaroline: a new cephalosporin with activity against methicillin-resistant Staphylococcus aureus (MRSA), Clin. Med. Rev. Ther., 3, 1
  47. Acebrón, 2015, The allosteric site for the nascent cell wall in penicillin-binding protein 2a: an achilles' heel of methicillin-resistant Staphylococcus aureus, Curr. Med. Chem., 22, 1678, 10.2174/0929867322666150311150215 · DOI
  48. Greninger, 2016, Whole-genome sequencing of methicillin-resistant Staphylococcus aureus resistant to fifth-generation cephalosporins reveals potential Non-mecA Mechanisms of Resistance, PloS One, 11, 10.1371/journal.pone.0149541 · DOI · Paper page
  49. Chan, 2015, Ceftobiprole- and ceftaroline-resistant methicillin-resistant Staphylococcus aureus, Antimicrob. Agents Chemother., 59, 2960, 10.1128/AAC.05004-14 · doi:10.1128/aac.05004-14
  50. Liu, 2021, Emerging resistance mechanisms for 4 types of common anti-MRSA antibiotics in Staphylococcus aureus: a comprehensive review, Microb. Pathog., 156, 10.1016/j.micpath.2021.104915 · DOI · Paper page
  51. Zhanel, 2010, New Lipoglycopeptides: a comparative review of dalbavancin, oritavancin and telavancin, Drugs (N. Y., N. Y. ), 70, 859
  52. Szemraj, 2022, Vancomycin heteroresistance among methicillin-resistant clinical isolates S. haemolyticus, S. hominis, S. simulans, and S. warneri, Braz. J. Microbiol.
  53. Peschel, 2000, The d-alanine residues ofstaphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes, Antimicrob. Agents Chemother., 44, 2845, 10.1128/AAC.44.10.2845-2847.2000 · DOI · Paper page
  54. Beauregard, 1995, Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics, Antimicrob. Agents Chemother., 39, 781, 10.1128/AAC.39.3.781 · DOI · Paper page
  55. Zhanel, 2012, Oritavancin: mechanism of action, Clin. Infect. Dis., 54, S214, 10.1093/cid/cir920 · DOI · Paper page
  56. Cong, 2019, Vancomycin resistant Staphylococcus aureus infections: a review of case updating and clinical features, J. Adv. Res., 21
  57. Perichon, 2009, VanA-type vancomycin-resistant Staphylococcus aureus, Antimicrob. Agents Chemother., 53, 4580, 10.1128/AAC.00346-09 · DOI · Paper page
  58. Jacoby, G. Correction to: Transmissible Antibiotic Resistance. 2019. · doi:10.1007/978-3-319-78538-7_25
  59. Thaker, 2015, Vancomycin-variable enterococci can give rise to constitutive resistance during antibiotic therapy, Antimicrob. Agents Chemother., 59, 1405, 10.1128/AAC.04490-14 · DOI
  60. Melo-Cristino, 2013, First case of infection with vancomycin-resistant Staphylococcus aureus in Europe, Lancet, 382, 205, 10.1016/S0140-6736(13)61219-2 · DOI
  61. Hiramatsu, 2014, Vancomycin-intermediate resistance in Staphylococcus aureus, J. Glob. Antimicrob. Resist., 2, 213, 10.1016/j.jgar.2014.04.006 · DOI
  62. Delaune, 2012, The WalKR system controls major Staphylococcal virulence genes and is involved in triggering the host inflammatory response, Infect. Immun., 80, 3438, 10.1128/IAI.00195-12 · DOI · Paper page
  63. Yin, 2006, VraSR Two-component regulatory system and its role in induction of pbp2 and vraSR expression by cell wall antimicrobials in Staphylococcus aureus, Antimicrob. Agents Chemother., 50, 336, 10.1128/AAC.50.1.336-343.2006 · DOI
  64. Chen, 2021, The role of graRS in regulating virulence and antimicrobial resistance in methicillin-resistant Staphylococcus aureus, Front. Microbiol., 12
  65. Zhu, 2021, A novel mutation of walK confers vancomycin-intermediate resistance in methicillin-susceptible Staphylococcus aureus, Int. J. Med. Microbiol., 311, 10.1016/j.ijmm.2021.151473 · DOI
