188
Views
0
CrossRef citations to date
0
Altmetric
ORIGINAL RESEARCH

Characterization and Molecular Mechanism of Aminoglycoside-6-Adenyl Transferase Associated with Aminoglycoside Resistance from Elizabethkingia meningoseptica

, , , , , , , , , & show all
Pages 5523-5534 | Received 21 Jun 2023, Accepted 09 Aug 2023, Published online: 22 Aug 2023

References

  • King EO. Studies on a group of previously unclassified bacteria associated with meningitis in infants. Am J Clin Pathol. 1959;31(3):241–247. doi:10.1093/ajcp/31.3.241
  • Zajmi A, Teo J, Yeo CC. Epidemiology and characteristics of Elizabethkingia spp. Infections in Southeast Asia. Microorganisms. 2022;10(5):882. doi:10.3390/microorganisms10050882
  • Lau SK, Chow WN, Foo CH, et al. Elizabethkingia anophelis bacteremia is associated with clinically significant infections and high mortality. Sci Rep. 2016;6(1):26045. doi:10.1038/srep26045
  • Lee YL, Liu KM, Chang HL, et al. The evolutionary trend and genomic features of an emerging lineage of elizabethkingia anophelis strains in Taiwan. Microbiol Spectr. 2022;10(1):e0168221. doi:10.1128/spectrum.01682-21
  • Wang M, Gao H, Lin N, et al. The antibiotic resistance and pathogenicity of a multidrug-resistant Elizabethkingia anophelis isolate. Microbiologyopen. 2019;8(11):e804. doi:10.1002/mbo3.804
  • Jospe-Kaufman M, Siomin L, Fridman M. The relationship between the structure and toxicity of aminoglycoside antibiotics. Bioorg Med Chem Lett. 2020;30(13):127218. doi:10.1016/j.bmcl.2020.127218
  • Jaimee G, Halami PM. Emerging resistance to aminoglycosides in lactic acid bacteria of food origin-an impending menace. Appl Microbiol Biotechnol. 2016;100(3):1137–1151. doi:10.1007/s00253-015-7184-y
  • Ramirez MS, Tolmasky ME. Amikacin: uses, resistance, and prospects for inhibition. Molecules. 2017;22(12):2267. doi:10.3390/molecules22122267
  • Zarate SG, De la Cruz Claure ML, Benito-Arenas R, Revuelta J, Santana AG, Bastida A. Overcoming aminoglycoside enzymatic resistance: design of novel antibiotics and inhibitors. Molecules. 2018;23(2):284. doi:10.3390/molecules23020284
  • Wachino JI, Doi Y, Arakawa Y. Aminoglycoside resistance: updates with a focus on acquired 16s ribosomal RNA methyltransferases. Infect Dis Clin North Am. 2020;34(4):887–902. doi:10.1016/j.idc.2020.06.002
  • Carter AP, Clemons WM, Brodersen DE, Morgan-Warren RJ, Wimberly BT, Ramakrishnan V. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature. 2000;407(6802):340–348. doi:10.1038/35030019
  • Breurec S, Criscuolo A, Diancourt L, et al. Genomic epidemiology and global diversity of the emerging bacterial pathogen Elizabethkingia anophelis. Sci Rep. 2016;6(1):30379. doi:10.1038/srep30379
  • Teo J, Tan SY, Liu Y, et al. Comparative genomic analysis of malaria mosquito vector-associated novel pathogen Elizabethkingia anophelis. Genome Biol Evol. 2014;6(5):1158–1165. doi:10.1093/gbe/evu094
  • Sun G, Wang L, Bao C, Li T, Ma L, Chen L. Complete genome sequence of Elizabethkingia meningoseptica, isolated from a T-cell non-Hodgkin’s lymphoma patient. Genome Announc. 2015;3(3):10–128 doi:10.1128/genomeA.00673-15 doi:.1
  • Latorre M, Penalver P, Revuelta J, Asensio JL, Garcia-Junceda E, Bastida A. Rescue of the streptomycin antibiotic activity by using streptidine as a “decoy acceptor” for the aminoglycoside-inactivating enzyme adenyl transferase. Chem Commun. 2007;27(27):2829–2831. doi:10.1039/b704785a
  • Chen Y, Nasvall J, Wu S, Andersson DI, Selmer M. Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3”)(9) adenyltransferase. Acta Crystallogr D Biol Crystallogr. 2015;71(Pt 11):2267–2277. doi:10.1107/S1399004715016429
  • Hormeno L, Ugarte-Ruiz M, Palomo G, et al. ant(6)-I genes encoding aminoglycoside O-nucleotidyltransferases are widely spread Among streptomycin resistant strains of campylobacter jejuni and Campylobacter coli. Front Microbiol. 2018;9:2515. doi:10.3389/fmicb.2018.02515
  • Eberhardt J, Santos-Martins D, Tillack AF, Forli S. AutoDock vina 1.2.0: new docking methods, expanded force field, and python bindings. J Chem Inf Model. 2021;61(8):3891–3898. doi:10.1021/acs.jcim.1c00203
  • Larkin PMK, Mortimer L, Malenfant JH, et al. Investigation of phylogeny and drug resistance mechanisms of Elizabethkingia anophelis isolated from blood and lower respiratory tract. Microb Drug Resist. 2021;27(9):1259–1264. doi:10.1089/mdr.2020.0263
