Ligandomes obtained from different HLA-class II-molecules are homologous for N- and C-terminal residues outside the peptide-binding cleft
Human CD4+ T lymphocytes play an important role in inducing potent immune responses. T cells are activated and stimulated by peptides presented in human leucocyte antigen (HLA)-class II molecules. These HLA-class II molecules typically present peptides of between 12 and 20 amino acids in length. The region that interacts with the HLA molecule, designated as the peptide-binding core, is highly conserved in the residues which anchor the peptide to the molecule. In addition, as these peptides are the product of proteolytic cleavages, certain conserved residues may be expected at the N- and C-termini outside the binding core. To study whether similar conserved residues are present in different cell types, potentially harbouring different proteolytic enzymes, the ligandomes of HLA-DRB1*03:01/HLA-DRB > 1 derived from two different cell types (dendritic cells and EBV-transformed B cells) were identified with mass spectrometry and the binding core and N- and C-terminal residues of a total of 16,568 peptides were analysed using the frequencies of the amino acids in the human proteome. Similar binding motifs were found as well as comparable conservations in the N- and C-terminal residues. Furthermore, the terminal conservations of these ligandomes were compared to the N- and C-terminal conservations of the ligandome acquired from dendritic cells homozygous for HLA-DRB1*04:01. Again, comparable conservations were evident with only minor differences. Taken together, these data show that there are conservations in the terminal residues of peptides, presumably the result of the activity of proteases involved in antigen processing.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2019 |
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| Erschienen: |
2019 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:71 |
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| Enthalten in: |
Immunogenetics - 71(2019), 8-9 vom: 13. Sept., Seite 519-530 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Kampstra, Arieke S B [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 08.11.2019 Date Revised 04.03.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1007/s00251-019-01129-6 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM301285888 |
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| 100 | 1 | |a Kampstra, Arieke S B |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Ligandomes obtained from different HLA-class II-molecules are homologous for N- and C-terminal residues outside the peptide-binding cleft |
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Human CD4+ T lymphocytes play an important role in inducing potent immune responses. T cells are activated and stimulated by peptides presented in human leucocyte antigen (HLA)-class II molecules. These HLA-class II molecules typically present peptides of between 12 and 20 amino acids in length. The region that interacts with the HLA molecule, designated as the peptide-binding core, is highly conserved in the residues which anchor the peptide to the molecule. In addition, as these peptides are the product of proteolytic cleavages, certain conserved residues may be expected at the N- and C-termini outside the binding core. To study whether similar conserved residues are present in different cell types, potentially harbouring different proteolytic enzymes, the ligandomes of HLA-DRB1*03:01/HLA-DRB > 1 derived from two different cell types (dendritic cells and EBV-transformed B cells) were identified with mass spectrometry and the binding core and N- and C-terminal residues of a total of 16,568 peptides were analysed using the frequencies of the amino acids in the human proteome. Similar binding motifs were found as well as comparable conservations in the N- and C-terminal residues. Furthermore, the terminal conservations of these ligandomes were compared to the N- and C-terminal conservations of the ligandome acquired from dendritic cells homozygous for HLA-DRB1*04:01. Again, comparable conservations were evident with only minor differences. Taken together, these data show that there are conservations in the terminal residues of peptides, presumably the result of the activity of proteases involved in antigen processing | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Antigen presenting cells | |
| 650 | 4 | |a Cleavage sites | |
| 650 | 4 | |a Human leucocyte antigen | |
| 650 | 4 | |a Peptide flanking regions | |
| 650 | 4 | |a Peptidome | |
| 650 | 4 | |a Protein processing | |
| 650 | 7 | |a HLA-DR Antigens |2 NLM | |
| 650 | 7 | |a Ligands |2 NLM | |
| 650 | 7 | |a Peptide Fragments |2 NLM | |
| 650 | 7 | |a Proteome |2 NLM | |
| 700 | 1 | |a van Heemst, Jurgen |e verfasserin |4 aut | |
| 700 | 1 | |a Janssen, George M |e verfasserin |4 aut | |
| 700 | 1 | |a de Ru, Arnoud H |e verfasserin |4 aut | |
| 700 | 1 | |a van Lummel, Menno |e verfasserin |4 aut | |
| 700 | 1 | |a van Veelen, Peter A |e verfasserin |4 aut | |
| 700 | 1 | |a Toes, René E M |e verfasserin |4 aut | |
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