Shukho Kim1, Jong-Sook Jin2, Da-Won Lee3, Jungmin Kim4. 1. Department of Microbiology, School of Medicine, Kyungpook National University, 680 Gukchaebosang-ro, Jung-gu, Daegu 41944, Republic of Korea. Electronic address: shukhokim@knu.ac.kr. 2. Department of Microbiology, School of Medicine, Kyungpook National University, 680 Gukchaebosang-ro, Jung-gu, Daegu 41944, Republic of Korea. Electronic address: in75724@hanmail.net. 3. Department of Microbiology, School of Medicine, Kyungpook National University, 680 Gukchaebosang-ro, Jung-gu, Daegu 41944, Republic of Korea. Electronic address: dwdwdw0123@naver.com. 4. Department of Microbiology, School of Medicine, Kyungpook National University, 680 Gukchaebosang-ro, Jung-gu, Daegu 41944, Republic of Korea. Electronic address: minkim@knu.ac.kr.
Abstract
OBJECTIVES: Multidrug-resistant (MDR) Acinetobacter baumannii as well as MDR Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and other Enterobacteriaceae ('ESKAPE' pathogens) currently present a major public-health problem. 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. Here we describe the antibacterial action of a novel peptidoglycan hydrolase that targets the bacterial cell wall, identified in the genome of clinical isolate A. baumannii 1656-2. METHODS: We generated a recombinant protein from a sequence encoding a lysozyme-like protein identified in the genome of A. baumannii 1656-2. We named it Ablysin and tested its antibacterial activity and biofilm removal ability targeting ESKAPE pathogens. RESULTS: In vitro application of Ablysin resulted in growth inhibition of the six aforementioned bacterial species, with a highest activity against A. baumannii. Electron microscopy revealed the concentration-dependent (250-2000 μg/mL) rupture of A. baumannii bacterial cells accompanied by elimination of the associated biofilm. CONCLUSIONS: Ablysin represents a potential new class of antibacterial proteins that can be used to target MDR A. baumannii as well as other bacterial species.
OBJECTIVES: Multidrug-resistant (MDR) Acinetobacter baumannii as well as MDR Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and other Enterobacteriaceae ('ESKAPE' pathogens) currently present a major public-health problem. 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. Here we describe the antibacterial action of a novel peptidoglycan hydrolase that targets the bacterial cell wall, identified in the genome of clinical isolate A. baumannii 1656-2. METHODS: We generated a recombinant protein from a sequence encoding a lysozyme-like protein identified in the genome of A. baumannii 1656-2. We named it Ablysin and tested its antibacterial activity and biofilm removal ability targeting ESKAPE pathogens. RESULTS: In vitro application of Ablysin resulted in growth inhibition of the six aforementioned bacterial species, with a highest activity against A. baumannii. Electron microscopy revealed the concentration-dependent (250-2000 μg/mL) rupture of A. baumannii bacterial cells accompanied by elimination of the associated biofilm. CONCLUSIONS:Ablysin represents a potential new class of antibacterial proteins that can be used to target MDR A. baumannii as well as other bacterial species.
Authors: Pamela Hindieh; Joseph Yaghi; André El Khoury; Ali Chokr; Ali Atoui; Nicolas Louka; Jean Claude Assaf Journal: AMB Express Date: 2022-10-03 Impact factor: 4.126