  • Exner M, Bhattacharya S, Christiansen B, et al. Antibiotic resistance: what is so special about multidrug-resistant Gram-negative bacteria? GMS Hyg Infect Control. 2017;12:Doc05. doi:10.3205/dgkh000290
  • Yang C, Liu Z, Yu S, Ye K, Li X, Shen D. Comparison of three species of Elizabethkingia genus by whole-genome sequence analysis. FEMS Microbiol Lett. 2021;368(5):fnab018. doi:10.1093/femsle/fnab018
  • Chernyaeva E, Fedorova E, Zhemkova G, Korneev Y, Kozlov A. Characterization of multiple and extensively drug resistant Mycobacterium tuberculosis isolates with different ofloxacin-resistance levels. Tuberculosis. 2013;93(3):291–295. doi:10.1016/j.tube.2013.02.005
  • Orszulik ST. Quality and suitability of antimicrobial discs: theoretical and practical sources of error and variability. Expert Rev Mol Diagn. 2020;20(3):277–283. doi:10.1080/14737159.2020.1719070
  • Kowalska-Krochmal B, Dudek-Wicher R. The minimum inhibitory concentration of antibiotics: methods, interpretation, clinical relevance. Pathogens. 2021;10(2):165. doi:10.3390/pathogens10020165
  • Mielko KA, Jablonski SJ, Pruss L, et al. Metabolomics comparison of drug-resistant and drug-susceptible Pseudomonas aeruginosa strain (Intra- and Extracellular Analysis). Int J Mol Sci. 2021;22(19):10820. doi:10.3390/ijms221910820
  • Corzana F, Cuesta I, Bastida A, et al. Molecular recognition of aminoglycoside antibiotics by bacterial defence proteins: NMR study of the structural and conformational features of streptomycin inactivation by Bacillus subtilis aminoglycoside-6-adenyl transferase. Chemistry. 2005;11(17):5102–5113. doi:10.1002/chem.200400941
  • Zhang H, Ma G, Zhu Y, et al. Active-site conformational fluctuations promote the enzymatic activity of NDM-1. Antimicrob Agents Chemother. 2018;62(11). doi:10.1128/AAC.01579-18
  • Salahuddin P, Kumar A, Khan AU. Structure, function of serine and metallo-beta-lactamases and their inhibitors. Curr Protein Pept Sci. 2018;19(2):130–144. doi:10.2174/0929866524666170724160623
  • Matesanz R, Diaz JF, Corzana F, Santana AG, Bastida A, Asensio JL. Multiple keys for a single lock: the unusual structural plasticity of the nucleotidyltransferase (4’)/kanamycin complex. Chemistry. 2012;18(10):2875–2889. doi:10.1002/chem.201101888
  • Stern AL, Van der Verren SE, Kanchugal PS, Nasvall J, Gutierrez-de-teran H, Selmer M. Structural mechanism of AadA, a dual-specificity aminoglycoside adenylyltransferase from Salmonella enterica. J Biol Chem. 2018;293(29):11481–11490. doi:10.1074/jbc.RA118.003989
  • Fodor A, Abate BA, Deak P, et al. Multidrug Resistance (MDR) and collateral sensitivity in bacteria, with special attention to genetic and evolutionary aspects and to the perspectives of antimicrobial peptides-a review. Pathogens. 2020;9(7):522. doi:10.3390/pathogens9070522
  • Yin D, Guo Y, Li M, et al. Performance of VITEK 2, E-test, Kirby-Bauer disk diffusion, and modified Kirby-Bauer disk diffusion compared to reference broth microdilution for testing tigecycline susceptibility of carbapenem-resistant K. pneumoniae and A. baumannii in a multicenter study in China. Eur J Clin Microbiol Infect Dis. 2021;40(6):1149–1154. doi:10.1007/s10096-020-04123-z
  • Yuan S, Chen Y, Lin K, et al. Single cell raman spectroscopy deuterium isotope probing for rapid antimicrobial susceptibility test of Elizabethkingia spp. Front Microbiol. 2022;13:876925. doi:10.3389/fmicb.2022.876925
  • Boolchandani M, D’Souza AW, Dantas G. Sequencing-based methods and resources to study antimicrobial resistance. Nat Rev Genet. 2019;20(6):356–370. doi:10.1038/s41576-019-0108-4
  • Wu SH, Xiao YX, Hsiao HC, Jou R, She RC. Development and assessment of a novel whole-gene-based targeted next-generation sequencing assay for detecting the susceptibility of mycobacterium tuberculosis to 14 drugs. Microbiol Spectr. 2022;10(6):e0260522. doi:10.1128/spectrum.02605-22
  • Alcock BP, Huynh W, Chalil R, et al. CARD 2023: expanded curation, support for machine learning, and resistome prediction at the Comprehensive Antibiotic Resistance Database. Nucleic Acids Res. 2023;51(D1):D690–D699. doi:10.1093/nar/gkac920
  • Doster E, Lakin SM, Dean CJ, et al. MEGARes 2.0: a database for classification of antimicrobial drug, biocide and metal resistance determinants in metagenomic sequence data. Nucleic Acids Res. 2020;48(D1):D561–D569. doi:10.1093/nar/gkz1010