Beta-lactamase Inhibitors
Beta-lactamase Inhibitors - Related Videos
12:23
Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
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Cited by 5 •
2015
Effector translocation into host cells via a type III secretion system is a common virulence strategy among gram-negative bacteria. A beta-lactamase effector fusion based assay for quantitative analysis of translocation was applied. In Yersinia infected cells, conversion of a FRET reporter by the beta-lactamase is monitored using laser scanning microscopy.
08:06
The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
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Cited by 1 •
2018
In this work, we report a new method to study protein-protein interactions using a conductimetric biosensor based on the hybrid β-lactamase technology. This method relies on release of protons upon hydrolysis of β-lactams.
04:43
β-Lactamase-Based Conductimetric Biosensor Assay for Protein-Protein Interactions
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2025
This video demonstrates a conductimetric biosensor assay to study the interaction of an antibody with a target antigen immobilized on a transducer chip. The biosensor is engineered to have a bifunctional chimeric protein — a β-lactamase enzyme with a functional catalytic site fused to a nanobody for binding to the immobilized target antigen. Upon binding, the catalytic hydrolysis of an antibiotic substrate by the β-lactamase enzyme generates an electrical signal — confirming the...
01:25
Beta
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2024
Beta is a crucial metric in finance used to assess an investment's risk and expected return relative to the overall market. It is calculated as the slope of the line in a scatterplot that compares the returns of an individual stock to the returns of the market benchmark, typically represented by a broad market index. Beta quantifies how much a stock's price moves in response to market movements, providing insight into its volatility and systematic risk. A beta of one indicates that the stock's...
01:52
Eukaryotic Transcription Inhibitors
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2020
Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells. Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
FAQs
Inhibitors act against selected beta-lactamases rather than every resistance enzyme. If the bacterial enzyme falls within an inhibitor’s effective spectrum, the partner beta-lactam can remain intact and continue reaching penicillin-binding proteins. If the enzyme is not adequately blocked, hydrolysis may still occur, so treatment performance depends on matching the inhibitor with the resistance mechanism present.
Their protective effect occurs before the antibiotic’s main pharmacological target is disabled. By binding or inactivating susceptible beta-lactamases, the inhibitor reduces destruction of the antibiotic’s beta-lactam ring. The preserved drug can then retain access to penicillin-binding proteins, supporting disruption of bacterial cell-wall synthesis rather than being rendered ineffective by enzymatic hydrolysis.
A beta-lactam used alone may be vulnerable to hydrolysis by bacterial beta-lactamases. Adding a compatible inhibitor addresses that resistance mechanism by protecting the antibiotic from selected enzymes. The combination therefore adds a resistance-management function, but it does not guarantee activity against every resistant bacterium because effectiveness remains tied to inhibitor spectrum and the enzyme involved.
Three considerations are especially important: the inhibitor’s spectrum, the beta-lactamase produced by the bacterium, and local resistance patterns. These factors determine whether the inhibitor can protect its partner antibiotic in the relevant infection context. Consequently, the same combination may not have equal value across settings where the prevalent resistance enzymes differ.
A practical selection process begins by considering which bacterial beta-lactamase is involved, then comparing that enzyme with the inhibitor’s known spectrum. Local resistance patterns provide additional context for judging likely usefulness. This approach helps distinguish combinations that address the relevant mechanism from those whose inhibitor would not adequately protect the partner beta-lactam.
Amoxicillin-clavulanate and ceftazidime-avibactam illustrate how an inhibitor can be paired with a beta-lactam antibiotic to address enzyme-mediated resistance. These combinations are used in pharmacological treatment of infections caused by resistant bacteria. Their examples also show why the antibiotic and inhibitor must be considered together rather than evaluated as unrelated drugs.
They support antimicrobial stewardship because their value depends on using an inhibitor-antibiotic combination against a relevant resistance mechanism and considering local resistance patterns. They also guide drug development by emphasizing the need to design or select inhibitors with useful activity across important beta-lactamases. Both applications focus on preserving effective antibiotic treatment while addressing resistance.