Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
L1 family subclass B3 metallo-beta-lactamase
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| blaL1 | Card DatabaseReference Gene CatalogResFinder DatabaseReslit | 43 | CARBAPENEM, UNKNOWN BETA-LACTAM +14 | Stenotrophomonas maltophilia +4 | Hong Kong, Los Angeles|Southern California, Southern California, Europe, Brazil|India|Sweden|USA|Argentina|Italy|Japan, United Kingdom, Alberta, Canada, Global, Australia|South Australia, Japan, Lithuania, Lebanon | 1994, 1998, 2001, 2002, 2008, 2009, 2018, 2019, 2020, 2021, 2022, 2023, 2024, 2025 | AB294542.1 | BAF47404.1 |
| blaL1-like | Reslit | 2 | imipenem, meropenem +1 | Stenotrophomonas maltophilia +2 | Argentina | 2005, 2024 | NZ_BRFG00000000|NZ_BRFG01000003 | - |
| blaL1-1 | Reslit | 1 | imipenem | Escherichia coli MC1000 | Europe | 2022 | NCBI:WP_011401325.1|NCBI:WP_011401326.1|NCBI:WP_011401327.1|NCBI:WP_011401328.1|NCBI:WP_011401329.1 | - |
Plasmid location and molecular heterogeneity of the L1 and L2 beta-lactamase genes of Stenotrophomonas maltophilia.
Plasmid location and molecular heterogeneity of the L1 and L2 beta-lactamase genes of Stenotrophomonas maltophilia.
Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis.
The study characterized the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia and investigated the role of specific amino acid residues in substrate binding and catalysis through site-directed mutagenesis and kinetic analysis.
Sensitive EDTA-Based Microbiological Assays for Detection of Metallo-β-Lactamases in Nonfermentative Gram-Negative Bacteria.
The study describes the development of a sensitive microbiological assay (EIM) for detecting metallo-β-lactamases (MBLs) in nonfermentative gram-negative bacteria. It identifies several MBL genes, including bla VIM-11a, bla IMP-7, bla SPM-1, bla L1-like, bla GOB-like, bla IND-like, and bla BcII, which confer resistance to carbapenems.
Induction of L1 and L2 beta-lactamases of Stenotrophomonas maltophilia.
Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols.
Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols.
Sec- and Tat-Dependent Translocation of beta-Lactamases across the Escherichia coli Inner Membrane
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Modified nitrocefin-EDTA method to differentially quantify the induced L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.
Comprehensive Evaluation of the MBT STAR-BL Module for Simultaneous Bacterial Identification and beta-lactamase-Mediated Resistance Detection in Gram-Negative Rods from Cultured Isolates and Positive Blood Cultures.
The study evaluated the MBT STAR-BL module for detecting beta-lactamase-mediated resistance in Gram-negative rods from cultured isolates and blood cultures. It identified several beta-lactamase genes, including blaTEM-1b, blaCTX-M-13, blaCTX-M-14, blaNDM-5, blaKPC-2, blaCMY-2, blaOXA-23, blaOXA-51, blaVIM-4, blaPOM-1, and blaL1, which confer resistance to various β-lactam antibiotics.
Prevalence and characterization of carbapenem-resistant bacteria in water bodies in the Los Angeles-Southern California area.
The study identified bla_IMI-2 and bla_L1 as carbapenemase genes in carbapenem-resistant bacteria from water bodies in the Los Angeles area, highlighting the presence of these resistance mechanisms in environmental samples.
Structural and biochemical analysis of the metallo-beta-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.
The study characterizes the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia, revealing its di-metal scaffold and catalytic activity towards various β-lactam antibiotics.
Urban and agricultural soils in Southern California are a reservoir of carbapenem-resistant bacteria.
The study identifies blaL1 as a carbapenemase gene in Stenotrophomonas maltophilia isolates, highlighting the presence of carbapenem-resistant bacteria in urban and agricultural soils of Southern California.
Inhibitory Potential of Polyclonal Camel Antibodies against New Delhi Metallo-β-lactamase-1 (NDM-1).
Polyclonal camel antibodies (IgG1, IgG2, and IgG3) were shown to inhibit the activity of NDM-1, VIM-1, and L1 metallo-beta-lactamases, which are responsible for resistance to carbapenems.
Faropenem reacts with serine and metallo-beta-lactamases to give multiple products.
The study characterizes the reactions of faropenem with beta-lactamases, including KPC-2, VIM-2, and L1, revealing distinct product formations and highlighting the importance of enzyme-specific interactions in determining the fate of faropenem.
Metallo-beta-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
This review discusses the role of metallo-beta-lactamases (MBLs) in multidrug resistance, focusing on their structure, mechanism, and contribution to resistance against β-lactam antibiotics. It highlights the importance of MBLs in the spread of resistance and the challenges they pose for inhibitor design.
Inter-species interactions alter antibiotic efficacy in bacterial communities.
The study identifies the metallo-beta-lactamase blaL1 in Stenotrophomonas maltophilia K279a as responsible for imipenem detoxification, providing exposure protection to Pseudomonas aeruginosa PAO1. This resistance mechanism is dependent on the density of S. maltophilia and the inactivation rate of the antibiotic.
Breaking antimicrobial resistance by disrupting extracytoplasmic protein folding.
Disruption of DsbA-mediated disulfide bond formation incapacitates diverse β-lactamases and destabilizes mobile colistin resistance enzymes. Chemical inhibition of DsbA sensitizes multidrug-resistant clinical isolates to existing antibiotics.
