Authors

Vyacheslav M. Abramov, The Russian State Center for Animal Feed and Drug Standardization and Quality
Igor V. Kosarev, The Russian State Center for Animal Feed and Drug Standardization and Quality
Andrey V. Machulin, Skryabin Institute of Biochemistry and Physiology of Microorganisms
Tatiana V. Priputnevich, Kulakov National Medical Research Center for Obstetrics
Eugenia I. Deryusheva, Institute for Biological Instrumentation of the Russian Academy of Sciences
Ekaterina L. Nemashkalova, Institute for Biological Instrumentation of the Russian Academy of Sciences
Irina O. Chikileva, Institute of Immunological Engineering
Tatiana N. Abashina, Skryabin Institute of Biochemistry and Physiology of Microorganisms
Alexander N. Panin, The Russian State Center for Animal Feed and Drug Standardization and Quality
Vyacheslav G. Melnikov, Gabrichevsky Moscow Research Institute of Epidemiology and Microbiology
Natalia E. Suzina, Scryabin Institute of Biochemistry and Physiology of Microorganisms
Ilya N. Nikonov, Moscow State Academy of Veterinary Medicine and Biotechnology named after K.I. Skryabin
Marina V. Selina, Moscow State Academy of Veterinary Medicine and Biotechnology named after K.I. Skryabin
Valentin S. Khlebnikov, Institute of Immunological Engineering
Vadim K. Sakulin, Institute of Immunological Engineering
Vladimir A. Samoilenko, Skryabin Institute of Biochemistry and Physiology of Microorganisms
Alexey B. Gordeev, Kulakov National Medical Research Center for Obstetrics
Gennady T. Sukhikh, Kulakov National Medical Research Center for Obstetrics
Vladimir N. Uversky, University of South FloridaFollow
Andrey V. Karlyshev, Kingston University

Document Type

Article

Publication Date

2023

Keywords

L. Fermentum, Bacteriocin, Antibacterial Activity, S. Aureus, Antibiotic Resistance

Digital Object Identifier (DOI)

https://doi.org/10.3390/antibiotics12030471

Abstract

LF3872 was isolated from the milk of a healthy lactating and breastfeeding woman. Earlier, the genome of LF3872 was sequenced, and a gene encoding unique bacteriocin was discovered. We have shown here that the LF3872 strain produces a novel thermolabile class III bacteriolysin (BLF3872), exhibiting antimicrobial activity against antibiotic-resistant Staphylococcus aureus strains. Sequence analysis revealed the two-domain structural (lysozyme-like domain and peptidase M23 domain) organization of BLF3872. At least 25% residues of this protein are expected to be intrinsically disordered. Furthermore, BLF3872 is predicted to have a very high liquid-liquid phase separation. According to the electron microscopy data, the bacterial cells of LF3872 strain form co-aggregates with the S. aureus 8325-4 bacterial cells. LF3872 produced bacteriolysin BLF3872 that lyses the cells of the S. aureus 8325-4 mastitis-inducing strain. The sensitivity of the antibiotic-resistant S. aureus collection strains and freshly isolated antibiotic-resistant strains was tested using samples from women with lactation mastitis; the human nasopharynx and oral cavity; the oropharynx of pigs; and the cows with a diagnosis of clinical mastitis sensitive to the lytic action of the LF3872 strain producing BLF3872. The co-cultivation of LF3872 strain with various antibiotic-resistant S. aureus strains for 24 h reduced the level of living cells of these pathogens by six log. The LF3872 strain was found to be able to co-aggregate with all studied S. aureus strains. The cell-free culture supernatant of LF3872 (CSLF3872) induced S. aureus cell damage and ATP leakage. The effectiveness of the bacteriolytic action of LF3872 strain did not depend on the origin of the S. aureus strains. The results reported here are important for the creation of new effective drugs against antibiotic-resistant strains of S. aureus circulating in humans and animals.

Rights Information

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This work is licensed under a Creative Commons Attribution 4.0 License.

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Yes

Citation / Publisher Attribution

Antibiotics, v. 12, issue 3, art. 471

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