The antibacterial and antifungal properties of trappin-2 (pre-elafin) do not depend on its protease inhibitory function

  • Baranger K
  • Zani M
  • Chandenier J
 et al. 
  • 29


    Mendeley users who have this article in their library.
  • 68


    Citations of this article.


Trappin-2 (also known as pre-elafin) is an endogenous inhibitor of neutrophil serine proteases and is involved in the control of excess proteolysis, especially in inflammatory events, along with the structurally related secretory leucocyte proteinase inhibitor. Secretory leucocyte proteinase inhibitor has been shown to have antibacterial and antifungal properties, whereas recent data indicate that trappin-2 has antimicrobial activity against Pseudomonas aeruginosa and Staphylococcus aureus. In the present study, we tested the antibacterial properties of trappin-2 towards other respiratory pathogens. We found that trappin-2, at concentrations of 5-20 microm, has significant activity against Klebsiella pneumoniae, Haemophilus influenzae, Streptococcus pneumoniae, Branhamella catarrhalis and the pathogenic fungi Aspergillus fumigatus and Candida albicans, in addition to P. aeruginosa and S. aureus. A similar antimicrobial activity was observed with trappin-2 A62D/M63L, a trappin-2 variant that has lost its antiprotease properties, indicating that trappin-2 exerts its antibacterial effects through mechanisms independent from its intrinsic antiprotease capacity. Furthermore, the antibacterial and antifungal activities of trappin-2 were sensitive to NaCl and heparin, demonstrating that its mechanism of action is most probably dependent on its cationic nature. This enables trappin-2 to interact with the membranes of target organisms and disrupt them, as shown by our scanning electron microscopy analyses. Thus, trappin-2 not only provides an antiprotease shield, but also may play an important role in the innate defense of the human lungs and mucosae against pathogenic microorganisms.

Author-supplied keywords

  • Antifungal activity
  • Antimicrobial activity
  • Serine protease inhibitors
  • Trappin-2
  • WAP protein

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Kévin Baranger

  • Marie Louise Zani

  • Jacques Chandenier

  • Sandrine Dallet-Choisy

  • Thierry Moreau

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free