Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
penicillin-binding protein 2A
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| E63K | - | reduced penicillin susceptibility | Streptococcus agalactiae | penicillin | Reslit | Candidate |
| K336G | - | - | Enterococcus faecalis | vancomycin | Reslit | Candidate |
| E150K | - | altered allosteric communication | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| N146K | - | - | Staphylococcus aureus | ceftarolineceftobiprole|ceftaroline | Reslit | Candidate |
| E239R | - | - | Staphylococcus aureus | cefoxitin | Reslit | Candidate |
| T459A | - | - | Streptococcus mitis | cefotaxime | Reslit | Candidate |
| V541I | - | - | Streptococcus agalactiae | penicillin | Reslit | Candidate |
| A27T | - | - | Streptococcus agalactiae | penicillin | Reslit | Candidate |
| N741A | - | - | Streptococcus agalactiae | penicillin | Reslit | Candidate |
| V744A | - | - | Streptococcus agalactiae | penicillin | Reslit | Candidate |
| Y446N | - | resistance to ceftaroline | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| E239K | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| G246E | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| E447K | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| L357I | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| I563T | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| S649A | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| N104K | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| V117I | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| A228V | - | - | Staphylococcus aureus | ceftaroline | Reslit | Candidate |
| T584A | - | - | Streptococcus suis | penicillin|ampicillin | Reslit | Candidate |
| H588Y | - | - | Streptococcus suis | penicillin|ampicillin | Reslit | Candidate |
| E549Q | - | - | Streptococcus suis | ceftiofur | Reslit | Candidate |
| A568S | - | - | Streptococcus suis | ceftiofur | Reslit | Candidate |
| P601L | - | - | Streptococcus pyogenes | ampicillin|cefotaxime | Reslit | Candidate |
| D239L | - | - | - | ceftobiprole|ceftaroline | Reslit | Candidate |
| S225R | - | - | - | ceftobiprole|ceftaroline | Reslit | Candidate |
| 259ins | - | - | - | ceftobiprole|ceftaroline | Reslit | Candidate |
| G425S | - | Streptococcus pneumoniae | penicillin|cefotaxime | Reslit | Candidate | |
| D440N | - | Streptococcus pneumoniae | penicillin|cefotaxime | Reslit | Candidate |
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| pbp2A | Reslit | 3 | penicillin, cefotaxime +2 | Streptococcus pneumoniae +1 | Netherlands|USA|Thailand | 2005, 2017, 2024 | AY461842 | - |
| pbp2a | Reslit | 15 | penicillin, ceftaroline +9 | Streptococcus pneumoniae +4 | United States, Europe|Russia, Portugal|Antarctic|South Shetland Islands|North Adriatic Sea|Bohai Sea|Adriatic Sea|Pacific Ocean|Baltic Sea | 1998, 2014, 2016, 2020, 2021, 2022, 2023, 2025 | ERP001840|ERS225580|ERS179073|ERS225581|ERS225582|ERS179074|ERS225576|ERS225577|ERS225578|ERS225579|ERS179072 | - |
| PBP2a | Reslit | 6 | methicillin, penicillin +2 | Staphylococcus aureus +2 | North America|Eastern Europe, USA | 2017, 2020, 2021, 2023, 2024, 2025 | PRJNA589866 | - |
Altered PBP 2A and Its Role in the Development of Penicillin, Cefotaxime, and Ceftriaxone Resistance in a Clinical Isolate of Streptococcus pneumoniae.
The study identifies altered PBP 2A as a critical determinant of β-lactam resistance in Streptococcus pneumoniae, demonstrating that the replacement of altered PBP 2A with an unaltered version leads to decreased resistance to penicillin, cefotaxime, and ceftriaxone.
Genomic analyses of DNA transformation and penicillin resistance in Streptococcus pneumoniae clinical isolates.
