Bacteriocins: Curial guardians of gastrointestinal tract.
antimicrobial peptides
defensive function
digestive system
distribution
mode of action
Journal
Comprehensive reviews in food science and food safety
ISSN: 1541-4337
Titre abrégé: Compr Rev Food Sci Food Saf
Pays: United States
ID NLM: 101305205
Informations de publication
Date de publication:
Jan 2024
Jan 2024
Historique:
revised:
05
12
2023
received:
30
08
2023
accepted:
14
12
2023
medline:
29
1
2024
pubmed:
29
1
2024
entrez:
29
1
2024
Statut:
ppublish
Résumé
The human gastrointestinal (GI) tract microbiome secretes various metabolites that play pivotal roles in maintaining host physiological balance and influencing disease progression. Among these metabolites, bacteriocins-small, heat-stable peptides synthesized by ribosomes-are notably prevalent in the GI region. Their multifaceted benefits have garnered significant interest in the scientific community. This review comprehensively explores the methods for mining bacteriocins (traditional separation and purification, bioinformatics, and artificial intelligence), their effects on the stomach and intestines, and their complex bioactive mechanisms. These mechanisms include flora regulation, biological barrier restoration, and intervention in epithelial cell pathways. By detailing each well-documented bacteriocin, we reveal the diverse ways in which bacteriocins interact with the GI environment. Moreover, the future research direction is prospected. By further studying the function and interaction of intestinal bacteriocins, we can discover new pharmacological targets and develop drugs targeting intestinal bacteriocins to regulate and improve human health. It provides innovative ideas and infinite possibilities for further exploration, development, and utilization of bacteriocins. The inevitable fact is that the continuously exploration of bacteriocins is sure to bring the promising future for demic GI health understanding and interference strategy.
Identifiants
pubmed: 38284593
doi: 10.1111/1541-4337.13292
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1-27Subventions
Organisme : Natural Science Foundation of Zhejiang Province
ID : LR22C200005
Organisme : National Natural Science Foundation of China
ID : 32272301
Organisme : National Natural Science Foundation of China
ID : U20A2066
Organisme : Key R&D Project of Zhejiang Province
ID : 2020C04002
Informations de copyright
© 2024 Institute of Food Technologists®.
Références
Ahmad, V., Jamal, Q. M. S., Siddiqui, M. U., Shukla, A. K., Alzohairy, M. A., Al Karaawi, M. A., & Kamal, M. A. (2017). Methods of screening-purification and antimicrobial potentialities of bacteriocin in health care. Current Drug Metabolism, 18, 814-830. https://doi.org/10.2174/1389200218666170116111309,
Al-Shabib, N. A., Husain, F. M., Ahmad, I., Khan, M. S., Khan, R. A., & Khan, J. M. (2017). Rutin inhibits mono and multi-species biofilm formation by foodborne drug resistant Escherichia coli and Staphylococcus aureus. Food Control, 79, 325-332.
Alam, A., Leoni, G., Quiros, M., Wu, H., Desai, C., Nishio, H., Jones, R. M., Nusrat, A., & Neish, A. S. (2016). The microenvironment of injured murine gut elicits a local pro-restitutive microbiota. Nature Microbiology, 1, 15021. https://doi.org/10.1038/nmicrobiol.2015.21
Alessandra De, G., Federica, B., Matilde, F., Paola, F., Guido, S., & Patrizia Di, G. (2019). Identification of a bacteriocin-like compound from Lactobacillus plantarum with antimicrobial activity and effects on normal and cancerogenic human intestinal cells. Applied Microbiology and Biotechnology Express, 9, 88. https://doi.org/10.1186/s13568-019-0813-6
Ankaiah, D., Palanichamy, E., Perumal, V., Ayyanna, R., & Venkatesan, A. (2018). Probiotic characterization of Enterococcus faecium por1: Cloning, over expression of Enterocin-A and evaluation of antibacterial, anti-cancer properties. Journal of Functional Foods, 38, 280-292.
