Mapping the substrate-binding subsite specificity of a Porphyromonas gingivalis Tpr peptidase

  • Dominika Staniec Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Wioletta Rut Department of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wrocław, Poland
  • Marcin Drag Department of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wrocław, Poland
  • Michal Burmistrz Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Michael Kitching Christina Lee Brown Envirome Institute, Division of Environmental Medicine, Department of Medicine, University of Louisville, Louisville, KY, USA
  • Jan Potempa 1Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland; 2Department of Oral Immunity and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY, USA
DOI: https://doi.org/10.18388/abp.2020_6904

Abstract

Calcium-dependent peptidases of the calpain family are widespread in eukaryotes but uncommon in prokaryotes. A few bacterial calpain homologs have been discovered but none of them have been characterized in detail. Here we present an in-depth substrate specificity analysis of the bacterial calpain-like peptidase Tpr from Porphyromonas gingivalis. Using the positional scanning hybrid combinatorial substrate library method, we found that the specificity of Tpr peptidase differs substantially from the papain family of cysteine proteases, showing a strong preference for proline residues at positions P2 and P3. Such a degree of specificity indicates that this P. gingivalis cell-surface peptidase has a more sophisticated role than indiscriminate protein degradation to generate peptide nutrients, and may fulfil virulence-related functions such as immune evasion.

Published
2023-12-08
Issue
Vol. 70 No. 4 (2023)
Section
Articles

Copyright (c) 2023 Dominika Staniec, Wioletta Rut, Marcin Drag, Michal Burmistrz, Michael Kitching, Jan Potempa

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