The Science Journal of the Lander College of Arts and Sciences
Abstract
This paper reviews the antibacterial potential of enzybiotics against Methicillin-resistant Staphylococcus aureus (MRSA). Due to the increasing occurrence of antibiotic resistance, researchers are looking to make use of the natural antibacterial qualities of virus bacteriophages, viral derived lysins, and antimicrobial peptides to fight MRSA infections. The efficacy of bacteriophages, endolysins, and bacteriocins as potential antibacterial agents against MRSA was extensively researched through Touro’s online library database. Each of their mechanisms of action allows them to effectively lyse S. aureus cells, by essentially disrupting the peptidoglycan in the cell wall, causing it to burst. The narrow host range of these antimicrobials causes eradication of only pathogenic bacteria while maintaining the state of normal flora. Researchers have tested the ability of bacteriophages to effectively eliminate MRSA and have experimentally created therapeutically effective phage cocktails to delay the development of bacterial resistance. Different in-vitro and in-vivo studies demonstrate the ability of endolysins to rapidly kill S. aureus regardless of their metabolic state. Truncated and chimeric endolysins are used to optimize certain endolysin properties while eliminating negative ones. The therapeutic use of bacteriocins has significantly reduced and even completely eradicated MRSA infections in rabbit and mice in-vivo studies. Additionally, bacteriocins display synergy when used along with endolysins. All areas of enzybiotics show synergy with antibiotics when both treatments are combined. Additional research must be done before bacteriophages, endolysins, and bacteriocins can be used as a new antibacterial agent against MRSA.
Recommended Citation
Finkelstein, R. (2021). Enzybiotic Therapy as Treatment for MRSA. The Science Journal of the Lander College of Arts and Sciences, 15(1), 17-23. Retrieved from https://touroscholar.touro.edu/sjlcas/vol15/iss1/4