  66. Crotty, 2016, New gram-positive agents: the next generation of oxazolidinones and Lipoglycopeptides, J. Clin. Microbiol., 54, 2225, 10.1128/JCM.03395-15 · doi:10.1128/jcm.03395-15
  67. Gonzalez-Ruiz, 2011, Clinical experience with daptomycin in Europe: The first 2.5 years, J. Antimicrob. Chemother., 66, 912, 10.1093/jac/dkq528 · DOI
  68. Grein, 2020, Ca2+-Daptomycin targets cell wall biosynthesis by forming a tripartite complex with undecaprenyl-coupled intermediates and membrane lipids, Nat. Commun., 11, 10.1038/s41467-020-15257-1 · DOI · Paper page
  69. Heidary, 2018, Daptomycin, J. Antimicrob. Chemother., 73, 1, 10.1093/jac/dkx349 · DOI · Paper page
  70. Gray, 2020, More than a pore: a current perspective on the in vivo mode of action of the lipopeptide antibiotic daptomycin, Antibiotics, 9, 10.3390/antibiotics9010017 · DOI
  71. Grünewald, 2004, Synthesis and derivatization of daptomycin: a chemoenzymatic route to acidic lipopeptide antibiotics, J. Am. Chem. Soc., 126, 17025, 10.1021/ja045455t · DOI
  72. Gómez Casanova, 2017, Mechanisms of resistance to daptomycin in Staphylococcus aureus, Rev. Esp. Quimioter., 30, 391
  73. Gutiérrez-Chávez, 2021, The ecological roles of microbial lipopeptides: Where are we going?, Comput. Struct. Biotechnol. J., 19, 1400, 10.1016/j.csbj.2021.02.017 · DOI
  74. Zhang, 2014, Cardiolipin prevents membrane translocation and permeabilization by daptomycin, J. Biol. Chem., 289, 11584, 10.1074/jbc.M114.554444 · DOI · Paper page
  75. Miller, 2016, Mechanism of action and resistance to daptomycin in Staphylococcus aureus and Enterococci, Cold Spring Harb. Perspect. Med., 6, 10.1101/cshperspect.a026997 · DOI · Paper page
  76. Bayer, 2013, Mechanisms of daptomycin resistance in Staphylococcus aureus: role of the cell membrane and cell wall, Ann. N. Y. Acad. Sci., 1277, 139, 10.1111/j.1749-6632.2012.06819.x · DOI · Paper page
  77. Bayer, 2015, Frequency and distribution of single-nucleotide polymorphisms within mprF in methicillin-resistant staphylococcus aureus clinical isolates and their role in cross-resistance to daptomycin and host defense antimicrobial peptides, Antimicrob. Agents Chemother., 59, 4930, 10.1128/AAC.00970-15 · DOI
  78. Cafiso, 2014, dltA overexpression: A strain-independent keystone of daptomycin resistance in methicillin-resistant Staphylococcus aureus, Int. J. Antimicrob. Agents, 43, 26, 10.1016/j.ijantimicag.2013.10.001 · DOI
  79. Kattke, M., Gosschalk, J., Martinez, O., Kumar, G., Gale, R., Cascio, D., Sawaya, M., Phillips, M., Brown, E., Clubb, R., 2018. Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria; 2018. DOI: 10.1101/507483 10.1101/507483.. · DOI
  80. Bertsche, 2013, Increased cell wall teichoic acid production and D-alanylation are common phenotypes among daptomycin-resistant methicillin-resistant Staphylococcus aureus (MRSA) clinical isolates, PLoS One, 8, 10.1371/journal.pone.0067398 · DOI
  81. Koprivnjak, 2011, Characterization of Staphylococcus aureus Cardiolipin Synthases 1 and 2 and their contribution to accumulation of cardiolipin in stationary phase and within phagocytes, J. Bacteriol., 193, 4134, 10.1128/JB.00288-11 · DOI
  82. Lasek-Nesselquist, 2019, Insights into the evolution of staphylococcus aureus daptomycin resistance from an in vitro bioreactor model, Front. Microbiol., 10, 345, 10.3389/fmicb.2019.00345 · DOI
  83. Zhang, 2014, Cardiolipin prevents membrane translocation and permeabilization by daptomycin, J. Biol. Chem., 289
