antibioticsАнтибиотики и ХимиотерапияAntibiot Khimioter = Antibiotics and Chemotherapy0235-2990ООО «Издательство ОКИ»10.37489/0235-2990-2026-71-1-2-64-76SYVQDXantibiotics-1331Research ArticleОБЗОРЫREVIEWSПроблема антибиотикорезистентности при использовании кормовых добавок и фунгицидов в агропромышленном комплексе. Часть 1The Use of Feed Additives and Fungicides in the Agro-Industrial Complex in Light of the Antibiotic Resistance Problem. Part 1https://orcid.org/0000-0002-2598-913XОлсуфьеваЕ. Н.OlsufyevaE. N.

Олсуфьева Евгения Николаевна — д. х. н., профессор, главный научный сотрудник Лаборатории химической трансформации антибиотиков

Москва

Scopus Author ID: 35595443300

WOS Research ID: B-12302017

РИНЦ Ausor ID: 57864

Evgenia N. Olsufyeva — D. Sc. in Chemistry, Professor, Chief Researcher at the Laboratory of Chemical Transformation of Antibiotics

Moscow

Scopus Author ID: 35595443300

WOS Research ID: B-1230-2017

RSCI Ausor ID: 57864

olsufeva@list.ruhttps://orcid.org/0000-0003-2801-380XЯнковскаяВ. С.YankovskayaV. S.

Янковская Валентина Сергеевна — д. т. н., доцент, профессор кафедры управления качеством и товароведения продуции

Москва

ResearcherID: AAR-2725-2021.

AuthorID: 562520

ScopusAuthor ID: 57195148578

Valentina S. Yankovskaya — D. Sc. in Technical Sciences, Professor of the Department of Quality Management and Commodity Science

Moscow

ResearcherID: AAR-2725-2021

AuthorID: 562520

ScopusAuthor ID: 57195148578 

ФГБНУ «Научно-исследовательский институт по изысканию новых антибиотиков им. Г. Ф. Гаузе» (ФГБНУ «НИИНА»)РоссияGause Institute of New AntibioticsRussian FederationФГБОУ ВО «Российский государственный аграрный университет — МСХА им. К. А. Тимирязева» (ФГБОУ ВО РГАУ-МСХА им. К. А. Тимирязева)РоссияRussian State Agrarian University — Moscow Timiryazev Agricultural AcademyRussian Federation202625022026711-26476Copyright © Олсуфьева Е.Н., Янковская В.С., 20262026Олсуфьева Е.Н., Янковская В.С.Olsufyeva E.N., Yankovskaya V.S.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.antibiotics-chemotherapy.ru/jour/article/view/1331

В агропромышленном комплексе (АПК), по возможности, вместо нежелательных с точки зрения развития резистентности патогенных микроорганизмов антибиотических препаратов, рекомендуется использовать соединения, которые, как считается, не оказывают существенного влияния на проблему антибиотикорезистентности. Такие антибиотики рассматриваются в качестве кормовых добавок и стимуляторов роста для профилактики бактериальных инфекций и ускоренного роста молодняка, а также в качестве фунгицидов в ветеринарии и в растениеводстве. Антибиотики представлены разными классами соединений и имеют различные механизмы действия; они выступают как ингибиторы синтеза клеточной стенки бактерий и грибов, синтеза белка и функций клеточных мембран. В данном обзоре представлены структуры этих антибиотиков, механизмы их действия и возможности развития резистентности, включая фактор влияния на экосистему человека.

In the agro-industrial complex (AIC), it is recommended, whenever possible, to use the compounds that are considered not to have a significant impact on the problem of antibiotic resistance instead of antibiotic drugs that are undesirable from the point of view of the development of resistance of pathogenic microorganisms. Antibiotics are represented by different classes of compounds and have different mechanisms of action; they act as inhibitors of bacterial and fungal cell wall synthesis, protein synthesis, and cell membrane functions. A number of such antibiotics are considered as feed additives and growth promoters for the prevention of bacterial infections and accelerated growth of young animals, as well as fungicides in veterinary medicine and plant growing. Antibiotics come in a variety of classes and have different mechanisms of action; they act as inhibitors of bacterial and fungal cell wall synthesis, protein synthesis, and cell membrane function. This review presents the structures of these antibiotics, their mechanisms of action, and the potential for resistance development, including their impact on the human ecosystem.

