tailieunhanh - Báo cáo khoa học: The antibacterial and antifungal properties of trappin-2 (pre-elafin) do not depend on its protease inhibitory function

Trappin-2 (also known as pre-elafin) is an endogenous inhibitor of neutro-phil serine proteases and is involved in the control of excess proteolysis, especially in inflammatory events, along with the structurally related secre-tory leucocyte proteinase inhibitor. | ễFEBS Journal The antibacterial and antifungal properties of trappin-2 pre-elafin do not depend on its protease inhibitory function Kevin Baranger Marie-Louise Zani Jacques Chandenier Sandrine Dallet-Choisy and Thierry Moreau INSERM U618 Université Francois Rabelais Tours France Keywords antifungalactivity antimicrobial activity serine protease inhibitors trappin-2 WAP protein Correspondence T. Moreau INSERM U618 Proteases et Vectorisation Pulmonaires IFR 135 Imagerie Fonctionnelle University Francois Rabelais 10 Boulevard Tonnelle 37032 Tours Cedex France Fax 33 247 366 046 Tel 33 2 4736 6177 E-mail Received 8 January 2008 revised 18 February 2008 accepted 22 February 2008 doi 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 pM 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