Anna Rita, B., Simona, S., Emilia, C., Monica, B., Silvia Di, A., Tohru, Y., Craig, W. B., & Salvatore, C. (2011). Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy. International Journal of Nanomedicine, 6, 3011-3019. https://doi.org/10.2147/ijn.s26155
Chelliah, R., Saravanakumar, K., Daliri, E. B.-M., Kim, J.-H., Lee, J.-K., Jo, H., Kim, S.-H., Ramakrishnan, S. R., Madar, I. H., Wei, S., Rubab, M., Barathikannan, K., Ofosu, F. K., Subin, H., Eun-ji, P., Yeong, J. D., Elahi, F., Wang, M.-H., Park, J. H., … Oh, D.-H. (2020). Unveiling the potentials of bacteriocin (pediocin l50) from Pediococcus acidilactici with antagonist spectrum in a Caenorhabditis elegans model. International Journal of Biological Macromolecules, 143, 555-572. https://www.sciencedirect.com/science/article/pii/S0141813019338255
Artis, D. (2008). Epithelial-cell recognition of commensal bacteria and maintenance of immune homeostasis in the gut. Nature Reviews Immunology, 8(6), 411-420. https://doi.org/10.1038/nri2316
Babasaki, K., Takao, T., Shimonishi, Y., & Kurahashi, K. (1985). Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: Isolation, structural analysis, and biogenesis. Journal of Biochemistry, 98(3), 585-603. https://pubmed.ncbi.nlm.nih.gov/3936839
Baljinder, K., Neena, G., Atul, S., & Balvir, K. (2013). Effect of the oral intake of probiotic Pediococcus acidilactici BA28 on Helicobacter pylori causing peptic ulcer in C57BL/6 mice models. Applied Biochemistry and Biotechnology, 172, 973-983. https://doi.org/10.1007/s12010-013-0585-4
Balla, E., Dicks, L. M., Du Toit, M., Van Der Merwe, M. J., & Holzapfel, W. H. (2000). Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071. Applied and Environmental Microbiology, 66(4), 1298-1304. https://pubmed.ncbi.nlm.nih.gov/10742203
Baquero, F., Lanza, V. F., Baquero, M. R., Campo, R. D., & Bravo-Vázquez, D. A. (2019). Microcins in Enterobacteriaceae: Peptide antimicrobials in the eco-active intestinal chemosphere. Frontiers in Microbiology, 10, 2261. https://doi.org/10.3389/fmicb.2019.02261
Beaulieu, L. (2004). Production, purification et caracterisation de la pediocine PA-1 naturelle et de ses formes recombinantes: Contribution a la mise en evidence d'une nouvelle activite biologique (French and English text). Universite Laval (Canada).
Begde, D., Bundale, S., Mashitha, P., Rudra, J., Nashikkar, N., & Upadhyay, A. (2011). Immunomodulatory efficacy of nisin-A bacterial lantibiotic peptide. Journal of Peptide Science: An Official Publication of the European Peptide Society, 17(6), 438-444. https://doi.org/10.1002/psc.1341
Bennion, J. R., Sorvillo, F., Wise, M. E., Krishna, S., & Mascola, L. (2008). Decreasing listeriosis mortality in the United States, 1990-2005. Clinical Infectious Diseases: An Official Publication of the Infectious Diseases Society of America, 47(7), 867-874. https://doi.org/10.1086/591131
Bhunia, A. K., Johnson, M. C., Ray, B., & Belden, E. L. (1990). Antigenic property of pediocin AcH produced by Pediococcus acidilactici H. The Journal of Applied Bacteriology, 69, 211-215. https://doi.org/10.1111/j.1365-2672.1990.tb01511.x
Biedermann, L. R. G. (2015). The intestinal microbiota: Its role in health and disease. European Journal of Pediatrics, 174(2), 151-167. https://doi.org/10.1007/s00431-014-2476-2
Bierbaum, G., & Sahl, H. G. (2009). Lantibiotics: Mode of action, biosynthesis and bioengineering. Current Pharmaceutical Biotechnology, 10(1), 2-18. https://pubmed.ncbi.nlm.nih.gov/19149587
Breukink, E., & de Kruijff, B. (2006). Lipid II as a target for antibiotics. Nature Reviews Drug Discovery, 5(4), 321-332. https://pubmed.ncbi.nlm.nih.gov/16531990
Caitriona, M. G., Elaine, M. L., Paula, M. O. C., Órla, O. S., Colin, H., Ross, R. P., & Paul, D. C. (2016). The bacteriocin bactofencin A subtly modulates gut microbial populations. Anaerobe, 40, 41-49. https://doi.org/10.1016/j.anaerobe.2016.05.001
Caruso, R., Lo, B. C., & Núñez, G. (2020). Host-microbiota interactions in inflammatory bowel disease. Nature Reviews Immunology, 20(7), 411-426. https://doi.org/10.1038/s41577-019-0268-7
Cats, A., Kuipers, E. J., Bosschaert, M. A. R., Pot, R. G. J., Vandenbroucke-Grauls, C. M. J. E., & Kusters, J. G. (2003). Effect of frequent consumption of a Lactobacillus casei-containing milk drink in Helicobacter pylori-colonized subjects. Alimentary Pharmacology & Therapeutics, 17, 429-435. https://doi.org/10.1046/j.1365-2036.2003.01452.x
