The paper discusses the molecular mechanisms of drug resistance in Mycobacterium tuberculosis, focusing on genes like pncA, rspA, erm37, tlyA, eis, BlaC, mfpA, IniBAC, EfP, and Tap, which are involved in resistance to pyrazinamide, macrolides, lincosamides, capreomycin, viomycin, kanamycin, β-lactams, fluoroquinolones, isoniazid, ethambutol, and multiple antibiotics.

The study characterizes the beta-lactamase BlaC from Mycobacterium tuberculosis, demonstrating its ability to hydrolyze various β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems.

The study identified the I105F mutation in BlaC, a beta-lactamase from Mycobacterium tuberculosis, which enhances ampicillin resistance in E. coli and M. smegmatis. The mutation increases catalytic efficiency and stability of the enzyme.

Substitutions in the Mycobacterium tuberculosis beta-lactamase BlaC, particularly R220A, R220S, A244R, S130G, T237A, and T237S, were found to reduce the effectiveness of clavulanate, although the wild-type BlaC remains susceptible to ampicillin-clavulanate.

The study describes a computational method for discovering covalent chemical probes that target specific protein residues, including beta-lactamase inhibitors and kinase inhibitors. Experimental validation confirmed the effectiveness of these inhibitors against AmpC beta-lactamase and RSK2/MSK1 kinases.

Penem 2 was identified as a highly effective inhibitor of the beta-lactamase BlaC from Mycobacterium tuberculosis, demonstrating potent inhibition of the enzyme and significant growth inhibition of the bacteria.

The study identified that 2-aminoimidazole compounds enhance the effectiveness of β-lactam antibiotics against Mycobacterium tuberculosis by reducing β-lactamase secretion and increasing cell envelope permeability. The β-lactamase gene blaC was found to contribute to intrinsic resistance.

The study characterizes the beta-lactamase BlaC from Mycobacterium tuberculosis, demonstrating its ability to hydrolyze clavulanic acid and recover activity in the presence of phosphate ions. Phosphate enhances the hydrolysis of clavulanic acid by BlaC, promoting the recovery of enzyme activity.

The study reports the identification of bifunctional Class C-Class D beta-lactamases in environmental bacteria, highlighting their potential for broad-spectrum β-lactam resistance and suggesting possible horizontal gene transfer to clinically relevant bacteria.

The study characterizes the beta-lactamase BlaC from Mycobacterium tuberculosis, which confers resistance to cephalosporins by catalyzing the cleavage of the β-lactam ring in antibiotics like ceftriaxone.

The study describes a dual-targeting fluorogenic probe (CDG-DNB3) that labels live Mycobacterium tuberculosis specifically by exploiting the activities of BlaC and DprE1 enzymes. BlaC, a beta-lactamase, activates the probe, while DprE1 retains the fluorescent product through covalent modification.

The study identifies BlaC, a beta-lactamase from Mycobacterium tuberculosis, as a specific biomarker for detecting viable bacteria in clinical samples. BlaC is highly conserved among tuberculosis complex members and exhibits unique structural features that distinguish it from other beta-lactamases.

The study characterizes the dynamics of the beta-lactamase BlaC from Mycobacterium tuberculosis, showing that it exhibits flexibility on the millisecond timescale in the active site, which increases upon inhibitor binding.

Zidebactam (ZID) exhibits enhanced potency against AmpC EC compared to other DBOs due to faster carbamoylation and decarbamoylation rates, making it a more effective inhibitor of AmpC beta-lactamase.

The study identifies halisulfates 3 and 5 as potent inhibitors of AmpC BER, an extended-spectrum class C beta-lactamase, demonstrating their broad-spectrum inhibition activity against various beta-lactamases.

The study reveals that the Ω-loop pocket in beta-lactamase influences penicillin hydrolysis. Mutations affecting the Ω-loop pocket dynamics correlate with changes in benzylpenicillin activity, highlighting the functional relevance of this cryptic pocket.

The study characterizes the beta-lactamase BlaC from Mycobacterium tuberculosis, focusing on its interaction with ceftriaxone (CEF) and sulbactam (SUB).

The study identifies several genes and mutations associated with beta-lactam susceptibility in Mycobacterium tuberculosis, highlighting the role of specific genetic variations in influencing resistance patterns.

The study identified that the Acinetobacter baumannii strain ST1 retained its drug-resistant phenotype after spaceflight, with genes related to resistance to beta-lactams, cephalosporin, fluoroquinolone, macrolide, aminoglycosides, and tetracycline.

The study identifies key structural and dynamic factors influencing carbapenemase activity in class A beta-lactamases through QM/MM simulations, highlighting the roles of the 6α-1R-hydroxyethyl group, Asn132, and the disulfide bridge in determining carbapenem hydrolysis efficiency.

The study identified multiple AMR genes in lichen-associated bacteria, including beta-lactamases, efflux pump components, and enzymes conferring resistance to various antibiotics. These findings highlight the diverse AMR profiles of bacteria inhabiting extreme environments.

The paper discusses intrinsic and acquired drug resistance mechanisms in Mycobacterium tuberculosis, highlighting beta-lactamases (blaA, blaC, blaE), erm gene-mediated macrolide/lincosamide/streptogramin B resistance, mfpA-mediated fluoroquinolone/viomycin/capreomycin resistance, and the role of the Eis protein in aminoglycoside resistance. It also identifies mutations in rpoB and gyrA associated with rifampicin and fluoroquinolone resistance.

The study identifies the blaC gene encoding a beta-lactamase in Mycobacterium tuberculosis that reduces sensitivity to ampicillin/avibactam in a zebrafish-Mycobacterium marinum model. A specific mutation, K234R, was shown to further reduce sensitivity to these antibiotics.

The study characterizes the structural and functional effects of BlaC mutations P226G and P107T, demonstrating their role in beta-lactam resistance.

The study identifies and characterizes beta-lactamase homologous proteins in gram-negative bacteria of the ESKAPEE group, highlighting their potential role in resistance to beta-lactam antibiotics.

The study identifies the Ent385 AmpC beta-lactamase as a key player in enhanced ceftazidime hydrolysis, revealing that Tyr150 acts as a base in the deacylation process, facilitating efficient antibiotic degradation.

PanARGMiner effectively identifies key resistance genes from pan-genomic datasets, including both known and novel AMR genes, across multiple bacterial species.