2. Academic Validation
  3. The Mycobacterium tuberculosis prolyl dipeptidyl peptidase cleaves the N-terminal peptide of the immunoprotein CXCL-10

The Mycobacterium tuberculosis prolyl dipeptidyl peptidase cleaves the N-terminal peptide of the immunoprotein CXCL-10

  • Biol Chem. 2023 Jan 12. doi: 10.1515/hsz-2022-0265.
Trillion Surya Lioe 1,  Ziwen Xie 1,  Jianfang Wu 2,  Wenlong Li 1,  Li Sun 1,  Qiaoli Feng 1,  Raju Sekar 1,  Boris Tefsen 3 4,  David Ruiz-Carrillo 5
Affiliations

Affiliations

  • 1 Department of Biological Sciences, School of Science, Xi'an Jiaotong-Liverpool University, 111 Ren'ai Road, Suzhou, Jiangsu 215123, P. R. China.
  • 2 Department of Chemistry, School of Science, Xi'an Jiaotong-Liverpool University, 111 Ren'ai Road, Suzhou, Jiangsu 215123, P. R. China.
  • 3 Ronin Institute, Montclair, NJ 07043, USA.
  • 4 Microbiology, Department of Biology, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.
  • 5 European Molecular Biology Laboratory, Notkestraße 85, D-22607 Hamburg, Germany.
PMID: 36632703 DOI: 10.1515/hsz-2022-0265
Abstract

Dipeptidyl peptidases constitute a class of non-classical serine proteases that regulate an array of biological functions, making them pharmacologically attractive Enzymes. With this work, we identified and characterized a Dipeptidyl Peptidase from Mycobacterium tuberculosis (MtDPP) displaying a strong preference for proline residues at the P1 substrate position and an unexpectedly high thermal stability. MtDPP was also characterized with alanine replacements of residues of its active site that yielded, for the most part, loss of catalysis. We show that MtDPP catalytic activity is inhibited by well-known human DPP4 inhibitors. Using MALDI-TOF mass spectrometry we also describe that in vitro, MtDPP mediates the truncation of the C-X-C motif chemokine ligand 10, indicating a plausible role in immune modulation for this mycobacterial Enzyme.

Keywords

CXCL-10; DPP4; immune modulation; post-proline; prolyl oligopeptidase; thermostable.

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