The study identifies mosaic alleles of pbp2x, pbp2b, pbp1a, and pbp2a as critical contributors to penicillin resistance in Streptococcus pneumoniae through genomic transformation and sequencing.
Targeting Antibiotic Resistance.
The paper discusses the resistance mechanisms of oxazolidinones, highlighting the role of the cfr gene encoding a ribosomal methyltransferase that confers resistance to multiple antibiotics.
Synergistic antibacterial effects of herbal extracts and antibiotics on methicillin-resistant Staphylococcus aureus: A computational and experimental study.
The study identified several herbal constituents that show potential to inhibit PBP2a and PBP4, which are crucial for methicillin resistance in Staphylococcus aureus. These findings suggest that these compounds could enhance the efficacy of antibiotics against MRSA.
Deciphering the distance to antibiotic resistance for the pneumococcus using genome sequencing data.
The study identifies numerous genes and mutations associated with antibiotic resistance in Streptococcus pneumoniae through genome-wide association studies, highlighting the genetic basis of resistance to penicillin, trimethoprim, cotrimoxazole, erythromycin, and fluoroquinolones.
Expression Profiles and Mutational Analysis of Daptomycin-Nonsusceptible Staphylococcus aureus Strains
The study identifies genes and mutations associated with daptomycin nonsusceptibility in Staphylococcus aureus, highlighting the role of mprF, dltABCD, vraSR, walKR, and pbp2a in altering cell surface charge and resistance mechanisms.
Structural analysis of avibactam-mediated activation of the bla and mec divergons in methicillin-resistant Staphylococcus aureus.
Avibactam up-regulates the expression of blaZ and pbp2a in S. aureus SF8300, indicating its role in activating the bla and mec divergons.
Ribaxamase, an Orally Administered β-Lactamase, Diminishes Changes to Acquired Antimicrobial Resistance of the Gut Resistome in Patients Treated with Ceftriaxone.
The study identified several β-lactamase and vancomycin resistance genes that were significantly increased in placebo-treated patients compared to ribaxamase-treated patients following ceftriaxone exposure.
β-Lactams against the Fortress of the Gram-Positive Staphylococcus aureus Bacterium.
This review discusses the mechanisms of β-lactam resistance in Staphylococcus aureus, focusing on penicillin-binding proteins (PBPs) and their roles in peptidoglycan biosynthesis. It highlights the importance of PBP2, PBP1, PBP3, and PBP4 in resistance mechanisms and their interactions with β-lactam antibiotics.
Bacterial Targets of Antibiotics in Methicillin-Resistant Staphylococcus aureus.
The paper discusses the mechanisms of antibiotic resistance in methicillin-resistant Staphylococcus aureus (MRSA), focusing on genes such as blaZ, mecA, and dltA, which are involved in beta-lactam and glycopeptide resistance. It highlights the importance of understanding these resistance mechanisms to develop new therapeutic strategies.
Study on Demethoxycurcumin as a Promising Approach to Reverse Methicillin-Resistance of Staphylococcus aureus.
Demethoxycurcumin (DMC) inhibits the expression of PBP2a and beta-lactamase (blaZ), reversing methicillin-resistance in Staphylococcus aureus.
Impact of FtsZ Inhibition on the Localization of the Penicillin Binding Proteins in Methicillin-Resistant Staphylococcus aureus.
The study identifies PBP2a as a key factor in methicillin-resistant Staphylococcus aureus (MRSA) resistance to β-lactam antibiotics, showing that its localization and function are altered by FtsZ inhibition and combination therapy with oxacillin.
Non-β-Lactam Allosteric Inhibitors Target Methicillin-Resistant Staphylococcus aureus: An In Silico Drug Discovery Study.
The study identifies eMol26313223 and eMol26314565 as potent allosteric inhibitors of PBP2a in methicillin-resistant Staphylococcus aureus, demonstrating strong binding affinities and stability in molecular dynamics simulations.