антибиотикиагро-промышленный комплекс (АПК)кормовые добавкистимуляторы ростаантибиотикорезистентностьфунгицидыantibioticsagro-industrial complex (AIC)feed additivesgrowth promotersantibiotic resistancefungicidesДанное исследование было проведено при финансовой поддержке Министерства науки и высшего образования Российской Федерации.ReferencesЩекотихин А. Е., Олсуфьева Е. Н., Янковская В. С. Антибиотики и родственные соединения. Научное издание. М.: Лаборатория знаний, 2022; 511 c. ISBN 978-5-93208-247-8.Shchekotikhin AE, Olsufyeva EN, Yankovskaya VS. Antibiotiki i rodstvennye soedineniya. Nauchnoe izdanie. Moscow: Laboratoriya Znanij, 2022; 511. (in Russ.)]. ISBN 978-5-93208-247-8.Олсуфьева Е. Н., Янковская В. С. Анализ проблемы антибиотикорезистентности в агропромышленном комплексе. Antibiot Khimioter = Antibiotics and Chemotherapy. 2024; 69 (9–10): 108–132. doi: https://doi.org/10.37489/02352990-2024-69-9-10-108-132].Olsufyeva EN, Yankovskaya VS. Analysis of the problem of antibiotic resistance in the agricultural sector. Antibiotiki i Khimioter. 2024; 69 (9–10): 108–132.(in Russ.)]. doi: https://doi.org/10.37489/02352990-2024-69-9-10-108-132].Butaye P, Devriese LA, Haesebrouck F. Antimicrobial growth promoters used in animal feed: effects of less well known antibiotics on grampositive bacteria. Clin Microbiol. Rev. 2003; 16 (2): 175–188. doi: 10.1128/CMR.16.2.175–188.2003.Butaye P, Devriese LA, Haesebrouck F. Antimicrobial growth promoters used in animal feed: effects of less well known antibiotics on grampositive bacteria. Clin Microbiol. Rev. 2003; 16 (2): 175–188. doi: 10.1128/CMR.16.2.175–188.2003.Yin X, Zabriskie TM. The enduracidin biosynthetic gene cluster from Streptomyces fungicidicus. Microbiology (Reading). 2006; 152: 2969–2983. doi: 10.1099/mic.0.29043-0.Yin X, Zabriskie TM. The enduracidin biosynthetic gene cluster from Streptomyces fungicidicus. Microbiology (Reading). 2006; 152: 2969–2983. doi: 10.1099/mic.0.29043-0.Zhang J, He Z, Xu J, Song S, Zhu Q, Wu G, et al. Semi-rational mutagenesis of an industrial Streptomyces fungicidicus strain for improved enduracidin productivity. Appl Microbiol Biotechnol, 2020; 104: 3459–3471. doi: 10.1007/s00253-020-10488-0.Zhang J, He Z, Xu J, Song S, Zhu Q, Wu G, et al. Semi-rational mutagenesis of an industrial Streptomyces fungicidicus strain for improved enduracidin productivity. Appl Microbiol Biotechnol, 2020; 104: 3459–3471. doi: 10.1007/s00253-020-10488-0.Fang X, Tiyanont K, Zhang Y, Wanner J, Boger D, Walker S. The mechanism of action of ramoplanin and enduracidin. Mol BioSyst. 2006; 2 (1): 69–76. doi: 10.1039/b515328j.Fang X, Tiyanont K, Zhang Y, Wanner J, Boger D, Walker S. The mechanism of action of ramoplanin and enduracidin. Mol BioSyst. 2006; 2 (1): 69–76. doi: 10.1039/b515328j.https://rubikonvet.by/ru/drugs/enramicin-8-porosokhttps://rubikonvet.by/ru/drugs/enramicin-8-porosokWallhausser KH, Nesemann G, Prave P, Steigler A. Moenomycin, a new antibiotic. I. Fermentation and isolation. Antimicrob Agents Chemother. (Bethesda), 1965; 5: 734–736. PMID: 5883490.Wallhausser KH, Nesemann G, Prave P, Steigler A. Moenomycin, a new antibiotic. I. Fermentation and isolation. Antimicrob Agents Chemother. (Bethesda), 1965; 5: 734–736. PMID: 5883490.King DT, Wasney GA, Nosella M, Fong A, Strynadka NCJ. Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B. J Biol Chem. 2017; 292 (3): 979–993. doi: 10.1074/jbc.M116.718403King DT, Wasney GA, Nosella M, Fong A, Strynadka NCJ. Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B. J Biol Chem. 2017; 292 (3): 979–993. doi: 10.1074/jbc.M116.718403https://www.vidal.ru/veterinar/flavomycin-80-27907https://www.vidal.ru/veterinar/flavomycin-80-27907Kofoed CB, Vester B. Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA. Antimicrob Agents Chemother. 2002; 46 (11): 3339–3342. doi: 10.1128/AAC.46.11.3339-3342.2002Kofoed CB, Vester B. Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA. Antimicrob Agents Chemother. 2002; 46 (11): 3339–3342. doi: 10.1128/AAC.46.11.3339-3342.2002Kyriakis SC. The effect of avilamycin in the control of stress induced post-weaning diarrhea in piglets. J Vet Pharmacol Ther. 1989; 12: 296–301.Kyriakis SC. The effect of avilamycin in the control of stress induced post-weaning diarrhea in piglets. J Vet Pharmacol Ther. 1989; 12: 296–301.Birgand G. Glycopeptide resistant enterococci: What’s the problem? Current Anaesthesia & Critical Care. 2009; 20 (5–6): 248–250. doi: 10.1016/j.cacc.2009.07.001.Birgand G. Glycopeptide resistant enterococci: What’s the problem? Current Anaesthesia & Critical Care. 2009; 20 (5–6): 248–250. doi: 10.1016/j.cacc.2009.07.001.McNicholas PM, Najarian DJ, Mann PA, Hesk D, Hare RS, Shaw KJ, et al. Evernimicin binds exclusively to the 50S ribosomal subunit and inhibits translation in cell-free systems derived from both gram-positive and gram-negative bacteria. Antimicrob Agents Chemother. 