LOEWE Center for
Insect Biotechnology
& Bioresources

Therapeutic proteases

RNDr. Zdeněk Franta (PhD)

Wound healing is well-orchestrated multi facet process, which consists of three defined phases (the inflammatory phase, the proliferative phase and the tissue remodeling phase). Although wound care has significantly improved with the advances of modern medicine, chronic and non-healing wounds still remain a serious problem and their treatment bears a high financial burdens. One of the alternative treatments for various chronic wounds represents maggot debridement therapy (MDT). MDT can be defined as artificial induced myiasis, which is carefully controlled. Nowadays, larvae of the blow fly Lucilia sericata are used as an exclusive species in MDT and their beneficial effect on wound (i) debridement, (ii) disinfection as well as (iii) direct stimulation of wound healing processes has been well documented. Despite the superb effect of MDT on wound healing up to now only several molecules have been isolated and characterized in more details.

In our group, we focus primarily on identification of maggot derived proteolytic enzymes, their recombinant production and biochemical as well as biological characterization. To systematically identified maggot enzymes we applied next generation sequencing and explored transcriptomes of various larval tissues. This approach uncovered more than 180 peptidases species with different tissue profiles, which could be attributed to five classes of proteolytic enzymes (aspartic, cysteine, serine, threonine and metallopeptidases). With this valuable database in our hands we apply diverse molecular approaches and biochemical methods to identify enzymes, which could supplement live larvae in MDT or have a therapeutic or technical potential.

Figure 1:  Lucilia sericata larvae

Figure 2: Schematic workflow

Figure 3: Verification of digital gene expression analysis by quantitative RT-PCR.
(Source: Franta Z. et al. 2016; BioMed Research International)

Figure 4: Degradation of Extracellular matrix proteins by recombinant serine peptidase (Jonahm)
(Source: Pöppel A. et al. 2016; Insect Biochemistry and Molecular Biology)