Changzheng, Y., Davies, A., Tzu Tsun, L., Liyan, H., Yusa, H., Yunhan, X., Xinxin, Y., Qian, Y., Peige, S., & Igor, R. (2022). The global prevalence of and factors associated with Helicobacter pylori infection in children: A systematic review and meta-analysis. The Lancet Child & Adolescent Health, 6, 185-194. https://doi.org/10.1016/s2352-4642(21)00400-4
Chelakkot, C., Ghim, J., & Ryu, S. H. (2018). Mechanisms regulating intestinal barrier integrity and its pathological implications. Experimental & Molecular Medicine, 50(8), 1-9. https://doi.org/10.1038/s12276-018-0126-x
Chen, J., Stevenson, D. M., & Weimer, P. J. (2004). Albusin B, a bacteriocin from the ruminal bacterium Ruminococcus albus 7 that inhibits growth of Ruminococcus flavefaciens. Applied and Environmental Microbiology, 70(5), 3167-3170. https://pubmed.ncbi.nlm.nih.gov/15128585
Chhaya, G., Malik, R. K., & Diwas, P. (2018). Purification and characterization of a broad spectrum bacteriocin produced by a selected Lactococcus lactis strain 63 isolated from Indian dairy products. Journal of Food Science and Technology -, 55, 1-10. https://doi.org/10.1007/s13197-018-3298-4
Chikindas, M. L., Weeks, R., Drider, D., Chistyakov, V. A., & Dicks, L. M. (2018). Functions and emerging applications of bacteriocins. Current Opinion in Biotechnology, 49, 23-28. https://doi.org/10.1016/j.copbio.2017.07.011
Choi, H. J., Cheigh, C. I., Kim, S. B., & Pyun, Y. R. (2000). Production of a nisin-like bacteriocin by Lactococcus lactis subsp. lactis A164 isolated from Kimchi. Journal of Applied Microbiology, 88, 563-571. https://doi.org/10.1046/j.1365-2672.2000.00976.x
Cimermancic, P., Medema, M. H., Claesen, J., Kurita, K., Wieland Brown, L. C., Mavrommatis, K., Pati, A., Godfrey, P. A., Koehrsen, M., Clardy, J., Birren, B. W., Takano, E., Sali, A., Linington, R. G., & Fischbach, M. A. (2014). Insights into secondary metabolism from a global analysis of prokaryotic biosynthetic gene clusters. Cell, 158(2), 412-421. https://doi.org/10.1016/j.cell.2014.06.034
Collin, F., & Maxwell, A. (2019). The microbial toxin microcin b17: Prospects for the development of new antibacterial agents. Journal of Molecular Biology, 431(18), 3400-3426. https://doi.org/10.1016/j.jmb.2019.05.050
Concepción Curbelo, J. L., & Garcia Diaz, M. E. (2000). The purified colicin S8 is a multimeric protein. International Microbiology: The Official Journal of the Spanish Society for Microbiology, 3(4), 239-245. https://pubmed.ncbi.nlm.nih.gov/11334308
Coronelli, C., Tamoni, G., & Lancini, G. C. (1976). Gardimycin, a new antibiotic from Actinoplanes. II. Isolation and preliminary characterization. The Journal of Antibiotics, 29(5), 507-510. https://pubmed.ncbi.nlm.nih.gov/956038
Corr, S. C., Li, Y., Riedel, C. U., O'Toole, P. W., Hill, C., & Gahan, C. G. M. (2007). Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118. Proceedings of the National Academy of Sciences of the United States of America, 104(18), 7617-7621. https://pubmed.ncbi.nlm.nih.gov/17456596
Crost, E. H., Ajandouz, E. H., Villard, C., Geraert, P. A., Puigserver, A., & Fons, M. (2011). Ruminococcin C, a new anti-Clostridium perfringens bacteriocin produced in the gut by the commensal bacterium Ruminococcus gnavus E1. Biochimie, 93(9), 1487-1494. https://doi.org/10.1016/j.biochi.2011.05.001
Dabard, J., Bridonneau, C., Phillipe, C., Anglade, P., Molle, D., Nardi, M., Ladiré, M., Girardin, H., Marcille, F., Gomez, A., & Fons, M. (2001). Ruminococcin A, a new lantibiotic produced by a Ruminococcus gnavus strain isolated from human feces. Applied and Environmental Microbiology, 67(9), 4111-4118. https://pubmed.ncbi.nlm.nih.gov/11526013
de Pablo, M. A., Gaforio, J. J., Gallego, A. M., Ortega, E., Gálvez, A. M., & Alvarez de Cienfuegos López, G. (1999). Evaluation of immunomodulatory effects of nisin-containing diets on mice. FEMS Immunology and Medical Microbiology, 24(1), 35-42. https://pubmed.ncbi.nlm.nih.gov/10340710
del Campo, R., Tenorio, C., Jiménez-Díaz, R., Rubio, C., Gómez-Lus, R., Baquero, F., & Torres, C. (2001). Bacteriocin production in vancomycin-resistant and vancomycin-susceptible Enterococcus isolates of different origins. Antimicrobial Agents and Chemotherapy, 45(3), 905-912. https://pubmed.ncbi.nlm.nih.gov/11181378
Destoumieux-Garzón, D., Duquesne, S., Peduzzi, J., & Rebuffat, S. (2007). Microcins, gene-encoded antibacterial peptides from enterobacteria. Cheminform, 24(4), 708-734. https://doi.org/10.1039/b516237h
