Antibacterial Activities of and Biofilm Removal by Ablysin, an Endogenous Lysozyme-Like Protein, Originated from Acinetobacter baumannii 1656-2.

Antibacterial Activities of and Biofilm Removal by Ablysin, an Endogenous Lysozyme-Like Protein, Originated from Acinetobacter baumannii 1656-2.

J Glob Antimicrob Resist. 2020 Oct 09;:

Authors: Kim S, Jin JS, Lee DW, Kim J

Abstract
OBJECTIVES: Multidrug-resistant (MDR) Acinetobacter baumannii as well as MDR Enterococcus faecalis, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa, and other Enterobacteriaceae (ESKAPE) currently present major public health problems. These bacteria are associated with opportunistic infections in intensive care units as well as in immunocompromised patients. There is an urgent need for new alternative antibacterials to control these MDR bacteria. We describe here the antibacterial action of a novel peptidoglycan hydrolase that targets bacterial cell walls identified in the genome of A. baumannii 1656-2 clinical isolate.
METHODS: We generated a recombinant protein from a sequence encoding a lysozyme-like protein identified in the A. baumannii 1656-2 genome. We named it Ablysin and tested its antibacterial activity and biofilm removal ability, targeting ESCAPE pathogens.
RESULTS: In vitro application of Ablysin resulted in a growth inhibition of the six aforementioned bacterial species with a highest activity against A. baumannii. Electron microscopy revealed the concentration-dependent (250-2,000 µg/mL) rupture of the A. baumannii bacterial cells accompanied by the elimination of the associated biofilm.
CONCLUSIONS: Taken together, Ablysin represents a potentially new class of antibacterial protein that can be used to target MDR A. baumannii as well as other bacterial species.

PMID: 33045439 [PubMed - as supplied by publisher]