2000; 44 (5): 1121–1126. doi: 10.1128/AAC.44.5.1121-1126.2000.McNicholas PM, Najarian DJ, Mann PA, Hesk D, Hare RS, Shaw KJ, et al. Evernimicin binds exclusively to the 50S ribosomal subunit and inhibits translation in cell-free systems derived from both gram-positive and gram-negative bacteria. Antimicrob Agents Chemother. 2000; 44 (5): 1121–1126. doi: 10.1128/AAC.44.5.1121-1126.2000.Krupkina M, Wekselmana I, Matzova D, Eyala Z, Posnera YD, Rozenberg H, et al. Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding. Proc Natl Acad Sci U S A. 2016; 113 (44): E6796–E6805. doi: 10.1073/pnas.1614297113.Krupkina M, Wekselmana I, Matzova D, Eyala Z, Posnera YD, Rozenberg H, et al. Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding. Proc Natl Acad Sci U S A. 2016; 113 (44): E6796–E6805. doi: 10.1073/pnas.1614297113.Клименко А. В. Альтернативы антибиотикам в животноводстве. Комбикорма. 2021; 5. 66– 69. https://kombi-korma.ru/sites/default/files/2/05_21/2021_05_66-69.pdfKlimenko AV. Alternativy antibiotikam v zhivotnovodstve. Kombikorma. 2021; 5: 66–69. (in Russ.)]. https://kombi-korma.ru/sites/default/files/2/05_21/2021_05_66-69.pdfРешение Коллегии Евразийской Экономической Комиссии от 13 февраля 2018 года № 28.https://stylab.ru/directory/antimicrobials/avilamycin/Reshenie Kollegii Evrazijskoj Ekonomicheskoj Komissii ot 13 fevralya 2018 goda № 28 (in Russ.)]. https://stylab.ru/directory/antimicrobials/avilamycin/Herzog HL, Meseck E, Delorenzo S, Murawski A, Charney W, Rosselet JP. Chemistry of antibiotics from micromonospora. 3. Isolation and characterization of everninomicin D and B. Appl Microbiol. 1965; 13: 515–520. doi: 10.1128/am.13.4.515-520.1965.Herzog HL, Meseck E, Delorenzo S, Murawski A, Charney W, Rosselet JP. Chemistry of antibiotics from micromonospora. 3. Isolation and characterization of everninomicin D and B. Appl Microbiol. 1965; 13: 515–520. doi: 10.1128/am.13.4.515-520.1965.Maertens JA. Sch-27899 (Schering-Plough Corp). IDrugs. 1999; 2: 446–453.Maertens JA. Sch-27899 (Schering-Plough Corp). IDrugs. 1999; 2: 446–453.Mikolajka A, Liu H, Chen Y, Starosta AL, Márquez V, Ivanova M, et al. Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases. Chem Biol. 2011; 18 (5): 589–600. doi: 10.1016/j.chembiol.2011.03.010.Mikolajka A, Liu H, Chen Y, Starosta AL, Márquez V, Ivanova M, et al. Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases. Chem Biol. 2011; 18 (5): 589–600. doi: 10.1016/j.chembiol.2011.03.010.Belova L, Tenson T, Xiong L, McNicholas PM, Mankin AS. A novel site of antibiotic action in the ribosome: interaction of evernimicin with the large ribosomal subunit. Proc Natl Acad Sci USA. 2001; 98 (7): 3726–3731. doi: 10.1073/pnas.071527498.Belova L, Tenson T, Xiong L, McNicholas PM, Mankin AS. A novel site of antibiotic action in the ribosome: interaction of evernimicin with the large ribosomal subunit. Proc Natl Acad Sci USA. 2001; 98 (7): 3726–3731. doi: 10.1073/pnas.071527498.Панин А. Н., Комаров А. А., Куликовский А. В., Макаров Д. А. Проблема резистентности к антибиотикам возбудителей болезней, общих для человека и животных. Ветеринария и зоотехния: ветеринария. 2017; 5: 18–24.Panin AN, Komarov AA, Kulikovskij AV, Makarov DA. Problema rezistentnosti k antibiotikam vozbuditelej boleznej, obshchikh dlya cheloveka i zhivotnykh. Veterinariya i Zootekhniya: Veterinariya. 2017; 5: 18–24. (in Russ.)].Arenz S, Juette MF, Graf M, Nguyen F, Huter P, Polikanov YS, et al. Structures of the orthosomycin antibiotics avilamycin and evernimicin in complex with the bacterial 70S ribosome. PNAS, 2016; 113 (27): 7527–7532. doi: 10.1073/pnas.1604790113Arenz S, Juette MF, Graf M, Nguyen F, Huter P, Polikanov YS, et al. Structures of the orthosomycin antibiotics avilamycin and evernimicin in complex with the bacterial 70S ribosome. PNAS, 2016; 113 (27): 7527–7532. doi: 10.1073/pnas.1604790113Haste M, Thienphrapa W, Tran DN, Loesgen S, Sun P, Nam S-J, et al. Activity of the thiopeptide antibiotic nosiheptide against contemporary strains of methicillin-resistant Staphylococcus aureus. J Antibiot (Tokyo). 