Dimitrijević, R., Stojanović, M., Zivković, I., Petersen, A., Jankov, R. M., Dimitrijević, L., & Gavrović-Jankulović, M. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. Journal of Applied Microbiology, 107(6), 2108-2115. https://doi.org/10.1111/j.1365-2672.2009.04539.x
Dobson, A., Cotter, P. D., Ross, R. P., & Hill, C. (2012). Bacteriocin production: A probiotic trait? Applied and Environmental Microbiology, 78(1), 1-6. https://doi.org/10.1128/AEM.05576-11
Dong Gun, L., Kyung-Soo, H., Yoonkyung, P., Hai-Young, K., Weontae, L., Sung-Chul, L., Youn-Kyung, S., & Cheol-Hee, C. (2005). Functional and structural characteristics of anticancer peptide Pep27 analogues. Cancer Cell International, 5, 21. https://doi.org/10.1186/1475-2867-5-21
Donia, M. S., Cimermancic, P., Schulze, C. J., Wieland Brown, L. C., Martin, J., Mitreva, M., Clardy, J., Linington, R. G., & Fischbach, M. A. (2014). A systematic analysis of biosynthetic gene clusters in the human microbiome reveals a common family of antibiotics. Cell, 158(6), 1402-1414. https://doi.org/10.1016/j.cell.2014.08.032
Drissi, F., Buffet, S., Raoult, D., & Merhej, V. (2015). Common occurrence of antibacterial agents in human intestinal microbiota. Frontiers in Microbiology, 6, 441. https://doi.org/10.3389/fmicb.2015.00441
Farkas-Himsley, H., Hill, R., Rosen, B., Arab, S., & Lingwood, C. A. (1995). The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1. Proceedings of the National Academy of Sciences of the United States of America, 92, 6996-7000. https://doi.org/10.1073/pnas.92.15.6996
Farkas-Himsley, H., & Yu, H. (1985). Purified colicin as cytotoxic agent of neoplasia: Comparative study with crude colicin. Cytobios, 42(167-168), 193-207. https://pubmed.ncbi.nlm.nih.gov/3891240
Flint, H. J., Scott, K. P., Louis, P., & Duncan, S. H. (2012). The role of the gut microbiota in nutrition and health. Nature Reviews Gastroenterology & Hepatology, 9(10), 577-589. https://doi.org/10.1038/nrgastro.2012.156
Fuchs, T. A., Abed, U., Goosmann, C., Hurwitz, R., Schulze, I., Wahn, V., Weinrauch, Y., Brinkmann, V., & Zychlinsky, A. (2007). Novel cell death program leads to neutrophil extracellular traps. The Journal of Cell Biology, 176(2), 231-241. https://pubmed.ncbi.nlm.nih.gov/17210947
Funderburg, N., Lederman, M. M., Feng, Z., Drage, M. G., Jadlowsky, J., Harding, C. V., Weinberg, A., & Sieg, S. F. (2007). Human-defensin-3 activates professional antigen-presenting cells via Toll-like receptors 1 and 2. Proceedings of the National Academy of Sciences of the United States of America, 104(47), 18631-18635. https://pubmed.ncbi.nlm.nih.gov/18006661
Fung, T. C., Olson, C. A., & Hsiao, E. Y. (2017). Interactions between the microbiota, immune and nervous systems in health and disease. Nature Neuroscience, 20(2), 145-155. https://doi.org/10.1038/nn.4476
Gao, M., Zhou, J., Su, Z., & Huang, Y. (2017). Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy. Protein Science: A Publication of the Protein Society, 26(12), 2334-2341. https://doi.org/10.1002/pro.3310
Garg, N., Tang, W., Goto, Y., Nair, S. K., & van der Donk, W. A. (2012). Lantibiotics from Geobacillus thermodenitrificans. Proceedings of the National Academy of Sciences of the United States of America, 109(14), 5241-5246. https://doi.org/10.1073/pnas.1116815109
Gaspar, C., Donders, G. G., Palmeira-de-Oliveira, R., Queiroz, J. A., Tomaz, C., Martinez-de-Oliveira, J., & Palmeira-de-Oliveira, A. (2018). Bacteriocin production of the probiotic Lactobacillus acidophilus KS400. Applied Microbiology and Biotechnology Express, 8(1), 153. https://doi.org/10.1186/s13568-018-0679-z
Ge, J., Sun, Y., Xin, X., Wang, Y., & Ping, W. (2016). Purification and partial characterization of a novel bacteriocin synthesized by Lactobacillus paracasei HD1-7 isolated from Chinese sauerkraut juice. Scientific Reports, 6, 19366. https://doi.org/10.1038/srep19366
Gilbert, C., Claude, F., & Denis, S. (2008). Antineoplastic properties of bacteriocins: Revisiting potential active agents. American Journal of Clinical Oncology, 31, 399-404. https://doi.org/10.1097/coc.0b013e31815e456d
Gisele, R., Gislaine Greice Oliveira, S., Danieli Fernanda, B., Harry Morales, D., Simoni Campos, D., & Octávio Luiz, F. (2019). Bacterial proteinaceous compounds with multiple activities toward cancers and microbial infection. Frontiers in Microbiology, 10, 1690. https://doi.org/10.3389/fmicb.2019.01690
Gratia, A. (1925). Sur un remarquable exemple d'antagonisme entre deux souches de colibacille. Comptes Rendus des Seances de la Societe de Biologie et de Ses Filiales, 93, 1040-1041.
