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.

Biocatalytic Method for Producing an Affinity Resin for the Isolation of Immunoglobulins.

Affinity chromatography is a widely used technique for antibody isolation. This article presents the successful synthesis of a novel affinity resin with a mutant form of protein A (BsrtA) immobilized on it as a ligand. The key aspect of the described process is the biocatalytic immobilization of the ligand onto the matrix using the sortase A enzyme.

Opioid Analgesic as a Positive Allosteric Modulator of Acid-Sensing Ion Channels.

Tafalgin (Taf) is a tetrapeptide opioid used in clinical practice in Russia as an analgesic drug for subcutaneous administration as a solution (4 mg/mL; concentration of 9 mM). We found that the acid-sensing ion channels (ASICs) are another molecular target for this molecule. ASICs are proton-gated sodium channels that mediate nociception in the peripheral nervous system and contribute to fear and learning in the central nervous system.

Affinity Resins for the Isolation of Immunoglobulins G Obtained Using Biocatalytic Technology.

Affinity chromatography resins that are obtained by conjugation of matrices with proteins of bacterial origin, like protein A, are frequently used for the purification of numerous therapeutic monoclonal antibodies. This article presents the development of a biocatalytic method for the production of novel affinity resins with an immobilized mutant form of protein A via sortase A mediated reaction. The conditions for activation of the agarose Seplife 6FF matrix, selection of different types of linkers with free amino groups and conditions for immobilization of recombinant protein A on the surface of the activated matrix were studied.

Gene Analysis, Cloning, and Heterologous Expression of Protease from a Micromycete Capable of Activating Protein C of Blood Plasma.

Micromycetes are known to secrete numerous enzymes of biotechnological and medical potential. Fibrinolytic protease-activator of protein C (PAPC) of blood plasma from micromycete VKM-F4104D was obtained in recombinant form utilising the bacterial expression system. This enzyme, which belongs to the proteinase-K-like proteases, is similar to the proteases encoded in the genomes of ATCC MYA-4609, ATCC 42149 and 28.