Cargando…

Antimicrobial Peptides Designed against the Ω-Loop of Class A β-Lactamases to Potentiate the Efficacy of β-Lactam Antibiotics

Class A serine β-lactamases (SBLs) have a conserved non-active site structural domain called the omega loop (Ω-loop), in which a glutamic acid residue is believed to be directly involved in the hydrolysis of β-lactam antibiotics by providing a water molecule during catalysis. We aimed to design and...

Descripción completa

Detalles Bibliográficos
Autores principales:	Biswal, Sarmistha, Caetano, Karina, Jain, Diamond, Sarrila, Anusha, Munshi, Tulika, Dickman, Rachael, Tabor, Alethea B., Rath, Surya Narayan, Bhakta, Sanjib, Ghosh, Anindya S.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2023
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10044640/ https://www.ncbi.nlm.nih.gov/pubmed/36978420 http://dx.doi.org/10.3390/antibiotics12030553

Ejemplares similares

Pharmacokinetics of Non-β-Lactam β-Lactamase Inhibitors
por: Luci, Giacomo, et al.
Publicado: (2021)

Role of AmpC-Inducing Genes in Modulating Other Serine Beta-Lactamases in Escherichia coli
por: Mallik, Dhriti, et al.
Publicado: (2022)

BADAN-conjugated β-lactamases as biosensors for β-lactam antibiotic detection
por: Au, Ho-Wah, et al.
Publicado: (2020)

Cryptic β-Lactamase Evolution Is Driven by Low β-Lactam Concentrations
por: Fröhlich, Christopher, et al.
Publicado: (2021)

Penicillin-Binding Proteins, β-Lactamases, and β-Lactamase Inhibitors in β-Lactam-Producing Actinobacteria: Self-Resistance Mechanisms
por: Martin, Juan F., et al.
Publicado: (2022)

Characterization of the MurT/GatD complex in Mycobacterium tuberculosis towards validating a novel anti-tubercular drug target
por: Maitra, Arundhati, et al.
Publicado: (2021)

The Role of Colistin in the Era of New β-Lactam/β-Lactamase Inhibitor Combinations
por: Aslan, Abdullah Tarık, et al.
Publicado: (2022)

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
por: Wilamowski, M., et al.
Publicado: (2022)

Synthesis and biological evaluation of novel β-lactam-metallo β-lactamase inhibitors
por: Shungube, Mbongeni, et al.
Publicado: (2023)

The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases
por: Egorov, Alexey, et al.
Publicado: (2019)

The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics
por: Kim, Si Won, et al.
Publicado: (2020)

Novel β-Lactam/β-Lactamase Combination Versus Meropenem for Treating Nosocomial Pneumonia
por: Lin, Wei-Ting, et al.
Publicado: (2019)

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
por: Lomovskaya, Olga, et al.
Publicado: (2023)

Chemiluminescence Detection of Hydrogen Sulfide Release by β-Lactamase-Catalyzed β-Lactam Biodegradation: Unprecedented Pathway for Monitoring β-Lactam Antibiotic Bacterial Resistance
por: Gholap, Sachin Popat, et al.
Publicado: (2021)

Structural Variabilities in β-Lactamase (blaA) of Different Biovars of Yersinia enterocolitica: Implications for β-Lactam Antibiotic and β-Lactamase Inhibitor Susceptibilities
por: Singhal, Neelja, et al.
Publicado: (2015)

Editorial for the Special Issue: “Targeting β-Lactamases to Fight Bacterial Resistance to β-Lactam Antibiotics”
por: Pozzi, Cecilia
Publicado: (2020)

Quantitative Insights Into β-Lactamase Inhibitor’s Contribution in the Treatment of Carbapenemase-Producing Organisms With β-Lactams
por: Feng, Yanfang, et al.
Publicado: (2021)

β-Lactam Antibiotics and β-Lactamase Enzymes Inhibitors, Part 2: Our Limited Resources
por: Alfei, Silvana, et al.
Publicado: (2022)

Management of clinical infections of Escherichia coli by new β-lactam/β-lactamase inhibitor combinations
por: Kadry, Ashraf Ahmed, et al.
Publicado: (2022)

Meropenem/Vaborbactam: β-Lactam/β-Lactamase Inhibitor Combination, the Future in Eradicating Multidrug Resistance
por: Duda-Madej, Anna, et al.
Publicado: (2023)