Hadis, F., Mahmood, S., Davoud, E., Rezvan, M., & Javad Amini, M. (2021). Anticancer effect of enterocin A-colicin E1 fusion peptide on the gastric cancer cell. Probiotics and Antimicrobial Proteins, 13, 1443-1451. https://doi.org/10.1007/s12602-021-09770-y
Hannah, N. B., Ryan, J. R., Joshua, G., Rashi, S., Miljan, K., Samuel, A. K., Wesley, H., Nupur, K. D., Anthony, A., Sumeet, S., Shannon, L. M., Peter, K. T., Eric, R. F., Costas, A. L., Steven, P. G., Joseph, D. M., & Yatrik, M. S. (2021). Reuterin in the healthy gut microbiome suppresses colorectal cancer growth through altering redox balance. Cancer Cell, 40, 185-200. https://doi.org/10.1016/j.ccell.2021.12.001
Harkness, R. E., & Olschläger, T. (1991). The biology of colicin M. FEMS Microbiology Reviews, 8(1), 27-41. https://pubmed.ncbi.nlm.nih.gov/1931137
Hatziioanou, D., Gherghisan-Filip, C., Saalbach, G., Horn, N., Wegmann, U., Duncan, S. H., Flint, H. J., Mayer, M. J., & Narbad, A. (2017). Discovery of a novel lantibiotic nisin O from Blautia obeum A2-162, isolated from the human gastrointestinal tract. Microbiology (Reading, England), 163(9), 1292-1305. https://doi.org/10.1099/mic.0.000515
Hauge, H. H., Mantzilas, D., Moll, G. N., Konings, W. N., Driessen, A. J., Eijsink, V. G., & Nissen-Meyer, J. (1998). Plantaricin A is an amphiphilic alpha-helical bacteriocin-like pheromone which exerts antimicrobial and pheromone activities through different mechanisms. Biochemistry, 37(46), 16026-16032. https://pubmed.ncbi.nlm.nih.gov/9819195
Heeney, D. D., Zhai, Z., Bendiks, Z., Barouei, J., Martinic, A., Slupsky, C., & Marco, M. L. (2019). Lactobacillus plantarum bacteriocin is associated with intestinal and systemic improvements in diet-induced obese mice and maintains epithelial barrier integrity in vitro. Gut Microbes, 10(3), 382-397. https://doi.org/10.1080/19490976.2018.1534513n
Heilbronner, S., Krismer, B., Brötz-Oesterhelt, H., & Peschel, A. (2021). The microbiome-shaping roles of bacteriocins. Nature Reviews Microbiology, 19(11), 726-739. https://doi.org/10.1038/s41579-021-00569-w
Heng, N. C. K., Wescombe, P. A., Burton, J. P., Jack, R. W., & Tagg, J. R. (2007). The diversity of bacteriocins in gram-positive bacteria. In M. A. Riley & M. A. Chavan (Eds.), Bacteriocins: Ecology and evolution (pp. 45-92). Springer. https://doi.org/10.1007/978-3-540-36604-1_4
Herrero, M., & Moreno, F. (1986). Microcin B17 blocks DNA replication and induces the SOS system in Escherichia coli. Journal of General Microbiology, 132(2), 393-402. https://pubmed.ncbi.nlm.nih.gov/3086495
Herschman, H. R., & Helinski, D. R. (1967). Purification and characterization of colicin E2 and colicin E3. The Journal of Biological Chemistry, 242(22), 5360-5368. https://pubmed.ncbi.nlm.nih.gov/4965137
Hetz, C., Bono, M. R., Barros, L. F., & Lagos, R. (2002). Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines. Proceedings of the National Academy of Sciences of the United States of America, 99, 2696-2701. https://doi.org/10.1073/pnas.052709699
Holo, H., Nilssen, O., & Nes, I. F. (1991). Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene. Journal of Bacteriology, 173(12), 3879-3887. https://pubmed.ncbi.nlm.nih.gov/1904860
Hu, J., Ma, L., Nie, Y., Chen, J., Zheng, W., Wang, X., Xie, C., Zheng, Z., Wang, Z., Yang, T., Shi, M., Chen, L., Hou, Q., Niu, Y., Xu, X., Zhu, Y., Zhang, Y., Wei, H., & Yan, X. (2018). A microbiota-derived bacteriocin targets the host to confer diarrhea resistance in early-weaned piglets. Cell Host & Microbe, 24(6), 817-832. https://doi.org/10.1016/j.chom.2018.11.006
Huang, F., Teng, K., Liu, Y., Cao, Y., Wang, T., Ma, C., Zhang, J., & Zhong, J. (2021). Bacteriocins: Potential for human health. Oxidative Medicine and Cellular Longevity, 2021, 5518825. https://doi.org/10.1155/2021/5518825
