<i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage
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...
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MDPI AG
2023-02-01
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| author | Vyacheslav M. Abramov Igor V. Kosarev Andrey V. Machulin Tatiana V. Priputnevich Evgenia I. Deryusheva Ekaterina L. Nemashkalova Irina O. Chikileva Tatiana N. Abashina Alexander N. Panin Vyacheslav G. Melnikov Nataliya E. Suzina Ilia N. Nikonov Marina V. Selina Valentin S. Khlebnikov Vadim K. Sakulin Vladimir A. Samoilenko Alexey B. Gordeev Gennady T. Sukhikh Vladimir N. Uversky Andrey V. Karlyshev |
| author_facet | Vyacheslav M. Abramov Igor V. Kosarev Andrey V. Machulin Tatiana V. Priputnevich Evgenia I. Deryusheva Ekaterina L. Nemashkalova Irina O. Chikileva Tatiana N. Abashina Alexander N. Panin Vyacheslav G. Melnikov Nataliya E. Suzina Ilia N. Nikonov Marina V. Selina Valentin S. Khlebnikov Vadim K. Sakulin Vladimir A. Samoilenko Alexey B. Gordeev Gennady T. Sukhikh Vladimir N. Uversky Andrey V. Karlyshev |
| author_sort | Vyacheslav M. Abramov |
| collection | DOAJ |
| description | 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 <i>Staphylococcus aureus</i> 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 <i>S. aureus</i> 8325-4 bacterial cells. LF3872 produced bacteriolysin BLF3872 that lyses the cells of the <i>S. aureus</i> 8325-4 mastitis-inducing strain. The sensitivity of the antibiotic-resistant <i>S. aureus</i> 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 <i>S. aureus</i> 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 <i>S. aureus</i> strains. The cell-free culture supernatant of LF3872 (CSLF3872) induced <i>S. aureus</i> cell damage and ATP leakage. The effectiveness of the bacteriolytic action of LF3872 strain did not depend on the origin of the <i>S. aureus</i> strains. The results reported here are important for the creation of new effective drugs against antibiotic-resistant strains of <i>S. aureus</i> circulating in humans and animals. |
| first_indexed | 2024-03-11T07:01:26Z |
| format | Article |
| id | doaj.art-6017fddc0919407b92a7054009d38e64 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-11T07:01:26Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-6017fddc0919407b92a7054009d38e642023-11-17T09:13:26ZengMDPI AGAntibiotics2079-63822023-02-0112347110.3390/antibiotics12030471<i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal DamageVyacheslav M. Abramov0Igor V. Kosarev1Andrey V. Machulin2Tatiana V. Priputnevich3Evgenia I. Deryusheva4Ekaterina L. Nemashkalova5Irina O. Chikileva6Tatiana N. Abashina7Alexander N. Panin8Vyacheslav G. Melnikov9Nataliya E. Suzina10Ilia N. Nikonov11Marina V. Selina12Valentin S. Khlebnikov13Vadim K. Sakulin14Vladimir A. Samoilenko15Alexey B. Gordeev16Gennady T. Sukhikh17Vladimir N. Uversky18Andrey V. Karlyshev19Federal Service for Veterinary and Phytosanitary Surveillance (Rosselkhoznadzor) Federal State Budgetary Institution “The Russian State Center for Animal Feed and Drug Standardization and Quality” (FGBU VGNKI), 123022 Moscow, RussiaFederal Service for Veterinary and Phytosanitary Surveillance (Rosselkhoznadzor) Federal State Budgetary Institution “The Russian State Center for Animal Feed and Drug Standardization and Quality” (FGBU VGNKI), 123022 Moscow, RussiaSkryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaKulakov National Medical Research Center for Obstetrics, Gynecology and Perinatology, Ministry of Health, 117997 Moscow, RussiaInstitute for Biological Instrumentation, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaInstitute for Biological Instrumentation, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaLaboratory of Cell Immunity, Blokhin National Research Center of Oncology, Ministry of Health RF, 115478 Moscow, RussiaSkryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaFederal Service for Veterinary and Phytosanitary Surveillance (Rosselkhoznadzor) Federal State