2012; 65 (12): 593–598. doi: 10.1038/ja.2012.77.Haste M, Thienphrapa W, Tran DN, Loesgen S, Sun P, Nam S-J, et al. Activity of the thiopeptide antibiotic nosiheptide against contemporary strains of methicillin-resistant Staphylococcus aureus. J Antibiot (Tokyo). 2012; 65 (12): 593–598. doi: 10.1038/ja.2012.77.Zhu R, Yu X, Zhang T, Kong Y, Wang F, Jia J, et al. In vitro and intracellular inhibitory activities of nosiheptide against Mycobacterium abscessus. Front Microbiol. 2022; 13: 926361. doi: 10.3389/fmicb.2022.926361.Zhu R, Yu X, Zhang T, Kong Y, Wang F, Jia J, et al. In vitro and intracellular inhibitory activities of nosiheptide against Mycobacterium abscessus. Front Microbiol. 2022; 13: 926361. doi: 10.3389/fmicb.2022.926361.Cundliffe E, Thompson J. The Mode of action of nosiheptide (multhiomycin) and the mechanism of resistance in the producing organism. J Gen Microbiol. 1981; 126 (1): 185–192. doi:10.1099/00221287-126-1-185.Cundliffe E, Thompson J. The Mode of action of nosiheptide (multhiomycin) and the mechanism of resistance in the producing organism. J Gen Microbiol. 1981; 126 (1): 185–192. doi:10.1099/00221287-126-1-185.https://www.nita-farm.ru/produktsiya/nozifhttps://www.nita-farm.ru/produktsiya/nozifBaumann S, Schoof S, Bolten M, Haering C, Takagi M, Shinya K, et al. Molecular determinants of microbial resistance to thiopeptide antibiotics. JACS. 2010; 132 (20): 6973–6981. doi: 10.1021/ja909317n.Baumann S, Schoof S, Bolten M, Haering C, Takagi M, Shinya K, et al. Molecular determinants of microbial resistance to thiopeptide antibiotics. JACS. 2010; 132 (20): 6973–6981. doi: 10.1021/ja909317n.Yin S, Jiang H, Chen D, Murchie AIH. Substrate recognition and modification by the nosiheptide resistance methyltransferase. PLoS one. 2015; 10 (4): e0122972. doi: 10.1371/journal.pone.0122972.Yin S, Jiang H, Chen D, Murchie AIH. Substrate recognition and modification by the nosiheptide resistance methyltransferase. PLoS one. 2015; 10 (4): e0122972. doi: 10.1371/journal.pone.0122972.Dewey RS, Arison BH, Hannah J, Shih DH, Albers-Schönberg G. The structure of efrotomycin. J Antibiot (Tokyo). 1985; 38 (12): 1691–1698. doi: 10.7164/antibiotics.38.1691.Dewey RS, Arison BH, Hannah J, Shih DH, Albers-Schönberg G. The structure of efrotomycin. J Antibiot (Tokyo). 1985; 38 (12): 1691–1698. doi: 10.7164/antibiotics.38.1691.Stutz MW, Johnson SL, Judith FR, Miller BM. In vitro and in vivo evaluations of the antibiotic efrotomycin. Poult Sci. 1983; 62 (8): 1612–1618. doi: 10.3382/ps.0621612.Stutz MW, Johnson SL, Judith FR, Miller BM. In vitro and in vivo evaluations of the antibiotic efrotomycin. Poult Sci. 1983; 62 (8): 1612–1618. doi: 10.3382/ps.0621612.Landini P, Bandera M, Soffientini A, Goldstein BP. Sensitivity of elongation factor Tu (EF-Tu) from different bacterial species to the antibiotics efrotomycin, pulvomycin and MDL 62879. J Gen Microbiol. 1993; 139 (4): 769–774. doi: 10.1099/00221287-139-4-769.Landini P, Bandera M, Soffientini A, Goldstein BP. Sensitivity of elongation factor Tu (EF-Tu) from different bacterial species to the antibiotics efrotomycin, pulvomycin and MDL 62879. J Gen Microbiol. 1993; 139 (4): 769–774. doi: 10.1099/00221287-139-4-769.Kimishima A, Hagimoto D, Honsho M, Watanabe Y, Iwatsuki M, Tsutsumi H, et al. Insights into the structure-activity relationship of a type III secretion system inhibitor, aurodox. Bioorg Med Chem Lett. 2022; 69: 128779–128784. doi: 10.1016/j.bmcl.2022.128779.Kimishima A, Hagimoto D, Honsho M, Watanabe Y, Iwatsuki M, Tsutsumi H, et al. Insights into the structure-activity relationship of a type III secretion system inhibitor, aurodox. Bioorg Med Chem Lett. 2022; 69: 128779–128784. doi: 10.1016/j.bmcl.2022.128779.Tate RL, Halley BA, Taub R, Green-Erwin ML, Chiu SHL. Efrotomycin interaction with soil clay and organic matter fractions. J Agric Food Chem. 1989; 37 (4): 1165–1169. doi: https://doi.org/10.1021/jf00088a076.Tate RL, Halley BA, Taub R, Green-Erwin ML, Chiu SHL. Efrotomycin interaction with soil clay and organic matter fractions. J Agric Food Chem. 1989; 37 (4): 1165–1169. doi: https://doi.org/10.1021/jf00088a076.Jackson KE, Pogula PK Patterson SE. Polyoxin and nikkomycin analogs: Recent design and synthesis of novel peptidyl nucleosides. Heterocyclic Commun. 2013; 19 (6): 375–386. doi: 10.1515/hc-2013-0141.Jackson KE, Pogula PK Patterson SE. Polyoxin and nikkomycin analogs: Recent design and synthesis of novel peptidyl nucleosides. Heterocyclic Commun. 2013; 19 (6): 375–386. doi: 10.1515/hc-2013-0141.Osada H. Discovery and applications of nucleoside antibioticsbeyond polyoxin. J Antibiot. 