Hiv Epitope Display
Hiv Epitope Display - Related Videos
05:46
Rapid Screening of HIV Reverse Transcriptase and Integrase Inhibitors
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Cited by 15 •
2014
Here we describe cellular cytotoxicity and single round infectivity assays that allow for the rapid and accurate screening of compounds to determine their cellular cytotoxicity (CC50) and IC50 values against WT and drug resistant HIV-1.
13:58
Amplifying and Quantifying HIV-1 RNA in HIV Infected Individuals with Viral Loads Below the Limit of Detection by Standard Clinical Assays
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Cited by 10 •
2011
Quantifying levels of HIV-1 RNA in plasma and sequencing single HIV-1 genomes from individuals with viral loads below the limit of detection (50-75 copies/ml) is difficult. Here we describe how to extract and quantify plasma viral RNA using a real time PCR assay that reliably measures HIV-1 RNA down to 0.3 copies/ml and how to amplify viral genomes by single genome sequencing, from samples with very low viral loads.
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.
13:08
Visualizing Cell-to-cell Transfer of HIV using Fluorescent Clones of HIV and Live Confocal Microscopy
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Cited by 4 •
2010
This visualized experiment is a guide for utilizing a fluorescent molecular clone of HIV for live confocal imaging experiments.
FAQs
Repeated presentation can strengthen binding signals by placing multiple copies of an epitope in an accessible arrangement. This increased availability helps antibodies interact with the selected antigenic region during analysis. The resulting signal can make differences in antibody recognition easier to evaluate, although interpretation still depends on which epitope and carrier format were used.
The carrier provides a physical framework that presents the selected HIV sequence in a form accessible to immune molecules. Phage, protein scaffolds, and virus-like particles offer alternative display formats, while surface attachment provides another way to expose the epitope. Comparing formats can help determine whether recognition reflects the sequence itself or its presentation context.
Focusing on a defined region separates responses to that sequence from responses directed against other parts of the viral protein. This supports immune-epitope mapping and helps identify regions associated with antibody binding or neutralization. In immunology and infection research, such isolation clarifies which antigenic targets may be relevant for evaluating immune responses and designing immunogens.
A typical workflow begins by selecting an antigenic region from an HIV protein, such as an envelope protein or another viral protein. Researchers then genetically fuse the sequence to a carrier or attach it to a surface. After presentation, they expose the system to antibodies or antigen-presenting cells and evaluate the resulting interaction or binding signal.
Displayed epitopes provide defined targets for testing whether antibodies recognize a particular HIV sequence. Binding assays can therefore compare responses directed toward selected antigenic regions rather than toward an entire viral protein. These measurements help characterize antibody specificity and can contribute to identifying regions linked with neutralization, making the approach useful for immune-epitope mapping.
Researchers can use displayed HIV epitopes to examine whether a vaccine candidate elicits antibodies that recognize selected viral regions. Emphasizing defined targets supports assessment of responses associated with neutralization and informs rational immunogen design. The method is therefore useful for refining which HIV protein regions should be represented or emphasized in candidate vaccine constructs.