  84. Bæk, 2015, Stepwise decrease in daptomycin susceptibility in clinical Staphylococcus aureus isolates associated with an initial mutation in rpoB and a compensatory inactivation of the clpX gene, Antimicrob. Agents Chemother., 59, 6983, 10.1128/AAC.01303-15 · DOI
  85. Howden, 2011, Evolution of multidrug resistance during Staphylococcus aureus infection involves mutation of the essential two component regulator WalKR, PLoS Pathog., 7, 10.1371/journal.ppat.1002359 · DOI · Paper page
  86. Pader, 2016, Staphylococcus aureus inactivates daptomycin by releasing membrane phospholipids, Nat. Microbiol., 2, 10.1038/nmicrobiol.2016.194 · DOI
  87. Pee, C., Pader, V., Ledger, E., Edwards, A., 2018. , A FASII inhibitor prevents staphylococcal evasion of daptomycin by inhibiting phospholipid decoy production; 2018. DOI: 10.1101/427989.. · doi:10.1101/427989
  88. Krause, 2016, Aminoglycosides: an overview, Cold Spring Harb. Perspect. Med., 6, 10.1101/cshperspect.a027029 · DOI · Paper page
  89. Ramirez, 2017, Amikacin: uses, resistance, and prospects for inhibition, Mol. (Basel, Switz. ), 22, 2267, 10.3390/molecules22122267 · DOI · Paper page
  90. Stankowicz, M., Ibrahim, J., Brown, D., 2015. Once-daily aminoglycoside dosing: An update on current literature. American Journal of Health-System Pharmacy: AJHP: Official Journal of The American Society of Health-System Pharmacists 2015, 72, 1357-1364. DOI: 10.2146/ajhp140564. · doi:10.2146/ajhp140564
  91. Serio, 2018, Aminoglycoside revival: review of a historically important class of antimicrobials undergoing rejuvenation, EcoSal, 8
  92. Zhanel, 2012, Comparison of the next-generation aminoglycoside plazomicin to gentamicin, tobramycin and amikacin, Expert Rev. Anti-Infect. Ther., 10, 459, 10.1586/eri.12.25 · DOI · Paper page
  93. Mingeot-Leclercq, 1999, Aminoglycosides: activity and resistance, Antimicrob. Agents Chemother., 43, 727, 10.1128/AAC.43.4.727 · DOI · Paper page
  94. Ramirez, 2017, Amikacin: uses, resistance, and prospects for inhibition, Molecules, 22, 2267, 10.3390/molecules22122267 · DOI · Paper page
  95. Serio, 2018, Aminoglycoside revival: review of a historically important class of antimicrobials undergoing rejuvenation, EcoSal, 8
  96. Kong, 2020, Exploration of antibiotic activity of aminoglycosides, in particular ribostamycin alone and in combination with ethylenediaminetetraacetic acid against pathogenic bacteria, Front. Microbiol., 11, 1718, 10.3389/fmicb.2020.01718 · DOI
  97. Webster, 2022, A mini-review: environmental and metabolic factors affecting aminoglycoside efficacy, World J. Microbiol. Biotechnol., 39
  98. Krause, 2016, Aminoglycosides: an overview, Cold Spring Harb. Perspect. Med., 6, a027029, 10.1101/cshperspect.a027029 · DOI · Paper page
  99. Ramirez, 2010, Aminoglycoside modifying enzymes, Drug Resist. Updates, 13, 151, 10.1016/j.drup.2010.08.003 · DOI · Paper page
  100. Doi, 2016, Aminoglycoside resistance: the emergence of acquired 16s ribosomal RNA methyltransferases, Infect. Dis. Clin. North Am., 30, 523, 10.1016/j.idc.2016.02.011 · DOI · Paper page
  101. Khosravi, 2017, Distribution of genes encoding resistance to aminoglycoside modifying enzymes in methicillin-resistant Staphylococcus aureus (MRSA) strains, Kaohsiung J. Med. Sci., 33, 587, 10.1016/j.kjms.2017.08.001 · DOI
  102. Szymanek-Majchrzak, 2018, Resistance to aminoglycosides of methicillin-resistant strains of staphylococcus aureus, originating in the surgical and transplantation wards of the warsaw clinical center—a retrospective analysis, Transplant. Proc., 50, 2170, 10.1016/j.transproceed.2018.02.158 · DOI · Paper page
