Peptide Hla
Peptide Hla - Related Videos
08:07
Personalized Peptide Arrays for Detection of HLA Alloantibodies in Organ Transplantation
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Cited by 2 •
2017
Mismatches in human leukocyte antigen (HLA) sequences between organ donor and recipient pairs are the major cause of antibody-mediated rejection in organ transplantation. Here we present the use of custom antigen arrays that are based on individual donors' HLA sequences to probe anti-donor HLA alloantibodies in organ recipients.
03:15
A Peptide Array-Based Detection of Anti-donor HLA Alloantibodies in Organ Recipients
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2025
This video demonstrates an assay to detect anti-donor HLA alloantibodies in organ recipients. A peptide array is synthesized to represent potential epitopes for antibody-mediated organ rejection. The array is incubated with the recipient's serum, containing alloantibodies that bind to their target epitopes. Antibody binding is detected using chemiluminescence to identify donor-specific HLA epitopes that incite alloantibody reactivity.
07:18
HLA-Ig Based Artificial Antigen Presenting Cells for Efficient ex vivo Expansion of Human CTL
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Cited by 17 •
2011
A new DC independent method for induction and expansion of antigen-specific T cells is described. HLA A2-Ig based artificial Antigen Presenting Cells (aAPC) are loaded with HLA-A2 restricted peptides to efficiently expand CTL of diverse antigen specificity. This technology holds great potential for CTL-based adoptive immunotherapy.
04:00
Immunoaffinity Based Extraction of Ubiquitinylated Peptides: A Technique to Selectively Extract Ubiquitin Tagged Peptides from Purified Peptide Fractions
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2023
This video describes a method to extract and purify ubiquitinylated peptides containing remnant di-glycine peptides from a complex peptide mixture. The presented method may help in identifying original ubiquitination sites in the protein.
10:37
Analysis of HBV-Specific CD4 T-cell Responses and Identification of HLA-DR-Restricted CD4 T-Cell Epitopes Based on a Peptide Matrix
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Cited by 2 •
2021
Based on a hepatitis B virus (HBV)-derived peptide matrix, HBV-specific CD4 T-cell responses could be evaluated in parallel with identification of HBV-specific CD4 T-cell epitopes.
FAQs
Sequence-specific binding determines whether a peptide can occupy the HLA groove in a form that can be recognized by T cells. This selectivity links the peptide’s amino-acid sequence to immune visibility rather than allowing every protein fragment to receive equal presentation. Consequently, studying binding patterns helps explain why some pathogen-, self-, or tumor-derived fragments become relevant to immune surveillance.
The source of a peptide helps define which T-cell population can respond. Peptides associated with intracellular proteins are considered through HLA class I and linked to CD8+ T-cell recognition, whereas fragments from extracellular material are associated with class II and CD4+ T-cell recognition. This distinction provides a framework for interpreting how different protein sources enter adaptive immune surveillance.
Sequence-specific interactions within the HLA groove make peptide selection a central variable in experiments. A study therefore cannot interpret a T-cell response from peptide identity alone; it must consider whether that sequence is compatible with the HLA molecule being examined. This principle helps explain differences in immune recognition among HLA contexts and guides comparisons of candidate peptides in infection, autoimmunity, and cancer studies.
The framework connects recognition of pathogen-derived fragments with recognition of self-derived fragments. In the first setting, it helps investigate immune responses to infection; in the second, it helps examine inappropriate immune activation. The same molecular question, whether a peptide sequence is presented and recognized in a particular HLA context, can therefore illuminate both protective surveillance and autoimmune disease mechanisms.
These studies can identify how peptide sequences participate in T-cell recognition and relate that recognition to immune activation. In immunology and infection research, the resulting information helps connect molecular presentation with pathogen recognition, tumor surveillance, and autoimmunity. It also provides a basis for selecting and evaluating peptide-HLA combinations in downstream vaccine, diagnostic, receptor-profiling, and immunotherapy work.
They provide a molecular basis for evaluating peptide candidates intended to engage antigen-specific T-cell responses. Because binding depends on sequence-specific interactions with an HLA molecule, vaccine-oriented studies can consider both the fragment and its presentation context rather than peptide sequence in isolation. This supports more informed investigation of immune activation against selected pathogen-related targets.
Peptide-HLA complexes support antigen-specific diagnostics by linking a defined peptide and HLA context to a T-cell recognition question. They also support T-cell receptor profiling, which examines receptor responses in relation to particular presented antigens. Together, these applications organize immune measurements around defined molecular targets and help researchers investigate antigen-specific T-cell responses associated with infection, autoimmunity, or tumor surveillance.
Targeted immunotherapy research uses peptide-HLA information to connect a selected antigenic fragment with the HLA context through which T cells encounter it. This focus can help investigators relate molecular recognition to tumor surveillance and immune activation. The approach is useful when the goal is to design or evaluate interventions aimed at particular antigen-specific T-cell responses rather than immune activity in general.