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Bacteriocin-sensitive bacterial pathogens refer to a diverse group of bacteria, including both Gram-positive and Gram-negative species, that are susceptible to the antimicrobial action of bacteriocins (Cotter et al., 2005). Bacteriocins are ribosomally synthesized peptides produced by bacteria that inhibit the growth of or kill other bacterial strains, often those closely related to the producer (Riley & Wertz, 2002). These pathogens include significant clinical and foodborne threats such as Listeria monocytogenes, Staphylococcus aureus, and Enterococcus faecalis (Bierbaum & Sahl, 2009). The interaction between bacteriocins and these pathogens typically involves the targeting of essential cellular components, such as Lipid II for cell wall synthesis inhibition or the cytoplasmic membrane for pore formation, leading to rapid cell death (Heng et al., 2007). While bacteriocins offer a promising alternative to traditional antibiotics due to their high potency and specificity, their clinical application faces challenges including susceptibility to proteolytic degradation and the potential for the emergence of resistant bacterial strains (Field et al., 2012). Consequently, they are extensively studied for applications in food preservation and as potential therapeutic agents against multi-drug resistant infections.
Bacteriocins exert their effects through several mechanisms, primarily pore formation in the cytoplasmic membrane and inhibition of cell wall synthesis by binding to Lipid II (Heng et al., 2007). Some bacteriocins, like colicins, may also exhibit nuclease activity, degrading DNA or RNA, or inhibit protein synthesis (Riley & Wertz, 2002).
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