Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
glycopeptide resistance
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| vanC2 | Reslit | 7 | vancomycin | Enterococcus gallinarum +9 | Belgium, France, Germany, South Western Nigeria, Brazil, Northern Italy | 1998, 1999, 2000, 2006, 2016, 2020, 2024 | SAL_QB2921AA | - |
| VanC2 | Reslit | 2 | vancomycin | Enterococcus casseliflavus +1 | - | 1997, 1998 | L29638 | - |
Comparison of direct plating and broth enrichment culture for the detection of intestinal colonization by glycopeptide-resistant enterococci among hospitalized patients.
The study identified the presence of glycopeptide-resistant enterococci (GRE) in hospitalized patients, highlighting the importance of broth enrichment culture for better detection. The vanA gene was found in E. faecium and E. faecalis, while vanC1 and vanC2 were found in E. gallinarum and E. casseliflavus, respectively.
Prevalence of Vancomycin-Resistant Enterococci in Fecal Samples from Hospitalized Patients and Nonhospitalized Controls in a Cattle-Rearing Area of France.
The study identified vanA, vanC1, and vanC2 genes as responsible for vancomycin resistance in enterococci isolated from hospitalized patients and nonhospitalized individuals in a cattle-rearing area of France.
Validation of VITEK 2 version 4.01 software for detection, identification, and classification of glycopeptide-resistant enterococci.
The study validated the VITEK 2 version 4.01 software for detecting, identifying, and classifying glycopeptide-resistant enterococci, including the accurate detection of vanA, vanB, vanC1, and vanC2 genotypes.
SURVEILLANCE FOR VANCOMYCIN RESISTANT ENTEROCOCCI IN A TERTIARY INSTITUTION IN SOUTH WESTERN NIGERIA.
The study identified vanA, vanB, vanC1, and vanC2 genes in Vancomycin-resistant Enterococcus isolates, highlighting the presence of glycopeptide resistance mechanisms in a Nigerian tertiary hospital.
Safety profiles of beneficial lactic acid bacteria isolated from dairy systems.
The study identified several AMR genes in lactic acid bacteria isolated from dairy systems, including vanC2, vanA, ermB, aac(6′)-Ie-aph(2″)-Ia, tet(S), ant(4′)-Ia, tdc, cpd, int, mur-2ed, asa1, ccf, and hyl. These genes conferred resistance to various antibiotics such as vancomycin, gentamicin, tetracycline, and chloramphenicol.
Wild Birds as Drivers of Salmonella Braenderup and Multidrug Resistant Bacteria in Wetlands of Northern Italy.
The study identifies several AMR genes in bacterial isolates from wild aquatic birds in Northern Italy, including beta-lactamases (blaTEM, blaCMY-1, blaCMY-2, blaNDM, blaKPC), colistin resistance genes (mcr-2, mcr-3, mcr-4), tetracycline resistance genes (tetA, tetB, tetC, tetL, tetM, tetK), macrolide resistance genes (ermB, vatD, vgA, msrC), vancomycin resistance genes (vanC1, vanC2, vanM, vanG), sulfonamide resistance genes (sul1, sul2, sul3), aminoglycoside resistance genes (aac(3), aac(6')-Ib, aph(3')-Ia, armA, rmtB, rmtC, rmtF), and nitrofurantoin resistance genes (nfsA, nfsB).
Bacterial resistance to vancomycin: Overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a d-Ala-d-Ser ligase.
The study characterizes VanC2 from Enterococcus casseliflavus as a d-Ala-d-Ser ligase, which contributes to vancomycin resistance by modifying peptidoglycan precursors.
Active-site mutants of the VanC2 D-alanyl-D-serine ligase, characteristic of one vancomycin-resistant bacterial phenotype, revert towards wild-type D-alanyl-D-alanine ligases.
Mutations in the VanC2 D-alanyl-D-serine ligase, such as Arg322Met, Phe250Tyr, and Leu282Arg, alter its specificity for D-amino acids, leading to changes in vancomycin resistance.
Active-site mutants of the VanC2 D-alanyl-D-serine ligase, characteristic of one vancomycin-resistant bacterial phenotype, revert towards wild-type D-alanyl-D-alanine ligases.
Mutations in the VanC2 D-alanyl-D-serine ligase, such as Arg322Met, Phe250Tyr, and Leu282Arg, alter its specificity for D-amino acids, leading to changes in vancomycin resistance.
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