In Vitro Activity of β-Lactams in Combination with β-Lactamase Inhibitors against Mycobacterium tuberculosis Clinical Isolates
por: Li, Fu, et al.
Publicado: (2018)

Induction of β-Lactamase Activity and Decreased β-Lactam Susceptibility by CO(2) in Clinical Bacterial Isolates
por: Mullen, Nathan, et al.
Publicado: (2017)

Antibiofilm Activity of β-Lactam/β-Lactamase Inhibitor Combination against Multidrug-Resistant Salmonella Typhimurium
por: Laure, Nana Nguefang, et al.
Publicado: (2022)

1230. Evaluation of the Interplay Between β-lactamases and Porin Production on β-Lactam MICs in Klebsiella pneumoniae
por: Whitney, Alyssa K, et al.
Publicado: (2021)

Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors
por: Reddy, Nakita, et al.
Publicado: (2023)

In vitro activity of new combinations of β-lactam and β-lactamase inhibitors against the Mycobacterium tuberculosis complex
por: Economou Lundeberg, Elin, et al.
Publicado: (2023)

Examining the Clinical Effectiveness of Non-Carbapenem β-Lactams for the Treatment of Extended-Spectrum β-Lactamase-Producing Enterobacteriaceae
por: Gibble, Allison M., et al.
Publicado: (2015)

Method Based on the β-Lactamase PenPC Fluorescent Labeled for β-Lactam Antibiotic Quantification in Human Plasma
por: Andresen, Max, et al.
Publicado: (2016)

Effect of β-Lactamase inhibitors on in vitro activity of β-Lactam antibiotics against Burkholderia cepacia complex species
por: Everaert, Annelien, et al.
Publicado: (2016)

Transcriptional and post-transcriptional regulation of PenA β-lactamase in acquired Burkholderia pseudomallei β-lactam resistance
por: Chirakul, Sunisa, et al.
Publicado: (2018)

Non‐Hydrolytic β‐Lactam Antibiotic Fragmentation by l,d‐Transpeptidases and Serine β‐Lactamase Cysteine Variants
por: Lohans, Christopher T., et al.
Publicado: (2019)

Thermostable β-Lactamase Mutant with Its Active Site Conjugated with Fluorescein for Efficient β-Lactam Antibiotic Detection
por: Au, Ho-Wah, et al.
Publicado: (2019)

In Vivo Secretion of β-Lactamase-Carrying Outer Membrane Vesicles as a Mechanism of β-Lactam Therapy Failure
por: Bielaszewska, Martina, et al.
Publicado: (2021)

In Vitro and In Vivo Development of a β-Lactam-Metallo-β-Lactamase Inhibitor: Targeting Carbapenem-Resistant Enterobacterales
por: Peters, Byron K., et al.
Publicado: (2023)

Penicillin-Binding Protein Occupancy Dataset for 18 β-Lactams and 4 β-Lactamase Inhibitors in Neisseria gonorrhoeae
por: López-Argüello, Silvia, et al.
Publicado: (2023)

600. β-Lactam Resistance Mechanisms in Pseudomonas aeruginosa Isolates Analyzed Using Whole-Genome Sequencing (WGS) and Transcriptions Analysis and Their Impact in Resistance to New β-Lactam/β-Lactamase Inhibitors
por: Castanheira, Mariana, et al.
Publicado: (2019)

Induction of plasmid-mediated AmpC β-lactamase DHA-1 by piperacillin/tazobactam and other β-lactams in Enterobacteriaceae
por: Akata, Kentaro, et al.
Publicado: (2019)

Theaflavin‐3,3´‐digallate increases the antibacterial activity of β‐lactam antibiotics by inhibiting metallo‐β‐lactamase activity
por: Teng, Zihao, et al.
Publicado: (2019)

1299. In Vitro-In Vivo Discordance with β-lactams against Metallo-β-lactamase-Producing Enterobacterales: Implications for Susceptibility Testing
por: Abdelraouf, Kamilia, et al.
Publicado: (2020)

In Vitro and In Vivo Evaluations of β-Lactam/β-Lactamase Mono- and Combined Therapies against Carbapenem-Nonsusceptible Enterobacteriaceae in Taiwan
por: Yang, Tsung-Ying, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_566t749a4c3mltdavj5ppdp4sg