A5015244107- Antimicrobial Resistance in Staphylococcus
- Veterinary medicine and infectious diseases
- Research on Leishmaniasis Studies
- Trypanosoma species research and implications
- Biochemical and Molecular Research
- Biochemical and Structural Characterization
- Infective Endocarditis Diagnosis and Management
- Pharmacological Effects of Natural Compounds
- Antibiotic Resistance in Bacteria
- Bacterial Identification and Susceptibility Testing
- Microbial Natural Products and Biosynthesis
- Parasites and Host Interactions
- Streptococcal Infections and Treatments
- Mycobacterium research and diagnosis
- Monoclonal and Polyclonal Antibodies Research
- Pneumonia and Respiratory Infections
- Chronic Lymphocytic Leukemia Research
- Lymphoma Diagnosis and Treatment
University of Arizona
2018-2023
Universidade Federal do Rio de Janeiro
2016-2021
National Institute of Science and Technology for Structural Biology and Bioimaging
2020
The final steps of cell-wall biosynthesis in bacteria are carried out by penicillin-binding proteins (PBPs), whose transpeptidase domains form the cross-links peptidoglycan chains that define bacterial cell wall. These enzymes targets β-lactam antibiotics, as their inhibition reduces structural integrity Bacterial resistance to antibiotics is a rapidly growing concern; however, underpinnings PBP-derived antibiotic poorly understood. PBP4 and PBP5 low-affinity, class B transpeptidases confer...
Abstract Penicillin-binding proteins (PBPs) are essential for the formation of bacterial cell wall. They also targets β-lactam antibiotics. In Enterococcus faecium , high levels resistance to β-lactams associated with expression PBP5, higher distinct PBP5 variants. To define molecular mechanism PBP5-mediated we leveraged biomolecular NMR spectroscopy – due its size (>70 kDa) a challenging target. Our data show that resistant variants significantly increased dynamics either alone or upon...
Enterococcus faecalis strains resistant to penicillin and ampicillin are rare have been associated with increases in quantities of low-affinity penicillin-binding protein 4 (PBP4) or amino acid substitutions PBP4. We report an E. strain (LS4828) isolated from a prosthetic knee joint that was subjected long-term exposure aminopenicillins. Subsequent cultures yielded MICs penicillins carbapenems higher than those for wild-type JH2-2. Sequence analysis the pbp4 gene LS4828 compared JH2-2...