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Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses

Author

Listed:
  • Mariena J. A. van der Plas

    (Lund University, BMC)

  • Ravi K. V. Bhongir

    (Lund University, BMC
    Present address: Division of Respiratory Medicine and Allergology, Department of Clinical Sciences Lund, Lund University, BMC, Tornavägen 10, Lund SE-22184, Sweden)

  • Sven Kjellström

    (Center for Molecular Protein Science, Lund University)

  • Helena Siller

    (Lund University, BMC)

  • Gopinath Kasetty

    (Lund University, BMC
    Present address: Division of Respiratory Medicine and Allergology, Department of Clinical Sciences Lund, Lund University, BMC, Tornavägen 10, Lund SE-22184, Sweden)

  • Matthias Mörgelin

    (Lund University, BMC)

  • Artur Schmidtchen

    (Lund University, BMC
    Dermatology and Venereology, Skane University Hospital
    Dermatology, LKCMedicine, Nanyang Technological University)

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen known for its immune evasive abilities amongst others by degradation of a large variety of host proteins. Here we show that digestion of thrombin by P. aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathways. Thus, P. aeruginosa ‘hijacks’ an endogenous anti-inflammatory peptide-based mechanism, thereby enabling modulation and circumvention of host responses.

Suggested Citation

  • Mariena J. A. van der Plas & Ravi K. V. Bhongir & Sven Kjellström & Helena Siller & Gopinath Kasetty & Matthias Mörgelin & Artur Schmidtchen, 2016. "Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses," Nature Communications, Nature, vol. 7(1), pages 1-13, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11567
    DOI: 10.1038/ncomms11567
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