Avidity Measurement
Avidity Measurement - Related Videos
01:41
Affinity and Avidity
0 Views •
2019
Overview Antibodies bind to toxins or substances on the surface of cells, bacteria, viruses, or fungi. The substance is called an antigen, and the precise binding site is the epitope. The strength of the antibody-epitope interaction is called affinity. When an antibody binds an antigen by multiple epitopes, the cumulative strength of the interaction is called avidity. The strength of the interaction influences the elicited immune response. The Adaptive Immune System Increases Efficiency by...
10:32
A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
0 Views •
Cited by 9 •
2016
Using a printed glycan microarray strategy, a conventional 96-well plate assay was miniaturized for analysis of influenza A virus hemagglutinin avidity and specificity for sialic acid containing receptors.
12:30
Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
0 Views •
Cited by 56 •
2012
AVEXIS is a high throughput protein interaction assay developed to systematically screen for novel extracellular receptor-ligand pairs involved in cellular recognition processes. It is specifically designed to detect transient protein interactions that are difficult to identify using other high throughput approaches.
07:22
Standardized Method for Measuring Collection Efficiency from Wipe-sampling of Trace Explosives
0 Views •
Cited by 7 •
2017
Optimized sampling protocols and the development of new wipe materials can be facilitated by standardized measurements of collection efficiency from wipe-sampling. Our approach for sampling trace explosives uses an automated device to control speed, force, and distance during wipe-sampling followed by extraction of collected explosives.
11:32
Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation
0 Views •
Cited by 23 •
2009
Regulated endocytosis governs the cell surface expression levels of the majority of membrane proteins. Here we utilize reducible, membrane impermeant biotinylation reagents to measure the endocytic rate of the dopamine transporter (DAT), a polytopic membrane protein. The method facilitates a straightforward approach to measuring the endocytic rate of most plasma membrane proteins.
FAQs
A chaotropic agent disrupts weaker antigen-antibody interactions while leaving stronger interactions more resistant. In an avidity assay, antibody binding is measured before and after this treatment, and the remaining signal indicates the relative strength of the multivalent interaction. A larger retained signal therefore reflects greater resistance to disruption, rather than simply more antibody being present.
B-cell responses generally mature through affinity selection, favoring antibodies that bind their targets more effectively. As this process proceeds, the overall binding strength of the antibody population can increase, producing higher measured avidity. This makes avidity a useful indicator of response maturation and helps distinguish a recent response from one that has become established.
Affinity describes the strength of an individual antibody-binding interaction, whereas avidity reflects the combined effect of multiple binding sites and their interactions with an antigen. Consequently, avidity can capture the functional strength of a multivalent antibody-antigen interaction more broadly than a measurement focused on one binding event. This distinction matters when interpreting antibody quality.
A typical workflow compares antibody binding under two conditions: before and after exposure to a chaotropic agent. The treatment selectively disrupts weaker interactions, and the resulting binding signals are compared with the untreated signal. This paired design provides a relative avidity assessment while keeping the antibody-antigen system under direct comparison.
In infection research, avidity measurement can add timing-related information to serological testing. Because antibody avidity generally rises as responses mature, the result may help distinguish antibodies associated with a recent response from those reflecting an established immune response. It therefore complements antibody detection when infection history is an important part of interpretation.
Researchers can use avidity measurement to examine whether vaccination produces antibodies with stronger, more mature interactions and to assess the quality and durability of the resulting response. The assay can also support comparisons of immune responses after infection or vaccination. Its value lies in evaluating binding strength alongside the presence of antibodies, not merely antibody detection alone.