Neutralization Epitopes
Neutralization Epitopes - Related Videos
13:58
Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells
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Cited by 28 •
2012
This protocol describes the use of peptide:MHC tetramers and magnetic microbeads to isolate low frequency populations of epitope-specific T cells and analyze them by flow cytometry. This method enables the direct study of endogenous T cell populations of interest from in vivo experimental systems.
05:15
Detection of Neutralization-sensitive Epitopes in Antigens Displayed on Virus-Like Particle (VLP)-Based Vaccines Using a Capture Assay
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Cited by 2 •
2022
Here, we present a protocol to detect neutralization epitopes on antigen-displaying virus-like particles (VLPs). Immunoprecipitation of the human immunodeficiency virus (HIV)-derived VLPs is performed using envelope glycoproteins-specific monoclonal antibodies coupled to protein G-conjugated magnetic beads. Captured VLPs are subsequently subjected to SDS-PAGE and Western blot-analysis employing viral core protein Gag-specific antibodies.
04:54
Cell-Based AAV Neutralizing Antibody Assay: A Colorimetric Technique to Detect Neutralizing Antibodies Against Specific Adeno-Associated Viruses in Serum
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2025
In this video, we demonstrate an in vitro colorimetric assay to detect the presence of neutralizing antibodies against alkaline phosphatase-expressing recombinant adeno-associated virus serotype 6 (rAAV6) vectors in sheep serum samples. The assay utilizes the reaction between the AAV encoding a human placental alkaline phosphatase gene and its substrate to generate an insoluble purple product.
07:59
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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Cited by 21 •
2014
Biochemical assays with recombinant human MHC II molecules can provide rapid, quantitative insights into immunogenic epitope identification, deletion, or design. Here, a peptide-MHC II binding assay scaled to 384-well plates is described. This cost effective format should prove useful in the fields of protein deimmunization and vaccine design and development.
07:55
Generation of Escape Variants of Neutralizing Influenza Virus Monoclonal Antibodies
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Cited by 10 •
2017
We describe a method by which we identify critical residues required for the binding of human or murine monoclonal antibodies that target the viral hemagglutinin of influenza A viruses. The protocol can be adapted to other virus surface glycoproteins and their corresponding neutralizing antibodies.
FAQs
Their location on a functional surface protein determines how antibody binding affects entry. Occupying a receptor-contacting region can obstruct attachment, whereas binding near a fusion-related site may prevent the structural rearrangement needed for membrane fusion. In other cases, the antibody stabilizes an inactive protein conformation. These mechanisms explain why epitope position matters for neutralizing activity.
Surface proteins often participate directly in attachment, entry, or membrane fusion, making them strategic targets for protective antibodies. An antibody response directed toward one of these proteins can affect an early step in infection rather than a later intracellular process. Studying the relevant regions therefore connects antibody recognition with the pathogen’s ability to enter host cells.
Comparing epitopes across strains can reveal differences in the antigenic regions recognized by neutralizing antibodies. When those regions change, existing antibodies may recognize the altered antigen less effectively, allowing the pathogen to escape aspects of prior immunity. Epitope comparison therefore helps connect molecular variation with differences in immune recognition and potential protection.
Epitope mapping identifies which antigenic regions are associated with antibodies capable of blocking infection. This information helps distinguish antibody recognition that is merely detectable from recognition linked to a protective effect. In immunology and infection research, the resulting map provides a framework for evaluating which parts of a pathogen antigen may be most important for effective immunity.
These maps can identify antigen regions that elicit antibodies able to interfere with attachment, entry, or fusion. Vaccine design can then focus attention on antigenic features associated with those protective responses rather than treating every region as equally relevant. Comparing maps across strains also helps assess whether a selected antigen reflects the diversity of recognized epitopes.
They identify antibody-binding regions where recognition can directly disrupt infection-related functions. A therapeutic antibody directed to an epitope involved in receptor interaction, protein activation, or fusion may block a critical entry step. Epitope information therefore supports the selection and characterization of antibody responses with a plausible mechanism for preventing pathogen infection.