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Natural T Cell Epitope Containing Methyl Lysines on Mycobacterial Heparin-Binding Hemagglutinin
- Source :
- The Journal of immunology, 204 (7, Journal of Immunology, Journal of Immunology, Publisher : Baltimore : Williams & Wilkins, c1950-. Latest Publisher : Bethesda, MD : American Association of Immunologists, 2020, 204 (7), pp.1715-1723. ⟨10.4049/jimmunol.1901214⟩, Journal of Immunology, 2020, 204 (7), pp.1715-1723. ⟨10.4049/jimmunol.1901214⟩
- Publication Year :
- 2020
- Publisher :
- The American Association of Immunologists, 2020.
-
Abstract
- T cell epitopes are mostly nonmodified peptides, although posttranslationally modified peptide epitopes have been described, but they originated from viral or self-proteins. In this study, we provide evidence of a bacterial methylated T cell peptide epitope. The mycobacterial heparin-binding hemagglutinin (HBHA) is a protein Ag with a complex C-terminal methylation pattern and is recognized by T cells from humans latently infected with Mycobacterium tuberculosis. By comparing native HBHAwith recombinant HBHA produced in Mycobacterium smegmatis (rHBHA-Ms), we could link antigenic differences to differences in the methylation profile. Peptide scan analyses led to the discovery of a peptide containing methyl lysines recognized by a mAb that binds to native HBHA ∼100-fold better than to rHBHA-Ms. This peptide was also recognized by T cells from latently infected humans, as evidenced by IFN-g release upon peptide stimulation. The nonmethylated peptide did not induce IFN-g, arguing that the methyl lysines are part of the T cell epitope.<br />SCOPUS: ar.j<br />info:eu-repo/semantics/published
- Subjects :
- medicine.drug_class
T-Lymphocytes
[SDV]Life Sciences [q-bio]
T cell
Mycobacterium smegmatis
Immunology
Epitopes, T-Lymphocyte
Hemagglutinin (influenza)
Peptide
Monoclonal antibody
Methylation
Epitope
Interferon-gamma
03 medical and health sciences
0302 clinical medicine
Antigen
Lectins
Immunologie
medicine
Humans
[CHIM]Chemical Sciences
Immunology and Allergy
ComputingMilieux_MISCELLANEOUS
chemistry.chemical_classification
Antigens, Bacterial
biology
Chemistry
Lysine
Mycobacterium tuberculosis
biology.organism_classification
Molecular biology
Sciences biomédicales
3. Good health
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
medicine.anatomical_structure
biology.protein
[SDV.IMM]Life Sciences [q-bio]/Immunology
Protein Processing, Post-Translational
030215 immunology
Subjects
Details
- ISSN :
- 15506606 and 00221767
- Volume :
- 204
- Database :
- OpenAIRE
- Journal :
- The Journal of Immunology
- Accession number :
- edsair.doi.dedup.....9f38c6f0d2f84bf5ff1ee0c985db7cec