  103. Costa, 2019, High Prevalence of the aac(6′)-Ie-aph(2′′)-Ia Gene in Hospital Isolates of Enterococcus faecalis Co-Resistant to Gentamicin and Penicillin, Microb. Drug Resist., 25, 1275, 10.1089/mdr.2018.0466 · DOI
  104. Frase, 2012, Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside Acetyltransferase(6′)-Ie/Aminoglycoside Phosphotransferase(2″)-Ia Enzyme, J. Biol. Chem., 287, 43262, 10.1074/jbc.M112.416453 · DOI
  105. Zárate, 2018, Overcoming aminoglycoside enzymatic resistance: design of novel antibiotics and inhibitors, Molecules, 23, 10.3390/molecules23020284 · DOI
  106. Shakya, 2010, Nucleotide selectivity of antibiotic kinases, Antimicrob. Agents Chemother., 54, 1909, 10.1128/AAC.01570-09 · DOI
  107. Kanchugal P, 2020, Structural recognition of spectinomycin by resistance enzyme ANT(9) from Enterococcus faecalis, Antimicrob. Agents Chemother., 64, 10.1128/AAC.00371-20 · DOI
  108. Cox, 2018, Plazomicin retains antibiotic activity against most aminoglycoside modifying enzymes, ACS Infect. Dis., 4, 980, 10.1021/acsinfecdis.8b00001 · DOI
  109. Rocha, 2021, Inhibition of Aminoglycoside 6′-N-acetyltransferase Type Ib (AAC(6′)-Ib): structure–activity relationship of substituted pyrrolidine pentamine derivatives as inhibitors, Biomedicines, 9, 1218, 10.3390/biomedicines9091218 · doi:10.3390/biomedicines9091218
  110. Labby, 2013, Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections, Future Med. Chem., 5, 1285, 10.4155/fmc.13.80 · DOI
  111. Quirke, 2022, Structure-Activity Relationships for 5'' Modifications of 4,5-Aminoglycoside Antibiotics, ChemMedChem, 17, 10.1002/cmdc.202200120 · doi:10.1002/cmdc.202200120
  112. Yan, 2022, Design, Synthesis, and Bioassay of 2′-Modified Kanamycin A, Molecules, 27, 10.3390/molecules27217482 · DOI
  113. Costa, 2020, Development of peptides that inhibit aminoglycoside-modifying enzymes and β-lactamases for control of resistant bacteria, Curr. Protein Pept. Sci., 21, 1011, 10.2174/1389203721666200915113630 · doi:10.2174/1389203721666200915113630
  114. Williams, 1979, Synthesis of a tight-binding, multisubstrate analog inhibitor of gentamicin acetyltransferase I, J. Antibiot. (Tokyo), 32, 1147, 10.7164/antibiotics.32.1147 · doi:10.7164/antibiotics.32.1147
  115. Wang, 2022, Antibiotic combination therapy: a strategy to overcome bacterial resistance to aminoglycoside antibiotics, Front. Pharmacol., 13
  116. Grossman, 2016, Tetracycline Antibiotics and Resistance, Cold Spring Harb. Perspect. Med., 6, a025387, 10.1101/cshperspect.a025387 · DOI · Paper page
  117. Duggar, 1948, Aureomycin; a product of the continuing search for new antibiotics. Annuals, N. Y. Acad. Sci., 51, 177, 10.1111/j.1749-6632.1948.tb27262.x · DOI · Paper page
  118. Finlay, 1950, Terramycin, a new antibiotic, Science, 111, 85, 10.1126/science.111.2874.85.a · doi:10.1126/science.111.2874.85.a
  119. Nelson, 2011, The history of the tetracyclines. Annuals, N. Y. Acad. Sci., 1241, 17, 10.1111/j.1749-6632.2011.06354.x · DOI · Paper page
  120. McCormick, 1957, A new family of antibiotics: the demethyltetracyclines, J. Am. Chem. Soc., 79, 4561, 10.1021/ja01573a089 · doi:10.1021/ja01573a089
  121. Rusu, 2021, The development of third-generation tetracycline antibiotics and new perspectives, Pharmaceutics, 13, 10.3390/pharmaceutics13122085 · DOI · Paper page
  122. Stein, 2006, Tigecycline: a critical analysis, Clin. Infect. Dis., 43, 518, 10.1086/505494 · DOI · Paper page