2019; 72 (12): 855–864. doi: 10.1038/s41429-0190237-1.Osada H. Discovery and applications of nucleoside antibioticsbeyond polyoxin. J Antibiot. 2019; 72 (12): 855–864. doi: 10.1038/s41429-0190237-1.Varnava KG, Ronimus RS, Sarojini V. A review on comparative mechanistic studies of antimicrobial peptides against archaea. Biotechnol Bioeng. 2017; 114 (11): 2457–2473. doi: 10.1002/bit.26387.Varnava KG, Ronimus RS, Sarojini V. A review on comparative mechanistic studies of antimicrobial peptides against archaea. Biotechnol Bioeng. 2017; 114 (11): 2457–2473. doi: 10.1002/bit.26387.Steinbach WJ, Stevens DA. Review of newer antifungal and immunomodulatory strategies for invasive Aspergillosis. Clin Infect Dis. 2003; 37 (s3): S157–S187. doi: 10.1086/376523.Steinbach WJ, Stevens DA. Review of newer antifungal and immunomodulatory strategies for invasive Aspergillosis. Clin Infect Dis. 2003; 37 (s3): S157–S187. doi: 10.1086/376523.Winn M, Goss RJM, Kimura K, Bugg TDH. Antimicrobial nucleoside antibiotics targeting cell wall assembly: recent advances in structure–function studies and nucleoside biosynthesis. Nat Prod Rep. 2010; 27 (2): 279–304. doi: 10.1039/b816215h.Winn M, Goss RJM, Kimura K, Bugg TDH. Antimicrobial nucleoside antibiotics targeting cell wall assembly: recent advances in structure–function studies and nucleoside biosynthesis. Nat Prod Rep. 2010; 27 (2): 279–304. doi: 10.1039/b816215h.Ramirez-Ramirez N, Gutierrez-Corona F, Lopez-Romero E. Nikkomycin-resistant mutants of Mucor rouxii: physiological and biochemical properties. Antonie Van Leeuwenhoek. 1993; 64 (1): 27–33. doi: 10.1007/BF00870918.Ramirez-Ramirez N, Gutierrez-Corona F, Lopez-Romero E. Nikkomycin-resistant mutants of Mucor rouxii: physiological and biochemical properties. Antonie Van Leeuwenhoek. 1993; 64 (1): 27–33. doi: 10.1007/BF00870918.Larwood DJ. Nikkomycin Z — ready to meet the promise? J Fungi. 2020; 6 (4): 261. doi: 10.3390/jof6040261.Larwood DJ. Nikkomycin Z — ready to meet the promise? J Fungi. 2020; 6 (4): 261. doi: 10.3390/jof6040261.https://pharmaoffer.com/ru/api-excipient-supplier/enzyme-replacements-modifiers/nikkomycin-zhttps://pharmaoffer.com/ru/api-excipient-supplier/enzyme-replacements-modifiers/nikkomycin-zCeregeghetti DM, Carreira EM. Amphotericin B: 50 years of chemistry and biochemistry. Synthesis. 2006; 6: 914–942. doi: 10.1055/s-2006926368.Ceregeghetti DM, Carreira EM. Amphotericin B: 50 years of chemistry and biochemistry. Synthesis. 2006; 6: 914–942. doi: 10.1055/s-2006926368.Касумов Х. М. Структура и мембранная функция полиеновых макролидных антибиотиков. Ред. Д. А. Алиев. М.: Элм-Наука. 2009; 512.Kasumov KhM. Struktura i membrannaya funktsiya polienovykh makrolidnykh antibiotikov. DA Aliev (ed.). Moscow: ElmNauka. 2009; 512. (in Russ.)].Ветлуrина Л. А., Никитина Е. Т. Противогрибковые полиеновые антибиотики. Алма-Ата: Наука. 1980; 248.Vetlurina LA, Nikitina ET. Protivogribkovye polienovye antibiotiki. Alma-Ata: Nauka. 1980; 248. (in Russ.)].Płosiński M, Laskowski T, Sowiński P, Pawlak J. Stereostructure of mycoheptin A2. Magn Reson Chem. 2012; 50 (12): 818–822. doi: 10.1002/mrc.3890.Płosiński M, Laskowski T, Sowiński P, Pawlak J. Stereostructure of mycoheptin A2. Magn Reson Chem. 2012; 50 (12): 818–822. doi: 10.1002/mrc.3890.https://www.med74.ru/infoitem5694.htmlhttps://www.med74.ru/infoitem5694.htmlШикова Ю. В., Лиходед В. А., Лиходед Т. А. Учебное пособие. Уфа: Изд-во ГОУ ВПО «Башгосмедуниверситет Росздрава». 2010; 318.Shikova YuV, Likhoded VA, Likhoded TA. Uchebnoe posobie. Ufa: Izdvo GOU VPO «Bashgosmeduniversitet Roszdrava». 2010; 318. (in Russ.)].Ветеринарная фармакология. Токсикология: практикум. Под ред. Т.В. Бурцева, Н. Г. Курочкина. Екатеринбург: Изд-во Уральского ГАУ. 2021; 136. ISBN 978-5-87203-477-3.Veterinarnaya farmakologiya. Toksikologiya: praktikum.  TV Burtseva, NG Kurochkina (eds.). Ekaterinburg: Izd-vo Uralskogo GAU. 2021; 136. (in Russ.)]. ISBN 978-5-87203-477-3.https://www.rlsnet.ru/active-substance/mikogeptin-1471https://www.rlsnet.ru/active-substance/mikogeptin-1471Шенин Ю. Д., Дауренбекова А. С., Моргунова А. Ф., Ветлугина Л. А., Яковлев А. А. Структура пентаенового антибиотика розеофунгина. Антибиотики и медицинская биотехнология. 1986; 31 (5): 341–349.Shenin YD, Daurenbekova AS, Morgunova AF, Vetlugina LA, Iakovlev AA. Structure of the pentaene antibiotic roseofungin. Antibiotiki i Meditsinskaya Biotekhnologiya. 1986; 31(5): 341–349. (in Russ.)].