Hyeran, N., Misun, H., On, B., & Yeonhee, L. (2002). Effect of Weissella confusa strain PL9001 on the adherence and growth of Helicobacter pylori. Applied and Environmental Microbiology, 68, 4642-4645. https://doi.org/10.1128/aem.68.9.4642-4645.2002
Ishida, K., Nakagawa, H., & Murakami, M. (2000). Microcyclamide, a cytotoxic cyclic hexapeptide from the cyanobacterium Microcystis aeruginosa. Journal of Natural Products, 63(9), 1315-1317. https://pubmed.ncbi.nlm.nih.gov/11000050
James, K. Y. H., Wan Ying, L., Wee Khoon, N., Michael, M. Y. S., Fox, E. U., Divine, T., Peter, M., David, Y. G., Vincent, W. S. W., Justin, C. Y. W., Francis, K. L. C., Joseph, J. Y. S., Gilaad, G. K., & Siew, C. N. (2017). Global prevalence of Helicobacter pylori infection: Systematic review and meta-analysis. Gastroenterology, 153, 420-429. https://doi.org/10.1053/j.gastro.2017.04.022
Jesaitis, M. A. (1970). The nature of colicin K from Proteus mirabilis. The Journal of Experimental Medicine, 131(5), 1016-1038. https://pubmed.ncbi.nlm.nih.gov/4986216
John, L. M. (2008). Managing potentially resectable metastatic colon cancer. Gastrointestinal cancer research: GCR, 2(4 Suppl 2), S23.
Johnson, E. M., Jung, D. Y.-G., Jin, D. Y.-Y., Jayabalan, D. R., Yang, D. S. H., & Suh, J. W. (2018). Bacteriocins as food preservatives: Challenges and emerging horizons. Critical Reviews in Food Science and Nutrition, 58(16), 2743-2767. https://doi.org/10.1080/10408398.2017.1340870
Kabuki, T., Saito, T., Kawai, Y., Uemura, J., & Itoh, T. (1997). Production, purification and characterization of reutericin 6, a bacteriocin with lytic activity produced by Lactobacillus reuteri LA6. International Journal of Food Microbiology, 34(2), 145-156. https://pubmed.ncbi.nlm.nih.gov/9039561
Kalmokoff, M. L., & Teather, R. M. (1997). Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: Evidence in support of the widespread occurrence of bacteriocin-like activity among ruminal isolates of B. fibrisolvens. Applied and Environmental Microbiology, 63(2), 394-402. https://pubmed.ncbi.nlm.nih.gov/9023920
Karczewska, E., Wojtas, I., Sito, E., Trojanowska, D., Budak, A., Zwolinska-Wcislo, M., & Wilk, A. (2010). Assessment of co-existence of Helicobacter pylori and Candida fungi in diseases of the upper gastrointestinal tract. Journal of Physiology and Pharmacology: An Official Journal of the Polish Physiological Society, 60, 33-39.
Karpiński, T. M., & Adamczak, A. (2018). Anticancer activity of bacterial proteins and peptides. Pharmaceutics, 10(2), 54. https://doi.org/10.3390/pharmaceutics10020054
Kawai, Y., Saito, T., Kitazawa, H., & Itoh, T. (1998). Gassericin A; an uncommon cyclic bacteriocin produced by Lactobacillus gasseri LA39 linked at N- and C-terminal ends. Bioscience, Biotechnology, and Biochemistry, 62(12), 2438-2440. https://pubmed.ncbi.nlm.nih.gov/9972271
Keikha, M., & Karbalaei, M. (2021). Probiotics as the live microscopic fighters against Helicobacter pylori gastric infections. BMC Gastroenterology, 21(1), 388. https://doi.org/10.1186/s12876-021-01977-1
Kemperman, R., Kuipers, A., Karsens, H., Nauta, A., Kuipers, O., & Kok, J. (2003). Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574. Applied and Environmental Microbiology, 69(3), 1589-1597. https://pubmed.ncbi.nlm.nih.gov/12620847
Kimberly, D. M., Leticia, N., Angela, B. M., Julia, H. R., Yabroff, K. R., Catherine, M. A., Ahmedin, J., Joan, L. K., & Rebecca, L. S. (2019). Cancer treatment and survivorship statistics, 2019. CA: A Cancer Journal for Clinicians, 69, 363-385. https://doi.org/10.3322/caac.21565
Klaenhammer, T. R. (1993). Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiology Reviews, 12(1-3), 39-85. https://pubmed.ncbi.nlm.nih.gov/8398217
Kommineni, S., Bretl, D. J., Lam, V., Chakraborty, R., Hayward, M., Simpson, P., Cao, Y., Bousounis, P., Kristich, C. J., & Salzman, N. H. (2015). Bacteriocin production augments niche competition by enterococci in the mammalian gastrointestinal tract. Nature, 526(7575), 719-722. https://doi.org/10.1038/nature15524
