In vitro evidence for immune evasion activity by human plasmin associated to pathogenic Leptospira interrogans

Microb Pathog. 2011 Nov;51(5):360-5. doi: 10.1016/j.micpath.2011.06.008. Epub 2011 Jul 23.

Abstract

Leptospirosis is a widespread re-emerging zoonosis of human and veterinary concern. It has been shown that virulent leptospires protect themselves against the host's innate immune system, a strategy that allows the bacteria to reach immunologically safe environments. Although extensive studies on host-pathogen interactions have been performed, little is known on how leptospires deal with host immune attack. In a previous work, we demonstrated the ability of leptospires to bind human plasminogen (PLG), that after treatment with activators, conferred plasmin (PLA) activity on the bacteria surface. In this study, we show that the PLA activity associated to the outer surface of Leptospira could interfere with the host immune attack by conferring some evasion advantage during infection. We demonstrate that PLA-coated leptospires interfere with complement C3b and IgG depositions on the bacterial surface, probably through the degradation of these components, thus diminishing opsonization process. Similar decrease on the deposition was observed when normal and immune sera from patients diagnosed with leptospirosis were employed as a source of IgG. We believe that decreasing opsonization by PLA generation might be an important aspect of the leptospiral immune escape strategy and survival. To our knowledge, this is the first proteolytic activity of plasmin associated-Leptospira related to anti-opsonic properties reported to date.

MeSH terms

  • Fibrinolysin / immunology*
  • Fibrinolysin / metabolism
  • Host-Pathogen Interactions
  • Humans
  • Immune Evasion*
  • Leptospira interrogans / immunology
  • Leptospira interrogans / pathogenicity*
  • Leptospira interrogans / physiology
  • Leptospirosis / enzymology*
  • Leptospirosis / immunology*
  • Leptospirosis / metabolism
  • Leptospirosis / microbiology
  • Plasminogen / metabolism
  • Protein Binding
  • Protein Processing, Post-Translational

Substances

  • Plasminogen
  • Fibrinolysin