Саданов А. К., Березин В. Э., Кулмагамбетов И. Р., Треножникова Л. П., Балгимбаева А. С. Розеофунгин-АС, мазь 2% для лечения Tinea Pedis и Tinea Corporis: результаты рандомизированного слепого проспективного многоцентрового клинического исследования III фазы. Фармация Казахстана. 2021; 5: 55–64.Sadanov AK, Berezin VE, Kulmagambetov IR, Trenozhnikova, LP Balgimbaeva AS. RoseofunginAS, 2% ointment for the treatment of Tinea Pedis and Tinea Corporis: results of a randomized, single-blind, prospective, multicenter phase III clinical trial. Farmatsiya Kazakhstana. 2021; 5: 55–64. (in Russ.)].https://drugs.medelement.com/drug/розеофунгин–ас-2-инструкция/40372161613464181?instruction_lang=RUhttps://drugs.medelement.com/drug/розеофунгин–ас-2-инструкция/40372161613464181?instruction_lang=RUСаданов А. К., Акылова М. А., Балгимбаева А. С., Ибрагимова Л. Н., Бекежанова Т. С., Итемирова А. О. и др. Известия Национальной академии наук Республики Казахстан. Серия биологическая и медицинская. 2018; 330 (6):44–49. doi: https://doi.org/10.32014/2018.2518-1629.16.Sadanov AK, Akylova MА, Balgimbaeva AS, Ibragimova LN, Bekezhanova TS, Itemirova AO, et al. Activity of antibiotic roseofungin against clinical pathogens of vaginal candidiasis. News of the National Academy of Sciences of the Republic of Kazakhstan. 2018; 330 (6): 44–49]. (in Russ.)]. doi: https://doi.org/10.32014/2018.2518-1629.16.Саданов А. К., Березин В. Э., Кулмагамбетов И. Р., Треножникова Л. П., Балгимбаева А. С. Новый оригинальный лекарственный препарат «Розеофунгин-АС, мазь 2%». Фармация Казахстана. 2021; 5 (238): 55–64.doi: https://doi.org/10.53511/pharmkaz.2021.70.20.011.Sadanov AK, Berezin VE,Kulmagambetov IR,Trenozhnikova LP, Balgimbayeva AS. New original drug Roseofungin-AS, ointment 2%. Pharmacy of Kazakhstan. 2021; 5 (238): 55–64. (in Russ.)]. doi: https://doi.org/10.53511/pharmkaz.2021.70.20.011.Shi L, Nwet TT, Ge B, Zhao W, Liu B, Cui H, Zhang K. Antifungal and plant growth-promoting activities of Streptomyces roseoflavus strain NKZ-259. Biol Control. 2018; 125: 57–64. doi: 10.1016/j.biocontrol.2018. 06.012.Shi L, Nwet TT, Ge B, Zhao W, Liu B, Cui H, Zhang K. Antifungal and plant growth-promoting activities of Streptomyces roseoflavus strain NKZ-259. Biol Control. 2018; 125: 57–64. doi: 10.1016/j.biocontrol.2018. 06.012.Sarkar DJ, Mukherjee I, Shakil NA, Rana VS, Kaushik P, Debnath S. Antibiotics in agriculture: use and impact. indian journal of ethnophytopharmaceuticals (IJEPP). 2018; 4 (1): 4–19. https://www.researchgate.net/publication/325010472Sarkar DJ, Mukherjee I, Shakil NA, Rana VS, Kaushik P, Debnath S. Antibiotics in agriculture: use and impact. indian journal of ethnophytopharmaceuticals (IJEPP). 2018; 4 (1): 4–19. https://www.researchgate.net/publication/325010472Lokhande PD, Gawai KR, Kodam KM, Waghmare BY, Chabukswar AR, Jagdale SC. Water soluble amide derivatives of polyene antibiotic and their antifungal activity. Trends in Applied Sciences Research. 2006; 1 (5): 529–533. https://scialert.net/abstract/?doi=tasr.2006.529.533Lokhande PD, Gawai KR, Kodam KM, Waghmare BY, Chabukswar AR, Jagdale SC. Water soluble amide derivatives of polyene antibiotic and their antifungal activity. Trends in Applied Sciences Research. 2006; 1 (5): 529–533. https://scialert.net/abstract/?doi=tasr.2006.529.533Sawant SD, Sawant IS, Banerjee K, Shetty D, Waghmare M, Kalbhor G, et al. Bio-efficacy of Aureofungin-sol in control of downy and powdery mildews in grape. J Hortl Sci. 2011;6 (2): 136–140. doi: 10.24154/jhs.v6i2.421.Sawant SD, Sawant IS, Banerjee K, Shetty D, Waghmare M, Kalbhor G, et al. Bio-efficacy of Aureofungin-sol in control of downy and powdery mildews in grape. J Hortl Sci. 2011;6 (2): 136–140. doi: 10.24154/jhs.v6i2.421.Ghosh P. K. Revisiting novel active pharmaceutical ingredients from India. Achievements and Future Challenges. RIS 2021; 21. ISBN: 81-7122-164-5.Ghosh P. K. Revisiting novel active pharmaceutical ingredients from India. Achievements and Future Challenges. RIS 2021; 21. ISBN: 81-7122-164-5.Misato T, Blasticidin S. In: Gottlieb D., Shaw PD. (eds) Mechanism of action. Antibiotics. 1967; 1. Springer, Berlin, Heidelberg. doi: 10.1007/9783-642-46051-7_32.Misato T, Blasticidin S. In: Gottlieb D., Shaw PD. (eds) Mechanism of action. Antibiotics. 1967; 1. Springer, Berlin, Heidelberg. doi: 10.1007/9783-642-46051-7_32.Hamer JE, Talbot NJ. Infection-related development in the rice blast fungus Magnaporthe grisea. Curr Opin Microbiol. 1998; 1 (6): 693–697. doi: 10.1016/s1369-5274(98)80117-3.Hamer JE, Talbot NJ. Infection-related development in the rice blast fungus Magnaporthe grisea. Curr Opin Microbiol. 