Lagos, R., Tello, M., Mercado, G., García, V., & Monasterio, O. (2009). Antibacterial and antitumorigenic properties of microcin E492, a pore-forming bacteriocin. Current Pharmaceutical Biotechnology, 10, 74-85. https://doi.org/10.2174/138920109787048643
Laviña, M., Gaggero, C., & Moreno, F. (1990). Microcin H47, a chromosome-encoded microcin antibiotic of Escherichia coli. Journal of Bacteriology, 172(11), 6585-6588. https://pubmed.ncbi.nlm.nih.gov/2228975
Lee, H., Churey, J. J., & Worobo, R. W. (2009). Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361. FEMS Microbiology Letters, 299(2), 205-213. https://doi.org/10.1111/j.1574-6968.2009.01749.x
Lee, I. C., van Swam, I. I., Boeren, S., Vervoort, J., Meijerink, M., Taverne, N., Starrenburg, M., Bron, P. A., & Kleerebezem, M. (2020). Lipoproteins contribute to the anti-inflammatory capacity of WCFS1. Frontiers in Microbiology, 11, 1822. https://doi.org/10.3389/fmicb.2020.01822
Lee, J.-H., Karamychev, V. N., Kozyavkin, S. A., Mills, D., Pavlov, A. R., Pavlova, N. V., Polouchine, N. N., Richardson, P. M., Shakhova, V. V., Slesarev, A. I., Weimer, B., & O'Sullivan, D. J. (2008). Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth. BMC Genomics, 9, 247. https://doi.org/10.1186/1471-2164-9-247
Leroy, F., & De Vuyst, L. (2004). Lactic acid bacteria as functional starter cultures for the food fermentation industry. Trends in Food Science & Technology, 15(2), 67-78. https://doi.org/10.1016/j.tifs.2003.09.004
Levy, J. (2000). The effects of antibiotic use on gastrointestinal function. American Journal of Gastroenterology, 95(S1), S8-S10. https://doi.org/10.1016/Sooo2-9270(99)00808-4
Li, Q., Montalban-Lopez, M., & Kuipers, O. P. (2018). Increasing the antimicrobial activity of nisin-based lantibiotics against gram-negative pathogens. Applied and Environmental Microbiology, 84(12), e00052-18. https://doi.org/10.1128/AEM.00052-18
Liang, Y., Yan, J., Chen, Z., Gu, Q., & Li, P. (2022). Antibacterial effects of bacteriocin PLNC8 against Helicobacter pylori and its potential mechanism of action. Foods, 11(9), 1235. https://doi.org/10.3390/foods11091235
Lim, E.-S. (2015). Purification and characterization of two bacteriocins from Lactobacillus brevis BK11 and Enterococcus faecalis BK61 showing anti- Helicobacter pylori activity. Applied Biological Chemistry, 58, 703-714. https://doi.org/10.1007/s13765-015-0094-y
Lishay, P., Tamar, A.-M., Asaf, S., Deborah, N., Amjad, S., Tanya, F.-L., Olga, Y., Batya, I., Jawad, A., Naseem, M., Aviram, N., Judith, S., Einav, Y.-S., Falk, P., Jörg, V., Ofer, M., Zvi, G., Ravid, S., & Gilad, B. (2020). Breast cancer colonization by Fusobacterium nucleatum accelerates tumor growth and metastatic progression. Nature Communications, 11(1), 3259. https://doi.org/10.1038/s41467-020-16967-2
Liu, L., Hao, T., Xie, Z., Horsman, G. P., & Chen, Y. (2016). Genome mining unveils widespread natural product biosynthetic capacity in human oral microbe Streptococcus mutans. Scientific Reports, 6, 37479. https://doi.org/10.1038/srep37479
Lorenzo, V. (1984). Isolation and characterization of microcin E 492 from Klebsiella pneumoniae. Archives of Microbiology, 139, 72-75.
Loris Riccardo, L., Maria Ernestina, G., Angela, S., Franco, S., Antonio, G., & Giovanni, C. (2019). Bacteriocins and bacteriophages: Therapeutic weapons for gastrointestinal diseases? International Journal of Molecular Sciences, 20, 183. https://doi.org/10.3390/ijms20010183
Luciana, C., Jan, M., Edmar, C.-S., & Andréa, M. A. N. (2002). Recent updated aspects of colicins of Enterobacteriaceae. Brazilian Journal of Microbiology, 33, 185-195. https://doi.org/10.1590/s1517-83822002000300001
Luo, L., Yi, L., Chen, J., Liu, B., & Xin, L. (2020). Antibacterial mechanisms of bacteriocin BM1157 against Escherichia coli and Cronobacter sakazakii. Food Control, 123(1-2), 107730.