  123. Gallagher, 2019, Omadacycline: a modernized tetracycline, Clin. Infect. Dis., 69, S1, 10.1093/cid/ciz394 · doi:10.1093/cid/ciz394
  124. Coppock, 2018, FDA approves eravacycline for adults with complicated intra-abdominal infections, Pharmacy
  125. Durães, 2019, Omadacycline: a newly approved antibacterial from the class of tetracyclines, Pharm. (Basel), 12
  126. Wilson, 2020, Target protection as a key antibiotic resistance mechanism, Nat. Rev. Microbiol., 18, 637, 10.1038/s41579-020-0386-z · DOI · Paper page
  127. Ero, 2021, Ribosome protection proteins—“New” players in the global arms race with antibiotic-resistant pathogens, Int. J. Mol. Sci., 22, 10.3390/ijms22105356 · DOI
  128. Dönhöfer, 2012, Structural basis for TetM-mediated tetracycline resistance, Proc. Natl. Acad. Sci., 109, 16900, 10.1073/pnas.1208037109 · DOI · Paper page
  129. Arenz, 2015, Cryo-EM structure of the tetracycline resistance protein TetM in complex with a translating ribosome at 3.9-å resolution, Proc. Natl. Acad. Sci., 112, 5401, 10.1073/pnas.1501775112 · DOI
  130. Burdett, 1996, Tet(M)-promoted release of tetracycline from ribosomes is GTP dependent, J. Bacteriol., 178, 3246, 10.1128/jb.178.11.3246-3251.1996 · DOI · Paper page
  131. Nguyen, 2014, Tetracycline antibiotics and resistance mechanisms, Biol. Chem., 395, 559, 10.1515/hsz-2013-0292 · DOI · Paper page
  132. Zhang, 2022, Dissemination and prevalence of plasmid-mediated high-level tigecycline resistance gene tet (X4), Front. Microbiol., 13
  133. Kannan, 2011, Macrolide antibiotics in the ribosome exit tunnel: species-specific binding and action. Annuals, N. Y. Acad. Sci., 1241, 33, 10.1111/j.1749-6632.2011.06315.x · DOI
  134. Miklasińska-Majdanik, 2021, Mechanisms of resistance to macrolide antibiotics among Staphylococcus aureus, Antibiotics, 10, 1406, 10.3390/antibiotics10111406 · DOI · Paper page
  135. Schwarz, 2016, Lincosamides, streptogramins, phenicols, and pleuromutilins: mode of action and mechanisms of resistance, Cold Spring Harb. Perspect. Med., 6, 10.1101/cshperspect.a027037 · DOI
  136. Tenson, 2003, The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome, J. Mol. Biol., 330, 1005, 10.1016/S0022-2836(03)00662-4 · DOI · Paper page
  137. Feßler, 2018, Mobile macrolide resistance genes in staphylococci, Plasmid, 99, 2, 10.1016/j.plasmid.2018.05.001 · DOI
  138. Galarion, 2023, The native ABC-F proteins of Staphylococcus aureus do not contribute to intrinsic resistance against ribosome-targeting antibacterial drugs, J. Antimicrob. Chemother., 78, 2601, 10.1093/jac/dkad238 · DOI
  139. Sharkey, 2016, ABC-F proteins mediate antibiotic resistance through ribosomal protection, mBio, 7, 10.1128/mBio.01975-15 · DOI · Paper page
  140. Ero, 2019, Ribosome protection by ABC-F proteins-molecular mechanism and potential drug design, Protein Sci., 28, 684, 10.1002/pro.3589 · DOI
  141. Vimberg, 2020, Ribosome-mediated attenuation of vga(A) expression is shaped by the antibiotic resistance specificity of Vga(A) Protein Variants, Antimicrob. Agents Chemother., 64, 10.1128/AAC.00666-20 · DOI
  142. Izard, 2001, Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity, Protein Sci., 10, 1508, 10.1002/pro.101508 · doi:10.1002/pro.101508
  143. Foti, 2021, Oxazolidinone antibiotics: chemical, biological and analytical aspects, Molecules, 26, 10.3390/molecules26144280 · DOI · Paper page
  144. Paukner, 2017, Pleuromutilins: potent drugs for resistant bugs-mode of action and resistance, Cold Spring Harb. Perspect. Med., 7, 10.1101/cshperspect.a027110 · DOI · Paper page
