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A simple screening method for detecting bindings between oligopeptides and HLA-DR molecules on filter papers: Possible application for mapping of putative helper T-cell epitopes on MSP1 of Plasmodium falciparum
- Source :
- Scopus-Elsevier
-
Abstract
- Binding capacities of synthetic peptides to HLA-DR molecules were tested on filter papers to identify putative helper T-cell epitopes on a malarial protein. The antigen tested was the merozoite surface glycoprotein 1 (MSP1) of Plasmodium falciparum, a vaccine candidate targeting the asexual erythrocytic stage. Bindings between synthetic oligopeptides and HLA-DR molecules were tested. Such bindings were not non-specific, and a known helper T-cell epitope peptide showed positive binding to the restricting HLA-DR molecule. By using this screening system, we observed the unequal distribution of HLA-DR-binding peptides in 10 out of 17 MSP1 blocks tested. Block #6 of MSP1 seemed to show the highest frequency in the positive binding; on the other hand, blocks #1 and #17, both of which were thought to be vaccine candidate regions, contained fewer HLA-DR binding peptides. This was not inconsistent with the results that block #17 was less stimulatory to peripheral T cells than block #6. The peptides with positive binding to HLA-DR showed actual epitope activities when we tested peptide-driven proliferation of human bulk T-cell lines, and association between the two parameters was statistically significant (P
- Subjects :
- Immunology
Molecular Sequence Data
Plasmodium falciparum
Epitopes, T-Lymphocyte
Peptide
Lymphocyte Activation
Microbiology
Epitope
Antigen
Virology
HLA-DR
Animals
Humans
Amino Acid Sequence
Binding site
Peptide sequence
Merozoite Surface Protein 1
chemistry.chemical_classification
biology
HLA-DR Antigens
T-Lymphocytes, Helper-Inducer
biology.organism_classification
Molecular biology
Epitope mapping
chemistry
Immunologic Techniques
Oligopeptides
Epitope Mapping
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Scopus-Elsevier
- Accession number :
- edsair.doi.dedup.....fc13f96226020f7e26df99a929e09a79