Serratiopeptidase exhibits antibiofilm activity through the proteolytic function of N-terminal domain and versatile function of the C-terminal domain.

BACKGROUND

Serratiopeptidase, a serine protease traditionally used as an oral anti-inflammatory drug has been found to show antibiofilm action. Structurally, it comprises of two distinct domains; viz-the N-terminal catalytic domain (Ncat) and a C-terminal RTX (Repeat-In-Toxin) domain (Crtx). Understanding the antibiofilm action of the serratiopeptidase molecule, as well as the antibiofilm action of each of its two domains, was the objective of this study.

RESULTS

Separate clones to express the complete recombinant serratiopeptidase protein and its variant containing a mutation in the catalytic site, the N-terminal catalytic domain and its mutant, and the C-terminal Repeat-In-Toxin domain were prepared, and the proteins were purified. The impact of these proteins on pre-existing biofilms, as well as their effect upon addition of these proteins during biofilm formation was investigated.

CONCLUSIONS

In our investigation, we have been able to analyze the antibiofilm action of serratiopeptidase in detail. Obtained results conclude that while N-terminally located proteolytic domain of serratiopeptidase conventionally acts against biofilms by hydrolytic activity, the C-terminal domain regulates or prevents biofilm formation by yet unknown mechanism in addition to its known function as an C-terminal located calcium modulated internal chaperone ensuring the proper folding and secretion of the molecule. The study's findings give new evidence that the Crtx domain plays a significant role in antibiofilm action. The proteolytic Ncat domain breaks down pre-formed biofilms. The C-terminal domain, on the other hand, acts as an inhibitor of biofilm formation by regulating or preventing biofilm development.