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Microbial Biofilms-Aided Resistance and Remedies to Overcome It
Published in Bakrudeen Ali Ahmed Abdul, Microbial Biofilms, 2020
Lysostaphin is a zinc metalloprotease derived from Staphylococcus simulans and has endopeptidase activity against penta-glycine crosslink in peptidoglycans of S. aureus bacterial cell wall. Lysostaphin significantly reduced S. aureus biofilm by killing them as well as eradicated pre-formed biofilm on different surfaces such as polycarbonate, polystyrene, or glass. It also disrupts the matrix of three strains of S. epidermidis at 200 µg/mL of lysostaphin for 3 h (Wu et al. 2003). Similarly, Walencka et al. also confirmed the biofilm inhibition potential of lysostaphin against 13 S. aureus and 12 S. epidermidis clinical strains at different concentrations (Walencka et al. 2005). Lysostaphin also showed synergism with nafcillin to eradicate biofilm of MRSA in an implanted catheter in mice. Furthermore, the synergistic effect of lysostaphin (20 µg/mL) with 10 other antibiotics was reported against MRSA and methicillin sensitive Staphylococcus aureus. The highest synergism was found with doxycycline, i.e., its minimum biofilm eradication concentration was reduced from 4 to 0.5 mg/mL (Kokai-Kun et al. 2009). The ability of lysostaphin and other enzymes to disperse biofilms alone or in combination with rifampicin and vancomycin against MRSA and MSSA has also been documented (Hogan et al. 2017).
Enhanced production of recombinant Staphylococcus simulans lysostaphin using medium engineering
Published in Preparative Biochemistry & Biotechnology, 2019
Zeynep Efsun Duman, Aişe Ünlü, Mehmet Mervan Çakar, Hayriye Ünal, Barış Binay
Lysostaphin [EC 3.4.24.75] is a zinc-dependent glycyl-glycine endopeptidase natively encoded by Staphylococcus simulans biovar staphylolyticus [NRRLB‑2628 (gi|126496)], an environmental competitor of S. aureus.[11,12] Lysostaphin hydrolyzes the glycylglycine bonds of polyglycine interpeptide bridges on the cell walls of S. aureus, S. epidermidis and S. carnosus in all metabolic states (growing, resting, or heat-killed).[13,14] This antibacterial protein represents a promising therapeutic agent against the widespread hospital infections provoked by staphylococcal species, particularly the multidrug-resistant S. aureus.[6,15,16] It has been widely utilized as an agent in research laboratories in order to identify the species of staphylococci and also to lyse staphylococcal cell walls for the liberation of intracellular enzymes, nucleic acids, cell membrane, and surface components.[17] Moreover, lysostaphin has significant capacity to disrupt staphylococcal biofilms in vitro not only by killing the staphylococci that are normally difficult to treat with antibiotics but also by stripping the extracellular biofilm matrix from the artificial surface.[14,18–20] According to scanning electron microscopy studies, lysostaphin eradicates both the sessile cells and the extracellular matrix of biofilms.[16,19] Therefore, lysostaphin activity provides a new treatment option for patients to treat staphylococcal infections of indwelling devices such as artificial heart valves and other prosthetic devices.[16,21] Due to these types of specific applications, enhanced production of lysostaphin was widely studied. Up to now, lysostaphin has been cloned and produced in a wide range of expression host cells[22–26] and expression systems.[13,17,25,27] Although some improvements have been made using recombinant DNA technologies to produce lysostaphin, it is still not widely used in clinical applications that require high amounts of the enzyme.[28] However, in the last two decades, medium engineering has been gaining importance as a method to enhance the yield of expressed protein[29] where it provides a novel strategy to produce increased amounts of proteins.