1998; 1 (6): 693–697. doi: 10.1016/s1369-5274(98)80117-3.Svidritskiy E, Ling C, Ermolenkob DN, Korostelev AA. Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome. PNAS; 2013, 110 (30): 12283–12288. doi: 10.1073/pnas.1304922110.Svidritskiy E, Ling C, Ermolenkob DN, Korostelev AA. Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome. PNAS; 2013, 110 (30): 12283–12288. doi: 10.1073/pnas.1304922110.Izumi M, Miyazawa H, Kamakura T, Yamaguchi I, Endo T. Hanaoka, F. Blasticidin S-resistance gene (bsr): a novel selectable marker for mammalian cells. Exp. Cell Res. 1991; 197 (2): 229–233. doi: 10.1016/00144827(91)90427-v.Izumi M, Miyazawa H, Kamakura T, Yamaguchi I, Endo T. Hanaoka, F. Blasticidin S-resistance gene (bsr): a novel selectable marker for mammalian cells. Exp. Cell Res. 1991; 197 (2): 229–233. doi: 10.1016/00144827(91)90427-v.K’ominek LA. Cycloheximide production by Streptomyces griseus: control mechanisms of cycloheximide biosynthesis. Antimicrob Agents Chemother. 1975; 7(6): 856–6. doi: 10.1128/AAC.7.6.856.K’ominek LA. Cycloheximide production by Streptomyces griseus: control mechanisms of cycloheximide biosynthesis. Antimicrob Agents Chemother. 1975; 7(6): 856–6. doi: 10.1128/AAC.7.6.856.Müller F, Ackermann P, Margot P. Fungicides, Agricultural, 2. Individual fungicides. ullmann’s encyclopedia of industrial chemistry. 2012. Weinheim: Wiley-VCH. doi: 10.1002/14356007.o12_o06.Müller F, Ackermann P, Margot P. Fungicides, Agricultural, 2. Individual fungicides. ullmann’s encyclopedia of industrial chemistry. 2012. Weinheim: Wiley-VCH. doi: 10.1002/14356007.o12_o06.Schneider-Poetsch T, Ju J, Eyler DE, Dang Y, Bhat S, Merrick WC, et al. Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat Chem Biol. 2010; 6 (3): 209–217. doi: 10.1038/nchembio.304.Schneider-Poetsch T, Ju J, Eyler DE, Dang Y, Bhat S, Merrick WC, et al. Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat Chem Biol. 2010; 6 (3): 209–217. doi: 10.1038/nchembio.304.Pizzol MD, Freitas EC, Locatelli C, Guareze F, Reginatto P, Machado G, et al. Drug Des Devel Ther. 2021; 15: 2091–2098. doi: 10.2147/DDDT.S298059.Pizzol MD, Freitas EC, Locatelli C, Guareze F, Reginatto P, Machado G, et al. Drug Des Devel Ther. 2021; 15: 2091–2098. doi: 10.2147/DDDT.S298059.DeFalco AP. Cycloheximide. Encyclopedia of Toxicology (Fourth Edition). 2024; 3: 411–415. doi: 10.1016/B978-0-12-824315-2.00626-6.DeFalco AP. Cycloheximide. Encyclopedia of Toxicology (Fourth Edition). 2024; 3: 411–415. doi: 10.1016/B978-0-12-824315-2.00626-6.Syuhada NH, Merican F, Zaki S, Broady PA, Convey P, Muangmai N. Strong and widespread cycloheximide resistance in Stichococcus-like eukaryotic algal taxa. Sci. Rep., 2022; 12: 1080–1089. doi: 10.1038/s41598022-05116-y.Syuhada NH, Merican F, Zaki S, Broady PA, Convey P, Muangmai N. Strong and widespread cycloheximide resistance in Stichococcus-like eukaryotic algal taxa. Sci. Rep., 2022; 12: 1080–1089. doi: 10.1038/s41598022-05116-y.McCormick SP, Stanley AM, Stover NA, Alexander NJ. Trichothecenes: from simple to complex mycotoxins. Toxins. 2011; 3: 802–814. doi: 10.3390/toxins3070802.McCormick SP, Stanley AM, Stover NA, Alexander NJ. Trichothecenes: from simple to complex mycotoxins. Toxins. 2011; 3: 802–814. doi: 10.3390/toxins3070802.Буракаева А. Д. Микофильные грибы в биотехнологии фунгицидных препаратов. Вестник ОГУ. 2014 (6): 98–103.Burakaeva AD. Mikofilnye griby v biotekhnologii fungitsidnykh preparatov. Vestnik OGU. 2014 (6): 98–103. (in Russ.)].Wang W, Zhu Y, Abraham N, Li X-Z, Kimber M, Zhou T. The ribosomebinding mode of trichothecene mycotoxins rationalizes their structure — activity relationships. Int J Mol Sci. 2021; 22: 1604–1620. doi: 10.3390/ijms22041604Wang W, Zhu Y, Abraham N, Li X-Z, Kimber M, Zhou T. The ribosomebinding mode of trichothecene mycotoxins rationalizes their structure — activity relationships. Int J Mol Sci. 2021; 22: 1604–1620. doi: 10.3390/ijms22041604Егоров Н. С. Основы учения об антибиотиках. Классический университетский учебник. Изд. МГУ, Наука. 2004; 528.Egorov NS. Osnovy ucheniya ob antibiotikakh. Klassicheskij universitetskij uchebnik. Izd. MGU, Nauka. 2004; 528. (in Russ.)].Ye W, Zhu M, Cen Y, Liu T, Li H, Liu. H, Zhang W. The excavation of novel toxin-resistance proteins against trichothecenes toxins in Paramyrothecium roridum. Int J Biol Macromol. 2021; 192: 369–378. doi: 10.1016/j.ijbiomac.2021.09.185.Ye W, Zhu M, Cen Y, Liu T, Li H, Liu. H, Zhang W. The excavation of novel toxin-resistance proteins against trichothecenes toxins in Paramyrothecium roridum. Int J Biol Macromol. 