A Jonah-like chymotrypsin from the therapeutic maggot Lucilia sericata plays a role in wound debridement and coagulation
| Autor: | Andreas Vilcinskas, Anke Gökçen, Andre Baumann, Klaus T. Preissner, Zdeněk Franta, Jochen Wiesner, Anne-Kathrin Pöppel, Annika Beckert, Mareike Kahl |
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| Přispěvatelé: | Publica |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Proteases medicine.medical_treatment Molecular Sequence Data Biochemistry Chromatography Affinity Microbiology 030207 dermatology & venereal diseases 03 medical and health sciences 0302 clinical medicine Maggot therapy medicine Animals Chymotrypsin Humans Amino Acid Sequence music Molecular Biology Blood Coagulation Serine protease Factor XII Protease music.instrument Debridement biology business.industry fungi Kallikrein Recombinant Proteins Biotechnology 030104 developmental biology Drosophila melanogaster Insect Science Larva biology.protein Wound healing business |
| Popis: | Lucilia sericata larvae are used in maggot debridement therapy, a traditional wound healing approach that has recently been approved for the treatment of chronic wounds. Maggot excretion products (MEP) contain many different proteases that promote disinfection, debridement and the acceleration of wound healing, e.g. by activating the host contact phase/intrinsic pathway of coagulation. In order to characterise relevant procoagulant proteases, we analysed MEP and identified a chymotrypsin-like serine protease with similarities to Jonah proteases from Drosophila melanogaster and a chymotrypsin from Lucilia cuprina. A recombinant form of the L. sericata Jonah chymotrypsin was produced in Escherichia coli. The activated enzyme (Jonah(m)) had a pH optimum of 8.0 and a temperature optimum of 37 degrees C, based on the cleavage of the chromogenic peptide s-7388 and casein. Jonahm reduced the clotting time of human plasma even in the absence of the endogenous protease kallikrein, factor XI or factor XII and digested the extracellular matrix proteins fibronectin, laminin and collagen IV, suggesting a potential mechanism of wound debridement. Based on these characteristics, the novel L. sericata chymotrypsin-like serine protease appears to be an ideal candidate for the development of topical drugs for wound healing applications. |
| Databáze: | OpenAIRE |
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