Abstract
The mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1' position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1' position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83-99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal antigen degradation.
| Original language | English |
|---|---|
| Pages (from-to) | 1813-6 |
| Number of pages | 4 |
| Journal | Biological Chemistry |
| Volume | 383 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 2002 |
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Keywords
- Animals
- Antigen-Presenting Cells
- Chromatography, High Pressure Liquid
- Cysteine Endopeptidases
- Epitopes
- Immunochemistry
- Kidney
- Lysosomes
- Myelin Basic Protein
- Myoglobin
- Peptides
- Plant Proteins
- Structure-Activity Relationship
- Substrate Specificity
- Swine
- Journal Article
- Research Support, Non-U.S. Gov't
Cite this
Characterization of legumain. / Schwarz, Gerold; Brandenburg, Jens; Reich, Michael; Burster, Timo; Driessen, Christoph; Kalbacher, Hubert.
In: Biological Chemistry, Vol. 383, No. 11, 11.2002, p. 1813-6.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of legumain
AU - Schwarz, Gerold
AU - Brandenburg, Jens
AU - Reich, Michael
AU - Burster, Timo
AU - Driessen, Christoph
AU - Kalbacher, Hubert
PY - 2002/11
Y1 - 2002/11
N2 - The mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1' position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1' position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83-99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal antigen degradation.
AB - The mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1' position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1' position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83-99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal antigen degradation.
KW - Animals
KW - Antigen-Presenting Cells
KW - Chromatography, High Pressure Liquid
KW - Cysteine Endopeptidases
KW - Epitopes
KW - Immunochemistry
KW - Kidney
KW - Lysosomes
KW - Myelin Basic Protein
KW - Myoglobin
KW - Peptides
KW - Plant Proteins
KW - Structure-Activity Relationship
KW - Substrate Specificity
KW - Swine
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1515/BC.2002.203
DO - 10.1515/BC.2002.203
M3 - Article
VL - 383
SP - 1813
EP - 1816
JO - Biological Chemistry
JF - Biological Chemistry
SN - 1431-6730
IS - 11
ER -