Identification of diverse antibiotic resistant bacteria in agricultural soil with H(2)(18)O stable isotope probing combined with high-throughput sequencing.
The study identified several antimicrobial resistance genes (ARGs) in agricultural soil using H2 18O stable isotope probing combined with high-throughput sequencing. These included aph(3')-IIc, oqxB, blaTEM-181, blaL1, and dfrB3, which conferred resistance to various antibiotics such as aminoglycosides, chloramphenicol, quinolones, trimethoprim, and beta-lactams.
Genomic Characterization of Carbapenem-Resistant Bacteria from Beef Cattle Feedlots.
The study identified several intrinsic carbapenem resistance genes, including blaOXA-50, blaOXA-265, blaOXA-648, blaOXA-278, blaL1, blaL2, and blaPST-2, in carbapenem-resistant bacteria from beef cattle feedlots.
Abundance and prevalence of ESBL coding genes in patients undergoing first line eradication therapy for Helicobacter pylori.
The study identified several ESBL coding genes, including bla OXY, bla ADC, bla IMP, bla OXA, bla L1, bla LRA, bla EC, bla ACI, and bla FAR, which were found to be prevalent in patients undergoing H. pylori eradication therapy. The abundance of these genes varied between pre- and post-eradication states.
In vitro potency of xeruborbactam in combination with multiple β-lactam antibiotics in comparison with other β-lactam/β-lactamase inhibitor (BLI) combinations against carbapenem-resistant and extended-spectrum β-lactamase-producing Enterobacterales.
Xeruborbactam (XER) showed superior in vitro potency against carbapenem-resistant and extended-spectrum β-lactamase-producing Enterobacterales when combined with various β-lactam antibiotics compared to other β-lactam/β-lactamase inhibitor combinations. XER effectively inhibited a wide range of β-lactamases, including metallo-β-lactamases (MBLs) and serine β-lactamases, enhancing the activity of antibiotics such as meropenem, cefepime, ceftolozane, ceftriaxone, aztreonam, piperacillin, and ertapenem.
Biochemical characterization of the L1-like metallo-β-lactamase from Stenotrophomonas lactitubi.
The study characterized the L1-like metallo-β-lactamase from Stenotrophomonas lactitubi, demonstrating its high hydrolyzing efficiency for ampicillin and nitrocefin, and its resistance to DPA inhibition.
Multidrug-resistant Stenotrophomonas maltophilia in residential aged care facilities: An emerging threat.
The study identifies blaL1 and blaL2 beta-lactamase genes, eptA1 and eptA2 phosphoethanolamine transferases, and other resistance mechanisms in multidrug-resistant Stenotrophomonas maltophilia isolates from residential aged care facilities.
Clinical characteristics and genome epidemiology of Stenotrophomonas maltophilia in Japan.
The study identified several antimicrobial resistance genes in Stenotrophomonas maltophilia, including aac(6')-Iak, aph(3')-IIc, aph(6), bla L1, and bla L2, which contribute to resistance against various antibiotics such as trimethoprim/sulfamethoxazole, minocycline, levofloxacin, and ceftazidime.
Stenotrophomonas maltophilia of clinical origin display higher temperature tolerance comparing with environmental isolates.
The study identifies several AMR genes in clinical and environmental Stenotrophomonas maltophilia isolates, including beta-lactamases (bla L1, bla L2), aminoglycoside resistance genes (aph(9), aph(3), aph(6)), and a quinolone resistance gene (smqnr). Clinical isolates showed higher prevalence of these genes compared to environmental isolates.
Comprehensive screening of potential inhibitors from ZINC15 database for Metallo-L1 Β -Lactamase from Stenotrophomonas maltophilia via in Silico and in vitro approaches.
The study identified ZINC393032 and ZINC616394 as potential inhibitors of the Metallo-L1 beta-lactamase from Stenotrophomonas maltophilia, demonstrating significant enzyme inhibition and synergy with imipenem.
Ceftazidime retains in vivo efficacy against strains of Stenotrophomonas maltophilia for which traditional testing predicts resistance.
The study shows that ceftazidime remains effective against certain strains of Stenotrophomonas maltophilia, even when traditional testing suggests resistance, due to the influence of metal cations on the activity of the L1 metallo-beta-lactamase.
Nationwide surveillance of carbapenem-resistant Gram-negative pathogens in the Lebanese environment.
The study identified carbapenem-resistant Gram-negative bacteria in various environmental samples in Lebanon, including Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, and Acinetobacter baumannii. Key resistance genes detected include bla NDM-5, bla OXA-23, bla OXA-66, mexAB-OprM, bla IMP-1, and others, highlighting the widespread presence of carbapenem resistance in the environment.
Genomic analysis of contaminant Stenotrophomonas maltophilia, from placental swab culture, carrying antibiotic resistance: a potential hospital laboratory contaminant.
The study identified six antibiotic resistance genes in Stenotrophomonas maltophilia RAOG732, including aac(6')-Iz, aac(6')-Ib7, aph(3')-IIc, oqxB, sul1, and blaL1, which conferred resistance to aminoglycosides, fluoroquinolones, folate synthesis inhibitors, and beta-lactams.
Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
The study describes the overexpression, purification, and characterization of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia, demonstrating its ability to hydrolyze various penicillins and cephalosporins.
Molecular heterogeneity of the L-1 metallo-beta-lactamase family from Stenotrophomonas maltophilia.
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