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Overview of Lysins

In recent years, phage-derived lysins have gradually emerged as novel anti-infective drugs. They represent highly evolved enzymes for cleaving fundamental bonds in bacterial cell wall peptidoglycan to release phage progeny. Endolysins and exolysins are the two major lysinases. At the end of phage replication, endolysin is expressed to break down the peptidoglycan of the cell wall. Ectolysins break down peptidoglycan on the outside of bacteria during phage DNA invasion. Furthermore, lysins can act synergistically with antibiotics by resensitizing bacteria to insensitive antibiotics. Lysins have emerged as attractive clinical candidates due to their rapid bactericidal action, low drug resistance, and variable virulence.

Lysin Mechanism of Action

Unlike conventional antibiotics, which require bacterial cell division and metabolism to work, lysins quickly kill bacteria on contact. After binding to peptidoglycan, lysins cleave specific bonds within peptidoglycan, which are essential for maintaining cell wall stability and bacterial viability. Notably, animal cells lack peptidoglycan cell walls, so this mechanism provides excellent specificity for bacterial targets.

General Characteristics of Lysin-based Therapy

Phage lysins possess many key antimicrobial properties. They have a rapid killing effect on bacteria, and they can specifically target the target pathogen so that the normal microbiome can be preserved. In addition, they can act synergistically with other lysins or antibiotics and thus have a low tendency to develop resistance. Importantly, lysins are effective against colonizing pathogens that grow on mucosal surfaces and in biofilms. Therefore, lysins may offer new perspectives for antimicrobial therapy in the context of increasing antibiotic resistance.