Novel Phage Lysin Abp013 against Acinetobacter baumannii

As antimicrobial resistance (AMR) continues to pose an ever-growing global health threat, propelling us into a post-antibiotic era, novel alternative therapeutic agents are urgently required. Lysins are bacteriophage-encoded peptidoglycan hydrolases that display great potential as a novel class of antimicrobials for therapeutics. While lysins against Gram-positive bacteria are highly effective when applied exogenously, it is challenging for lysins to access and cleave the peptidoglycan of Gram-negative bacteria due to their outer membrane. In this study, we identify a novel phage lysin Abp013 against Acinetobacter baumannii. Abp013 exhibited significant lytic activity against multidrug-resistant strains of A. baumannii. Notably, we found that Abp013 was able to tolerate the presence of human serum by up to 10%. Using confocal microscopy and LIVE/DEAD staining, we show that Abp013 can access and kill the bacterial cells residing in the biofilm. These results highlight the intrinsic bacteriolytic property of Abp013, suggesting the promising use of Abp013 as a novel therapeutic agent.

Automated summary

As antimicrobial resistance becomes a growing health threat, the need for novel therapeutic agents is urgent. This study identifies a lysin called Abp013 that exhibits significant lytic activity against drug-resistant strains of Acinetobacter baumannii. Abp013 is able to tolerate the presence of human serum and effectively kill bacterial cells within biofilms. These findings suggest that Abp013 holds promising potential as a novel therapeutic agent.