Related Experiment Video
Updated: May 12, 2026
07:57
Accuracy in Dental Medicine, A New Way to Measure Trueness and Precision
Published on: April 29, 2014
[Recommendations for selecting antimicrobial agents for in vitro susceptibility studies using automatic and
Rafael Cantón1, Juan Ignacio Alós, Fernando Baquero
1Servicio de Microbiología, Hospital Universitario Ramón y Cajal, Madrid, España.
Enfermedades Infecciosas Y Microbiologia Clinica
|June 23, 2007
Summary
This study provides expert recommendations for optimizing automated antimicrobial susceptibility testing. It defines antimicrobial categories and reporting groups to improve resistance detection and clinical decision-making in microbiology labs.
Area of Science:
- Clinical Microbiology
- Antimicrobial Resistance
- Diagnostic Technology
Background:
- Increasing adoption of automated susceptibility testing in clinical microbiology labs.
- Current systems often use microdilution panels/cards to determine MIC values and clinical categories.
- Need for standardized recommendations for antimicrobial agents and concentrations in automated systems.
Framework:
- Recommendations developed by expert groups GEMARA and MENSURA.
- Defined antimicrobial categories (A, B, C) for panel inclusion.
- Established reporting groups (0-4) for antimicrobial agents based on clinical relevance and resistance detection.
Implementation:
- Selected antimicrobial agents based on clinical significance and resistance mechanisms.
- Defined specific concentrations for antimicrobial agents, adapted from EUCAST, CLSI, and MENSURA breakpoints.
- Categorized agents for inclusion in automated susceptibility testing panels.
Implications:
- Enhanced accuracy in antimicrobial susceptibility testing results.
- Improved detection of antimicrobial resistance mechanisms.
- Facilitates achieving the clinical objective of the antibiogram for better patient management.
Related Concept Videos
02:04Protein-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
01:42Phosphoinositides and PIPs
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
01:20¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...