Lioe, Trillion Surya, Xie, Ziwen, Wu, Jianfang, Li, Wenlong, Sun, Li, Feng, Qiaoli, Sekar, Raju 
ORCID: 0000-0002-1182-9004, Tefsen, Boris ORCID: 0000-0001-6668-217X and Ruiz-Carrillo, David
(2023)
The <i>Mycobacterium tuberculosis</i> prolyl dipeptidyl peptidase cleaves the N-terminal peptide of the immunoprotein CXCL-10.
BIOLOGICAL CHEMISTRY, 404 (6).
pp. 633-643.
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 <i>Mycobacterium tuberculosis</i> (MtDPP) displaying a strong preference for proline residues at the P<sub>1</sub> 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 <i>in vitro</i>, MtDPP mediates the truncation of the C-X-C motif chemokine ligand 10, indicating a plausible role in immune modulation for this mycobacterial enzyme.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CXCL-10, DPP4, immune modulation, post-proline, prolyl oligopeptidase, thermostable |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 18 Apr 2023 08:40 |
| Last Modified: | 12 Apr 2024 04:54 |
| DOI: | 10.1515/hsz-2022-0265 |
| Open Access URL: | https://doi.org/10.1515/hsz-2022-0265 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3169638 |
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