2021; 192: 369–378. doi: 10.1016/j.ijbiomac.2021.09.185.Beekman AM, Barrow RA. Fungal metabolites as pharmaceuticals. Australian Journal of Chemistry. 2014; 67: 827–843. doi: 10.1071/CH13639.Beekman AM, Barrow RA. Fungal metabolites as pharmaceuticals. Australian Journal of Chemistry. 2014; 67: 827–843. doi: 10.1071/CH13639.Lana AJD, Pippi B, Carvalho AR, Moraes RC, Kaiser S, Ortega GG, et al. In vitro additive effect on griseofulvin and terbinafine combinations against multidrug-resistant dermatophytes. Braz J Pharm Sci. 2018; 54 (2): e17149. doi: 10.1590/s2175-97902018000217149.Lana AJD, Pippi B, Carvalho AR, Moraes RC, Kaiser S, Ortega GG, et al. In vitro additive effect on griseofulvin and terbinafine combinations against multidrug-resistant dermatophytes. Braz J Pharm Sci. 2018; 54 (2): e17149. doi: 10.1590/s2175-97902018000217149.Polak-Sliwinska M, Paszczyk B. Trichothecenes in food and feed, relevance to human and animal health and methods of detection: a systematic review. Molecules. 2021; 26 (2): 454–475. doi: 10.3390/molecules26020454.Polak-Sliwinska M, Paszczyk B. Trichothecenes in food and feed, relevance to human and animal health and methods of detection: a systematic review. Molecules. 2021; 26 (2): 454–475. doi: 10.3390/molecules26020454.Nardoni S, Mugnaini L, Papini R, Fiaschi M, Mancianti F. Canine and feline dermatophytosis due to Microsporum gypseum: a retrospective study of clinical data and therapy outcome with griseofulvin. J Mycol Med. 2013; 23 (3): 164–167. doi: 10.1016/j.mycmed.2013.05.005.Nardoni S, Mugnaini L, Papini R, Fiaschi M, Mancianti F. Canine and feline dermatophytosis due to Microsporum gypseum: a retrospective study of clinical data and therapy outcome with griseofulvin. J Mycol Med. 2013; 23 (3): 164–167. doi: 10.1016/j.mycmed.2013.05.005.Petersen AB, Rønnest MH, Larsen TO, Clausen MH. The chemistry of griseofulvin. Chem Rev. 2014; 114 (24): 12088–12107. doi: 10.1021/cr400368e.Petersen AB, Rønnest MH, Larsen TO, Clausen MH. The chemistry of griseofulvin. Chem Rev. 2014; 114 (24): 12088–12107. doi: 10.1021/cr400368e.Даниленко Р. У., Хисматуллина З. Р., Мухамадеева О. Р. Формы зооантропонозной трихофитии, резистентные к терапии гризеофульвином. Аллергология и дерматология. 2015; 108 (7): 39–41.Danilenko RU, Khismatullina ZR, Mukhamadeeva OR. GriseofulvinResistant Forms of Tinea Anthropozoonosis. Allergologiya i Dermatologiya. 2015; 108 (7): 39–41. (in Russ.)].https://vettorg.ru/catalog/item-1743.htmlhttps://vettorg.ru/catalog/item-1743.htmlhttps://www.vidal.ru/drugs/griseofulvin__3692https://www.vidal.ru/drugs/griseofulvin__3692Parrino B, Schillaci D, Carnevale I, Giovannetti E, Diana P, Cirrincione G, Cascioferro S. Synthetic small molecules as anti-biofilm agents in the struggle against antibiotic resistance. Eur J Med Chem. 2019; 161: 154–178. doi: 10.1016/j.ejmech.2018.10.036.Parrino B, Schillaci D, Carnevale I, Giovannetti E, Diana P, Cirrincione G, Cascioferro S. Synthetic small molecules as anti-biofilm agents in the struggle against antibiotic resistance. Eur J Med Chem. 2019; 161: 154–178. doi: 10.1016/j.ejmech.2018.10.036.Решение комиссии Европейского Союза от 23 июня 2023 г. N 70 О внесении изменений в некоторые решения комиссии таможенного союза и совета евразийской экономической комиссии». https://www.alta.ru/tamdoc/18kr0028/ от 17.03.2018Reshenie komissii Evropejskogo Soyuza ot 23 iyunya 2023 g. N 70 O vnesenii izmenenij v nekotorye resheniya komissii tamozhennogo soyuza i soveta evrazijskoj ekonomicheskoj komissii». (in Russ.)]. https://www.alta.ru/tamdoc/18kr0028/ от 17.03.2018Олсуфьева Е. Н., Янковская В. С., Дунченко Н. И. Обзор рисков контаминации антибиотиками молочной продукции. Антибиотики и химиотер. 2022; 67(7–8): 82-96 (In Russ.). doi: https://doi.org/10.37489/02352990-2022-67-7-8-82-96.Olsufyeva EN, Yankovskaya VS, Dunchenko NI. Review of risks of antibiotic contamination of dairy products. Antibiot Khimioter = Antibiotics and Chemotherapy. 2022; 67 (7–8): 82–96. doi: https://doi.org/10.37489/0235-2990-2022-67-7-8-82-96.]Malagón-Rojas JN, Parra-Barrera EL, Lagos L. From environment to clinic: the role of pesticides in antimicrobial resistance. Rev Panam Salud Publica. 2020; 44: e44–e48. doi: 10.26633/RPSP.2020.44.Malagón-Rojas JN, Parra-Barrera EL, Lagos L. From environment to clinic: the role of pesticides in antimicrobial resistance. Rev Panam Salud Publica. 2020; 44: e44–e48. doi: 10.26633/RPSP.2020.44.

The authors declare that there are no conflicts of interest present.