Bacterial Lactamase
Bacterial Lactamase - Related Videos
04:43
β-Lactamase-Based Conductimetric Biosensor Assay for Protein-Protein Interactions
0 Views •
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...
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.
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.
05:26
Reporter Enzyme Fluorescence Imaging for In Vivo Tracking of Bacterial Infection
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2025
This video demonstrates the reporter enzyme fluorescence (REF) imaging for in vivo detection of Mycobacterium tuberculosis infection. The infected mice are intraperitoneally injected with a substrate for REF imaging. Upon being hydrolyzed by bacterial β-lactamase enzyme, the substrate emits fluorescence, the detection of which aids evaluation of infection.
05:21
Bacterial Transformation - Student Protocol
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2019
Bacterial Transformation ExpandIMPORTANT: In addition to wearing the appropriate personal protective equipment, be sure to take care to keep your face away from suspension cultures, and to avoid inhaling reagents. Do not touch your face while performing the experiment. Always wash your hands before and after every experiment. When you are ready to safely begin, check to make sure you have a tube or tubes of competent E. coli cells in your ice bucket. Then, transfer 50 µL from one of these tubes...
FAQs
These enzymes use distinct catalytic strategies to disrupt the beta-lactam structure: one relies on an active-site serine, whereas the other depends on metal ions. Identifying the catalytic mechanism gives researchers a framework for comparing enzyme behavior, interpreting resistance patterns, and evaluating whether an inhibitor-based approach is likely to preserve a particular antibiotic.
A lactamase’s substrate range indicates which beta-lactam drugs it can compromise, including particular penicillins, cephalosporins, or related agents. Mapping this range connects enzyme characterization with practical antibiotic selection. It also helps explain why an organism may resist some drugs while remaining susceptible to others, supporting more informed interpretation of treatment failure.
Testing how a bacterial lactamase responds to beta-lactamase inhibitors shows whether inhibitor combinations could counteract the enzyme’s activity. This information supports evaluation of therapies designed to preserve clinically important beta-lactam drugs. Comparing inhibitor response with substrate range can also clarify which antibiotic and inhibitor combinations merit further consideration.
Researchers can relate the enzyme’s substrate range and inhibitor response to antimicrobial susceptibility results. Together, these findings indicate which beta-lactam agents are more likely to be compromised and whether combination therapy may retain activity. This integrated interpretation helps connect molecular resistance mechanisms with treatment decisions in infection research.
Susceptibility testing shows how an organism responds to available antimicrobial agents and can reveal patterns consistent with resistance that may cause treatment failure. When interpreted alongside lactamase characterization, the results help distinguish compromised beta-lactams from potentially useful options and provide evidence for selecting an appropriate therapeutic strategy.
Tracking lactamase characteristics across resistant organisms supports surveillance of resistance patterns and helps researchers monitor threats to beta-lactam treatment. In immunology and infection studies, these data connect microbial enzyme activity with failed antimicrobial control, guide susceptibility testing, and inform development of combination therapies intended to protect important drugs.