Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.

PMID: 355625462022

Key Findings

The study identifies D27E and L28Q substitutions in DfrA1 and DfrA5 as key determinants of trimethoprim resistance, revealing a common mechanism of resistance in plasmid-encoded dihydrofolate reductases.

View on PubMed

2gene entries

4mutation entries

AMR Genes

Gene Name	Alleles	Encodes	Confers Resistance To	Organisms	Database	Validation Status
dfrA1	1	dihydrofolate reductase	Trimethoprim	Escherichia coli	Reslit	-
dfrA5	1	dihydrofolate reductase	Trimethoprim	Escherichia coli	Reslit	-

AMR Mutations

Gene	Protein Change	Nucleotide Change	Mechanism	Organism	Resistance To	Database	Validation Status
dfrA5	D27E	-	-	-	Trimethoprim	Reslit	-
dfrA1	D27E	-	increased ligand dissociation rates while maintaining the enzyme’s ability to turnover substrate	Salmonella enterica, Escherichia coli	Trimethoprim	Reslit	-
dfrA5	L28Q	-	-	-	Trimethoprim	Reslit

Browse Papers

Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.

AMR Genes

AMR Mutations