  145. Zhanel, 2021, Lefamulin: a novel oral and intravenous pleuromutilin for the treatment of community-acquired bacterial pneumonia, Drugs, 81, 233, 10.1007/s40265-020-01443-4 · DOI
  146. Mohamad, 2022, Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci, Nucleic Acids Res., 50, 2128, 10.1093/nar/gkac058 · DOI
  147. Khoshnood, 2019, A review on mechanism of action, resistance, synergism, and clinical implications of mupirocin against Staphylococcus aureus, Biomed. Pharmacother., 109, 1809, 10.1016/j.biopha.2018.10.131 · DOI
  148. Westgeest, 2024, Eradication of community-onset Methicillin-resistant Staphylococcus aureus carriage: a narrative review, Clin. Microbiol. Infect., 10.1016/j.cmi.2024.01.003 · DOI
  149. Tucaliuc, 2019, Mupirocin: applications and production, Biotechnol. Lett., 41, 495, 10.1007/s10529-019-02670-w · doi:10.1007/s10529-019-02670-w
  150. Dadashi, 2020, Mupirocin resistance in Staphylococcus aureus: a systematic review and meta-analysis, J. Glob. Antimicrob. Resist., 20, 238, 10.1016/j.jgar.2019.07.032 · doi:10.1016/j.jgar.2019.07.032
  151. Wang, 2022, Methicillin-resistant Staphylococcus aureus in China: a multicentre longitudinal study and whole-genome sequencing, Emerg. Microbes Infect., 11, 532, 10.1080/22221751.2022.2032373 · DOI · Paper page
  152. González-López, 2024, Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane, Sci. Rep., 14, 10.1038/s41598-024-64868-x · DOI
  153. Fernandes, 2016, Fusidic acid: a bacterial elongation factor inhibitor for the oral treatment of acute and chronic staphylococcal infections, Cold Spring Harb. Perspect. Med., 6, a025437, 10.1101/cshperspect.a025437 · DOI
  154. Lesher, 1962, 1,8-naphthyridine derivatives. A new class of chemotherapeutic agents, J. Med. Pharm. Chem., 5, 1063, 10.1021/jm01240a021 · DOI · Paper page
  155. Correia, 2017, Mechanisms of quinolone action and resistance: where do we stand?, J. Med. Microbiol., 66, 551, 10.1099/jmm.0.000475 · DOI · Paper page
  156. Baggio, 2021, Fluoroquinolone antibiotics and adverse events, Aust. Prescr., 44, 161, 10.18773/austprescr.2021.035 · DOI · Paper page
  157. Aldred, 2014, Mechanism of quinolone action and resistance, Biochemistry, 53, 1565, 10.1021/bi5000564 · DOI · Paper page
  158. Tang, 2023, Quinolone antibiotics: resistance and therapy, Infect. Drug Resist., 16, 811, 10.2147/IDR.S401663 · DOI
  159. Shariati, 2022, The resistance mechanisms of bacteria against ciprofloxacin and new approaches for enhancing the efficacy of this antibiotic, Front. Public Health, 10, 10.3389/fpubh.2022.1025633 · DOI · Paper page
  160. Pham, 2019, Quinolone antibiotics, MedChemComm, 10, 1719, 10.1039/C9MD00120D · DOI · Paper page
  161. Huynh, 2023, Genomic alterations involved in fluoroquinolone resistance development in Staphylococcus aureus, PLoS One, 18, 10.1371/journal.pone.0287973 · DOI
  162. Hamza, 2023, Molecular investigation of quinolone-resistant genes among clinical Staphylococcus aureus isolates in Babylon hospitals, Med. J. Babylon., 20, 553, 10.4103/MJBL.MJBL_347_23 · doi:10.4103/mjbl.mjbl_347_23
  163. Masters, 2003, Trimethoprim-sulfamethoxazole revisited, Arch. Intern. Med., 163, 402, 10.1001/archinte.163.4.402 · DOI · Paper page
  164. Stevens, 2014, Practice guidelines for the diagnosis and management of skin and soft tissue infections: 2014 update by the infectious diseases society of America, Clin. Infect. Dis., 59, e10, 10.1093/cid/ciu296 · DOI · Paper page