Budgetary Institution “The Russian State Center for Animal Feed and Drug Standardization and Quality” (FGBU VGNKI), 123022 Moscow, RussiaGabrichevsky Research Institute for Epidemiology and Microbiology, 125212 Moscow, RussiaSkryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaFederal State Educational Institution of Higher Professional Education, Moscow State Academy of Veterinary Medicine and Biotechnology named after K.I. Skryabin, 109472 Moscow, RussiaFederal State Educational Institution of Higher Professional Education, Moscow State Academy of Veterinary Medicine and Biotechnology named after K.I. Skryabin, 109472 Moscow, RussiaInstitute of Immunological Engineering, 142380 Lyubuchany, RussiaInstitute of Immunological Engineering, 142380 Lyubuchany, RussiaSkryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center “Pushchino Scientific Center for Biological Research of Russian Academy of Science”, Russian Academy of Science, 142290 Pushchino, RussiaKulakov National Medical Research Center for Obstetrics, Gynecology and Perinatology, Ministry of Health, 117997 Moscow, RussiaKulakov National Medical Research Center for Obstetrics, Gynecology and Perinatology, Ministry of Health, 117997 Moscow, RussiaDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USADepartment of Biomolecular Sciences, Faculty of Health, Science, Social Care and Education, Kingston University London, Kingston upon Thames KT1 2EE, UKLF3872 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 <i>Staphylococcus aureus</i> 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 <i>S. aureus</i> 8325-4 bacterial cells. LF3872 produced bacteriolysin BLF3872 that lyses the cells of the <i>S. aureus</i> 8325-4 mastitis-inducing strain. The sensitivity of the antibiotic-resistant <i>S. aureus</i> 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 <i>S. aureus</i> 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 <i>S. aureus</i> strains. The cell-free culture supernatant of LF3872 (CSLF3872) induced <i>S. aureus</i> cell damage and ATP leakage. The effectiveness of the bacteriolytic action of LF3872 strain did not depend on the origin of the <i>S. aureus</i> strains. The results reported here are important for the creation of new effective drugs against antibiotic-resistant strains of <i>S. aureus</i> circulating in humans and animals.https://www.mdpi.com/2079-6382/12/3/471<i>L. fermentum</i>bacteriocinantibacterial activity<i>S. aureus</i>antibiotic resistance |
| spellingShingle | Vyacheslav M. Abramov Igor V. Kosarev Andrey V. Machulin Tatiana V. Priputnevich Evgenia I. Deryusheva Ekaterina L. Nemashkalova Irina O. Chikileva Tatiana N. Abashina Alexander N. Panin Vyacheslav G. Melnikov Nataliya E. Suzina Ilia N. Nikonov Marina V. Selina Valentin S. Khlebnikov Vadim K. Sakulin Vladimir A. Samoilenko Alexey B. Gordeev Gennady T. Sukhikh Vladimir N. Uversky Andrey V. Karlyshev <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage Antibiotics <i>L. fermentum</i> bacteriocin antibacterial activity <i>S. aureus</i> antibiotic resistance |
| title | <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage |
| title_full | <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage |
| title_fullStr | <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage |
| title_full_unstemmed | <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage |
| title_short | <i>Limosilactobacillus fermentum</i> 3872 That Produces Class III Bacteriocin Forms Co-Aggregates with the Antibiotic-Resistant <i>Staphylococcus aureus</i> Strains and Induces Their Lethal Damage |
| title_sort | i limosilactobacillus fermentum i 3872 that produces class iii bacteriocin forms co aggregates with the antibiotic resistant i staphylococcus aureus i strains and induces their lethal damage |
| topic | <i>L. fermentum</i> bacteriocin antibacterial activity <i>S. aureus</i> antibiotic resistance |
| url | https://www.mdpi.com/2079-6382/12/3/471 |
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