Antimicrobial activity of probiotic strain Enterococcus faecium 1-35

Abstract

The study examines the search for alternative solutions to replace feed antibiotics for poultry farming. During the study of the probiotic strain Enterococcus faecium 1-35, its antimicrobial properties against some pathogenic microorganisms were established. Using a bioinformatics approach, genes for non-ribosomal peptide synthetases were discovered in the genome of Enterococcus faecium 1-35. A synthesis product of which is believed to have biological activity. Enterococcus faecium strain 1-35, capable of synthesizing active peptide products, can be regarded as an alternative solution when replacing feed antibiotics. The results obtained require additional studies of practical application to confirm the expected effect.

Keywords

antimicrobial resistance / alternative to antibiotics / non-ribosomal peptides / Enterococcus sp

References

[1] Fischbach M. A, Walsh C. T. Antibiotics for emerging pathogens. Science (New York, N.Y.). 2009 Aug;325(5944):1089–1093. DOI: 10.1126/science.1176667.

[2] Fischbach M. A., Walsh C. T. Antibiotics for emerging pathogens. Science (New York, N.Y.). 2009 Aug;325(5944):1089–1093. DOI: 10.1126/science.1176667.

[3] Okolelova T. M., Egorova T. V. and others. Guidelines for the use of biological products and feed additives to ensure the health and increase the productivity of broilers. Methodological recommendations // Sergiev Posad. 2013. (In Russ).

[4] Околелова Т. М., Егорова Т. В. и др. Руководство по использованию биопрепаратов и кормовых добавок для обеспечения здоровья и повышения продуктивности бройлеров. Методические рекомендации // Сергиев Посад. – 2013.

[5] Prjibelski A., Antipov D., Meleshko D., Lapidus A., & Korobeynikov A. (2020). Using SPAdes de novo assembler. Current Protocols in Bioinformatics, 70, e102. DOI: 10.1002/cpbi.102.

[6] Prjibelski A., Antipov D., Meleshko D., Lapidus A., & Korobeynikov, A. (2020). Using SPAdes de novo assembler. Current Protocols in Bioinformatics, 70, e102. DOI: 10.1002/cpbi.102.

[7] Blin K. [et al.]. antiSMASH 5.0: updates to the secondary metabolite genome mining pipeline // Nucleic Acids Res. – 2019. – Vol. 47, № W1. – P. W81–W87. DOI: 10.1093/nar/gkz310.

[8] Blin K. [et al.]. antiSMASH 5.0: updates to the secondary metabolite genome mining pipeline // Nucleic Acids Res. – 2019. – Vol. 47, № W1. – P. W81-W87. DOI: 10.1093/nar/gkz310.

[9] Flissi A, Dufresne Y, Michalik J, Tonon L, Janot S, Noé L, Jacques P, Leclère V, Pupin M. Norine, the knowledgebase dedicated to non-ribosomal peptides, is now open to crowdsourcing. Nucleic Acids Res. 2016 Jan 4;44(D1):D1113–8. DOI: 10.1093/nar/gkv1143.

[10] Orlova T. I., Bulgakova V. G., Polin A. N. Biologically active non-ribosomal peptides. III. The mechanism of biosynthesis of non-ribosomal peptides // Antibiotics and chemotherapy. 2012, no. 7–8 (57). pp. 43–54. (In Russ).

[11] Орлова Т. И., Булгакова В. Г., Полин А. Н. Биологические активные нерибосомальные пептиды. III. Механизм биосинтеза нерибосомальных пептидов // Антибиотики и химиотерапия. 2012, № 7–8 (57). С. 43–54.

[12] Kirstein J, Hoffmann A, Lilie H, Schmidt R, Rübsamen-Waigmann H, Brötz-Oesterhelt H, Mogk A, Turgay K. The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease. EMBO Mol Med. 2009 Apr;1(1):37–49. DOI: 10.1002/emmm.200900002.