  165. Haseeb, 2022, Trimethoprim-Sulfamethoxazole (Bactrim) dose optimization in Pneumocystis jirovecii Pneumonia (PCP) Management: a systematic review, Int. J. Environ. Res. Public Health, 19, 10.3390/ijerph19052833 · DOI
  166. McCarter, 2017, Antibiotics: challenges, mechanisms, opportunities Written by Christopher Walsh, PhD and Timothy Wencewicz, PhD, Lab. Med., 48, 10.1093/labmed/lmw070 · doi:10.1093/labmed/lmw070
  167. Goldberg, 2012, Contemporary unconventional clinical use of co-trimoxazole, Clin. Microbiol. Infect., 18, 8, 10.1111/j.1469-0691.2011.03613.x · DOI
  168. Sensi, 1960, A new antibiotic of the rifomycin family, Farm. Sci., 15, 228
  169. Hardie, 2022, JMM profile: rifampicin: a broad-spectrum antibiotic, J. Med. Microbiol., 71, 10.1099/jmm.0.001566 · doi:10.1099/jmm.0.001566
  170. Wang, 2019, Evolution of resistance mechanisms and biological characteristics of rifampicin-resistant Staphylococcus aureus strains selected in vitro, BMC Microbiol., 19, 220, 10.1186/s12866-019-1573-9 · DOI
  171. Zheng, 2021, Resistance profiles and biological characteristics of rifampicin-resistant Staphylococcus aureus small-colony variants, Infect. Drug Resist., 14, 1527, 10.2147/IDR.S301863 · DOI
  172. Zhang, 2023, The development of variation-based rifampicin resistance in Staphylococcus aureus deciphered through genomic and transcriptomic study, J. Hazard. Mater., 442, 10.1016/j.jhazmat.2022.130112 · DOI
  173. Lee, 2022, Rifamycin resistance, rpoB gene mutation and clinical outcomes of Staphylococcus species isolates from prosthetic joint infections in Republic of Korea, J. Glob. Antimicrob. Resist., 28, 43, 10.1016/j.jgar.2021.12.005 · doi:10.1016/j.jgar.2021.12.005
  174. Dashtbani-Roozbehani, 2021, Efflux pump mediated antimicrobial resistance by Staphylococci in Health-Related Environments: Challenges and the Quest for Inhibition, Antibiot. (Basel), 10
  175. Alnaseri, 2015, Inducible expression of a resistance-nodulation-division-type efflux pump in Staphylococcus aureus provides resistance to linoleic and arachidonic acids, J. Bacteriol., 197, 1893, 10.1128/JB.02607-14 · DOI
  176. Ding, 2023, Role of efflux pumps, their inhibitors, and regulators in colistin resistance, Front. Microbiol., 14, 10.3389/fmicb.2023.1207441 · DOI
  177. Nishino, 2021, Function and Inhibitory Mechanisms of Multidrug Efflux Pumps, Front. Microbiol., 12, 10.3389/fmicb.2021.737288 · DOI · Paper page
  178. Lekshmi, 2018, Modulation of antimicrobial efflux pumps of the major facilitator superfamily in Staphylococcus aureus, AIMS Microbiol., 4, 1, 10.3934/microbiol.2018.1.1 · DOI
  179. Floyd, 2010, LmrS is a multidrug efflux pump of the major facilitator superfamily from Staphylococcus aureus, Antimicrob. Agents Chemother., 54, 5406, 10.1128/AAC.00580-10 · DOI · Paper page
  180. Vimberg, 2020, VanZ reduces the binding of lipoglycopeptide antibiotics to Staphylococcus aureus and Streptococcus pneumoniae Cells, Front. Microbiol., 11, 566, 10.3389/fmicb.2020.00566 · DOI
  181. Liu, 2019, Potential of marine natural products against drug-resistant bacterial infections, Lancet Infect. Dis., 19, e237, 10.1016/S1473-3099(18)30711-4 · DOI
  182. Dash, 2021, Thanatin: an emerging host defense antimicrobial peptide with multiple modes of action, Int. J. Mol. Sci., 22, 10.3390/ijms22041522 · DOI
  183. Piller, 2022, Membrane Activity of LL-37 derived antimicrobial peptides against Enterococcus hirae: superiority of SAAP-148 over OP-145, Biomolecules, 12, 10.3390/biom12040523 · DOI
  184. Le, 2022, Efficiency of antimicrobial peptides against multidrug-resistant staphylococcal pathogens, Front. Microbiol., 13, 10.3389/fmicb.2022.930629 · DOI
