Characterization of legumain

Gerold Schwarz, Jens Brandenburg, Michael Reich, Timo Burster, Christoph Driessen, Hubert Kalbacher

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


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 languageEnglish
Pages (from-to)1813-6
Number of pages4
JournalBiological Chemistry
Issue number11
Publication statusPublished - Nov 2002


  • 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


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