Targeting mono- and dual-species biofilms of Staphylococcus aureus and Pseudomonas aeruginosa by the recombinant anticoagulant enzyme PAPC from micromycete Aspergillus ochraceus.

Microbial biofilms have recently emerged as a critical target for treating bacterial infections due to their crucial role in developing antibiotic resistance. The wide-spectrum activity of proteolytic enzymes makes them particularly suitable for disrupting biofilms formed by diverse bacterial species, including dual-species biofilms. In this study, we propose the Protease-Activator of Protein C (PAPC) of human blood plasma, an enzyme produced by the micromycete Aspergillus ochraceus, as a novel tool to degrade the protein scaffold of mono- or dual-species biofilms formed by Staphylococcus aureus and Pseudomonas aeruginosa.

Draft genome sequence of VKM-F4104D (L-1) producing peptidase activator of protein C.

VKM-F4104D (L-1) is a saprotrophic fungus isolated from buried soils of Phanagoria (Russia). This strain is known as a producer of the fibrinolytic peptidase-activating plasma protein C. We have sequenced and assembled its genome for a more detailed understanding of the fungus' physiology and encoded peptidases.

Fibrin and Fibrinolytic Enzyme Cascade in Thrombosis: Unravelling the Role.

Blood clot formation in blood vessels (thrombosis) is a major cause of life-threatening cardiovascular diseases. These clots are formed by αA-, βB-, and ϒ-peptide chains of fibrinogen joined together by isopeptide bonds with the help of blood coagulation factor XIIIa. These clot structures are altered by various factors such as thrombin, platelets, transglutaminase, DNA, histones, and red blood cells.

Hemostatically Active Proteinase Produced by : Key Specific Properties and Effect on Target Proteins.

The effect of proteinase on the proteins of the human hemostasis system, fibrin, fibrinogen, plasminogen, protein C, and factor X, was studied. These proteins are key targets for proteolytic enzymes in therapy and diagnosis of thromboembolic complications. It was shown that proteinase efficiently cleaves fibrin and fibrinogen, but does not act precisely, since it cuts all three subunits of these proteins.