  185. Gajdács, 2019, The continuing threat of methicillin-resistant Staphylococcus aureus, Antibiot. (Basel), 8
  186. Tripathy, 2019, FtsZ inhibitors as a new genera of antibacterial agents, Bioorg. Chem., 91, 10.1016/j.bioorg.2019.103169 · DOI
  187. Bibens, 2023, A review of fatty acid biosynthesis enzyme inhibitors as promising antimicrobial drugs, Pharm. (Basel), 16
  188. Naclerio, 2019, Antibacterial small molecules that potently inhibit staphylococcus aureus lipoteichoic acid biosynthesis, ChemMedChem, 14, 1000, 10.1002/cmdc.201900053 · DOI
  189. Hurtová, 2024, Nitrogen-containing flavonoids─preparation and biological activity, ACS Omega, 9, 34938, 10.1021/acsomega.4c04627 · doi:10.1021/acsomega.4c04627
  190. Magaña, 2023, Restoring susceptibility to aminoglycosides: identifying small molecule inhibitors of enzymatic inactivation, RSC Med. Chem., 14, 1591, 10.1039/D3MD00226H · doi:10.1039/d3md00226h
  191. Douglas, 2023, Novel antimicrobial strategies to treat multi-drug resistant Staphylococcus aureus infections, Microb. Biotechnol., 16, 1456, 10.1111/1751-7915.14268 · DOI
  192. Chand, 2023, Staphylococcus aureus vaccine strategy: promise and challenges, Microbiol. Res., 271, 10.1016/j.micres.2023.127362 · DOI
  193. Peck, 2019, A Phase 1, Randomized, Single-Ascending-Dose Study To Investigate the Safety, Tolerability, and Pharmacokinetics of DSTA4637S, an Anti-Staphylococcus aureus Thiomab Antibody-Antibiotic Conjugate, in Healthy Volunteers, Antimicrob. Agents Chemother., 63, 10.1128/AAC.02588-18 · DOI
  194. Atshan, 2023, Phage therapy as an alternative treatment modality for resistant staphylococcus aureus infections, Antibiot. (Basel), 12
  195. Liu, 2024, Bacteriophage therapy for drug-resistant Staphylococcus aureus infections, Front. Cell. Infect. Microbiol., 14
  196. Liu, 2024, Staphylococcus aureus Infections and Human Intestinal Microbiota, Pathogens, 13, 10.3390/pathogens13040276 · DOI · Paper page
  197. Walvekar, 2019, Self-assembled oleylamine grafted hyaluronic acid polymersomes for delivery of vancomycin against methicillin resistant Staphylococcus aureus (MRSA), Colloids Surf. B: Biointerfaces, 182, 10.1016/j.colsurfb.2019.110388 · DOI
  198. Thamilselvan, 2023, Polymer based dual drug delivery system for targeted treatment of fluoroquinolone resistant Staphylococcus aureus mediated infections, Sci. Rep., 13, 10.1038/s41598-023-38473-3 · DOI
  199. Joshi, 2023, Metal nanoparticles as inhibitors of enzymes and toxins of multidrug-resistant Staphylococcus aureus, Infect. Med., 2, 294, 10.1016/j.imj.2023.11.006 · DOI
  200. Rani, 2022, Surface-engineered liposomes for dual-drug delivery targeting strategy against methicillin-resistant Staphylococcus aureus (MRSA), Asian J. Pharm. Sci., 17, 102, 10.1016/j.ajps.2021.11.004 · DOI

200 of 204 shown

Cited by

See all 135

Metadata

Authors
Brdová, D., Ruml, T., & Viktorová, J.
Venue
Drug Resistance Updates
Publisher
Elsevier BV
Published
2024-11
Volume
77
Pages
101147
ISSN
1368-7646
Cited by
135
References
7
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Mechanism of staphylococcal resistance to clinically relevant antibiotics. https://app.cochat.ai/papers/10.1016/j.drup.2024.101147
The paper
Brdová, D., Ruml, T., & Viktorová, J. (2024). Mechanism of staphylococcal resistance to clinically relevant antibiotics. Drug Resistance Updates. https://doi.org/10.1016/j.drup.2024.101147

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.