Molecule Information

General Information of the Molecule (ID: Mol04270)

• Name: 16S rRNA adenine dimethyltransferase (KsgA) ,Escherichia coli
• Synonyms: 16S rRNA adenine dimethyltransferase (KsgA)
• Molecule Type: Protein

Kingdom: N.A.
Phylum: Proteobacteria
Class: Gammaproteobacteria
Order: Enterobacterales
Family: Enterobacteriaceae
Genus: Escherichia
Species: Escherichia coli

Type(s) of Resistant Mechanism of This Molecule

  ADTT: Aberration of the Drug's Therapeutic Target

Drug Resistance Data Categorized by Drug

Approved Drug(s) 3 drug(s) in total

Hygromycin B

Drug Sensitivity Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Lactobacillus casei infection [ICD-11: 1A00-1C4Z] [1]

• Sensitive Disease: Lactobacillus casei infection [ICD-11: 1A00-1C4Z]
• Sensitive Drug: Hygromycin B
• Molecule Alteration: Missense mutation; A1518/1519
• Experimental Note: Revealed Based on the Cell Line Data
• In Vitro Model: Pseudomonas aeruginosa strain UCBPP-PA14; 1763
• Experiment for Molecule Alteration: Primer extension analysis; MS analysis; Western blot assay; Semiquantitative RT-PCR
• Experiment for Drug Resistance: Phenotypic microarrays assay; MIC assay; Oxidative stress sensitivity testing; Superoxide dismutase enzyme activity assay
• Mechanism Description: In this study, we demonstrated the absence of A1518/1519 methylation in the 16S rRNA of a Pseudomonas aeruginosa ksgA mutant. Biolog phenotypic microarrays were used to screen the phenotypes of the ksgA mutant against various antimicrobial agents. The loss of ksgA led to increased sensitivity to menadione, a superoxide generator, which was, at least in part, attributed to decreased in a superoxide dismutase (SOD) activity. Interestingly, the decrease in SOD activity in the ksgA mutant was linked to a decrease in the SodM protein levels, but not the sodM mRNA levels. Furthermore, the ksgA mutant strain exhibited sensitivity to hygromycin B and tylosin antibiotics. The tylosin-sensitive phenotype was correlated with decreased transcriptional levels of tufA, tufB, and tsf, which encode elongation factors. Additionally, the ksgA mutant showed resistance to kasugamycin. Collectively, these findings highlight the role of KsgA in oxidative stress responses and antibiotic sensitivity in P. aeruginosa.

Kasugamycin

Drug Resistance Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Lactobacillus casei infection [ICD-11: 1A00-1C4Z] [1]

• Resistant Disease: Lactobacillus casei infection [ICD-11: 1A00-1C4Z]
• Resistant Drug: Kasugamycin
• Molecule Alteration: Missense mutation; A1518/1519
• Experimental Note: Revealed Based on the Cell Line Data
• In Vitro Model: Pseudomonas aeruginosa strain UCBPP-PA14; 1763
• Experiment for Molecule Alteration: Primer extension analysis; MS analysis; Western blot assay; Semiquantitative RT-PCR
• Experiment for Drug Resistance: Phenotypic microarrays assay; MIC assay; Oxidative stress sensitivity testing; Superoxide dismutase enzyme activity assay
• Mechanism Description: In this study, we demonstrated the absence of A1518/1519 methylation in the 16S rRNA of a Pseudomonas aeruginosa ksgA mutant. Biolog phenotypic microarrays were used to screen the phenotypes of the ksgA mutant against various antimicrobial agents. The loss of ksgA led to increased sensitivity to menadione, a superoxide generator, which was, at least in part, attributed to decreased in a superoxide dismutase (SOD) activity. Interestingly, the decrease in SOD activity in the ksgA mutant was linked to a decrease in the SodM protein levels, but not the sodM mRNA levels. Furthermore, the ksgA mutant strain exhibited sensitivity to hygromycin B and tylosin antibiotics. The tylosin-sensitive phenotype was correlated with decreased transcriptional levels of tufA, tufB, and tsf, which encode elongation factors. Additionally, the ksgA mutant showed resistance to kasugamycin. Collectively, these findings highlight the role of KsgA in oxidative stress responses and antibiotic sensitivity in P. aeruginosa.

Macrolides

Drug Sensitivity Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Lactobacillus casei infection [ICD-11: 1A00-1C4Z] [1]

• Sensitive Disease: Lactobacillus casei infection [ICD-11: 1A00-1C4Z]
• Sensitive Drug: Macrolides
• Molecule Alteration: Missense mutation; A1518/1519
• Experimental Note: Revealed Based on the Cell Line Data
• In Vitro Model: Pseudomonas aeruginosa strain UCBPP-PA14; 1763
• Experiment for Molecule Alteration: Primer extension analysis; MS analysis; Western blot assay; Semiquantitative RT-PCR
• Experiment for Drug Resistance: Phenotypic microarrays assay; MIC assay; Oxidative stress sensitivity testing; Superoxide dismutase enzyme activity assay
• Mechanism Description: In this study, we demonstrated the absence of A1518/1519 methylation in the 16S rRNA of a Pseudomonas aeruginosa ksgA mutant. Biolog phenotypic microarrays were used to screen the phenotypes of the ksgA mutant against various antimicrobial agents. The loss of ksgA led to increased sensitivity to menadione, a superoxide generator, which was, at least in part, attributed to decreased in a superoxide dismutase (SOD) activity. Interestingly, the decrease in SOD activity in the ksgA mutant was linked to a decrease in the SodM protein levels, but not the sodM mRNA levels. Furthermore, the ksgA mutant strain exhibited sensitivity to hygromycin B and tylosin antibiotics. The tylosin-sensitive phenotype was correlated with decreased transcriptional levels of tufA, tufB, and tsf, which encode elongation factors. Additionally, the ksgA mutant showed resistance to kasugamycin. Collectively, these findings highlight the role of KsgA in oxidative stress responses and antibiotic sensitivity in P. aeruginosa.

References

• Ref 1: 16S rRNA methyltransferase KsgA contributes to oxidative stress and antibiotic resistance in Pseudomonas aeruginosa. Sci Rep. 2024 Nov 3;14(1):26484.