WYBQ-4: a New Bactericidal Agent against Methicillin-Resistant Staphylococcus aureus.
WYBQ-4 is a new bactericidal agent with potent activity against methicillin-resistant Staphylococcus aureus (MRSA). It binds to penicillin-binding proteins (PBPs), including PBP1, PBP2, PBP3, PBP4, and PBP2a, and interferes with cell wall synthesis, leading to bacterial cell death.
In Silico Genome-Scale Analysis of Molecular Mechanisms Contributing to the Development of a Persistent Infection with Methicillin-Resistant Staphylococcus aureus (MRSA) ST239.
The study identified specific amino acid substitutions in PBP2 and PBP2a that confer resistance to ceftaroline in the MRSA ST239 strain SA943.
Molluscs-A ticking microbial bomb.
The paper discusses the presence of antibiotic resistance genes (ARGs) in bivalve molluscs, highlighting the spread of resistance to various antibiotics such as colistin, beta-lactams, fluoroquinolones, and tetracyclines. It emphasizes the role of bivalve aquacultures in the dissemination of ARGs and the potential risks to human health through the food chain.
Prevalence of multidrug-resistant coagulase-positive staphylococci in canine and feline dermatological patients over a 10-year period: a retrospective study.
The study found a high prevalence of multidrug-resistant (MDR) coagulase-positive staphylococci in canine and feline dermatological patients, with a significant increase in oxacillin resistance over the 10-year period. Methicillin resistance was primarily associated with the presence of PBP2a and OXA resistance.
Proteomic assay for rapid characterisation of Staphylococcus aureus antimicrobial resistance mechanisms directly from blood cultures.
The study presents a rapid proteomic method using LC-MS/MS to detect and quantify key antimicrobial resistance effectors in Staphylococcus aureus directly from blood cultures, achieving high agreement rates for PBP2a, PBP2c, APH(3')-III, ANT(4')-I, and AAC(6')-APH(2'').
Arginine impacts aggregation, biofilm formation, and antibiotic susceptibility in Enterococcus faecalis.
Arginine metabolism in Enterococcus faecalis leads to increased aggregation, decreased biofilm formation, and altered antibiotic susceptibility, particularly to ampicillin and ceftriaxone.
Surface Loading Proximity Ligation-Induced PCR Technique for Fluorescent Detection of Intact Methicillin-Resistant Staphylococcus aureus.
The study focuses on developing a novel method for detecting MRSA by targeting PBP2a, a protein responsible for drug resistance in MRSA. The method uses a surface loading proximity ligation assay combined with PCR for sensitive detection.
Dynamic Profiling of Penicillin-Binding Protein 2a (PBP2a)-Positive Extracellular Vesicles: Implications for Early Diagnosis and Treatment Monitoring of Methicillin-Resistant Staphylococcus Aureus Infections.
The study identifies PBP2a as a consistent component of MRS-derived EVs and shows that PBP2a+ EVs can serve as a biomarker for MRSA infections, with elevated levels correlating with infection progression and inflammatory markers.
PanARGMiner (Pan-Genomic Antimicrobial Resistance Gene Miner): An advanced feature selection framework for extracting key resistance genes from pan-genomic datasets.
PanARGMiner effectively identifies key resistance genes from pan-genomic datasets, including both known and novel AMR genes, across multiple bacterial species.
Molecular resistance mechanisms to newly approved antibiotics (2017-2025) in WHO priority pathogens.
The paper reviews molecular resistance mechanisms to newly approved antibiotics in WHO priority pathogens, identifying various beta-lactamases, efflux pumps, and target site modifications that confer resistance.
Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae.
The study demonstrates the acquisition of five high-Mr penicillin-binding protein (PBPs) variants (PBP2x, PBP2a, PBP2b, PBP1a, and PBP1b) during the transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae. These PBPs confer resistance to cefotaxime, oxacillin, and benzylpenicillin.
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