APH(3')-Ie, an aminoglycoside-modifying enzyme discovered in a rabbit-derived Citrobacter gillenii isolate.
| Autor: | Lin N; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China., Sha Y; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China., Zhang G; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China., Song C; Medical Molecular Biology Laboratory, School of Medicine, Jinhua Polytechnic, Jinhua, China., Zhang Y; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China., Zhao J; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China., Huang D; Department of Laboratory Sciences, The People's Hospital of Yuhuan, Yuhuan, China., Lu J; Medical Molecular Biology Laboratory, School of Medicine, Jinhua Polytechnic, Jinhua, China., Bao Q; Institute of Bioinformatics, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, China.; Medical Molecular Biology Laboratory, School of Medicine, Jinhua Polytechnic, Jinhua, China.; Department of Laboratory Sciences, Pingyang Hospital of Wenzhou Medical University, Pingyang, China., Pan W; Department of Laboratory Sciences, The People's Hospital of Yuhuan, Yuhuan, China. |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | Frontiers in cellular and infection microbiology [Front Cell Infect Microbiol] 2024 Jul 30; Vol. 14, pp. 1435123. Date of Electronic Publication: 2024 Jul 30 (Print Publication: 2024). |
| DOI: | 10.3389/fcimb.2024.1435123 |
| Abstrakt: | Background: Aminoglycoside-modifying enzymes (AMEs) play an essential role in bacterial resistance to aminoglycoside antimicrobials. With the development of sequencing techniques, more bacterial genomes have been sequenced, which has aided in the discovery of an increasing number of novel resistance mechanisms. Methods: The bacterial species was identified by 16S rRNA gene homology and average nucleotide identity (ANI) analyses. The minimum inhibitory concentration (MIC) of each antimicrobial was determined by the agar dilution method. The protein was expressed with the pCold I vector in E. coli BL21, and enzyme kinetic parameters were examined. The whole-genome sequence of the bacterium was obtained via the Illumina and PacBio sequencing platforms. Reconstruction of the phylogenetic tree, identification of conserved functional residues, and gene context analysis were performed using the corresponding bioinformatic techniques. Results: A novel aminoglycoside resistance gene, designated aph(3')-Ie , which confers resistance to ribostamycin, kanamycin, sisomicin and paromomycin, was identified in the chromosome of the animal bacterium Citrobacter gillenii DW61, which exhibited a multidrug resistance phenotype. APH(3')-Ie showed the highest amino acid identity of 74.90% with the functionally characterized enzyme APH(3')-Ia. Enzyme kinetics analysis demonstrated that it had phosphorylation activity toward four aminoglycoside substrates, exhibiting the highest affinity ( K Conclusion: In this work, a novel chromosomal aminoglycoside resistance gene, designated aph(3')-Ie , conferring resistance to aminoglycoside antimicrobials, was identified in a rabbit isolate C. gillenii DW61. The elucidation of the novel resistance mechanism will aid in the effective treatment of infections caused by pathogens carrying such resistance genes. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as potential conflicts of interest. (Copyright © 2024 Lin, Sha, Zhang, Song, Zhang, Zhao, Huang, Lu, Bao and Pan.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|