Ma, Y., Guo, Z., Xia, B., Zhang, Y., Liu, X., Yu, Y., Tang, N., Tong, X., Wang, M., Ye, X., Feng, J., Chen, Y., & Wang, J. (2022). Identification of antimicrobial peptides from the human gut microbiome using deep learning. Nature Biotechnology, 40(6), 921-931. https://doi.org/10.1038/s41587-022-01226-0
Maldonado, A., Jiménez-Díaz, R., & Ruiz-Barba, J. L. (2004). Induction of plantaricin production in Lactobacillus plantarum NC8 after coculture with specific gram-positive bacteria is mediated by an autoinduction mechanism. Journal of Bacteriology, 186(5), 1556-1564. https://pubmed.ncbi.nlm.nih.gov/14973042
Martin-Visscher, L. A., van Belkum, M. J., Garneau-Tsodikova, S., Whittal, R. M., Zheng, J., McMullen, L. M., & Vederas, J. C. (2008). Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307. Applied and Environmental Microbiology, 74(15), 4756-4763. https://doi.org/10.1128/AEM.00817-08
Martínez, B., Zomer, A. L., Rodríguez, A., Kok, J., & Kuipers, O. P. (2007). Cell envelope stress induced by the bacteriocin Lcn972 is sensed by the Lactococcal two-component system CesSR. Molecular Microbiology, 64(2), 473-486. https://pubmed.ncbi.nlm.nih.gov/17493129
McAuliffe, O., Ryan, M. P., Ross, R. P., Hill, C., Breeuwer, P., & Abee, T. (1998). Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential. Applied and Environmental Microbiology, 64(2), 439-445. https://pubmed.ncbi.nlm.nih.gov/9464377
McCormick, J. K., Klaenhammer, T. R., & Stiles, M. E. (1999). Colicin V can be produced by lactic acid bacteria. Letters in Applied Microbiology, 29(1), 37-41. https://pubmed.ncbi.nlm.nih.gov/10432630
Michaudel, C., & Sokol, H. (2020). The gut microbiota at the service of immunometabolism. Cell Metabolism, 32(4), 514-523. https://doi.org/10.1016/j.cmet.2020.09.004
Michiels, J., Dirix, G., Vanderleyden, J., & Xi, C. (2001). Processing and export of peptide pheromones and bacteriocins in gram-negative bacteria. Trends in Microbiology, 9(4), 164-168. https://pubmed.ncbi.nlm.nih.gov/11286880
Millette, M., Cornut, G., Dupont, C., Shareck, F., Archambault, D., & Lacroix, M. (2008). Capacity of human nisin- and pediocin-producing lactic acid bacteria to reduce intestinal colonization by vancomycin-resistant enterococci. Applied and Environmental Microbiology, 74(7), 1997-2003. https://doi.org/10.1128/AEM.02150-07
Mills, S., Ross, R. P., & Hill, C. (2017). Bacteriocins and bacteriophage a narrow-minded approach to food and gut microbiology. FEMS Microbiology Reviews, 41(Supp 1), S129-S153. https://doi.org/10.1093/femsre/fux022
Ming, Z., Meng, Y., Huaiyu, M., Xiaoming, L., Xiuying, T., Shukuan, L., Zhijian, Y., & Robert, M. H. (2006). Targeted therapy with a Salmonella typhimurium leucine-arginine auxotroph cures orthotopic human breast tumors in nude mice. Cancer Research, 66, 7647-7652. https://doi.org/10.1158/0008-5472.can-06-0716
Muriana, P. M., & Klaenhammer, T. R. (1991). Purification and partial characterization of lactacin F, a bacteriocin produced by Lactobacillus acidophilus 11088. Applied and Environmental Microbiology, 57(1), 114-121. https://pubmed.ncbi.nlm.nih.gov/1903624
Ni, J., Wu, G. D., Albenberg, L., & Tomov, V. T. (2017). Gut microbiota and IBD: Causation or correlation? Nature Reviews Gastroenterology & Hepatology, 14(10), 573-584. https://doi.org/10.1038/nrgastro.2017.88
Jamaluddin, N., Stuckey, D. C., Ariff, A. B., & Faizal Wong, F. W. (2017). Novel approaches to purifying bacteriocin: A review. Critical Reviews in Food Science & Nutrition, 58, 2453-2465. https://doi.org/10.1080/10408398.2017.1328658
Norouzi, Z., Salimi, A., Halabian, R., & Fahimi, H. (2018). Nisin, a potent bacteriocin and anti-bacterial peptide, attenuates expression of metastatic genes in colorectal cancer cell lines. Microbial Pathogenesis, 00, 00. https://doi.org/10.1016/j.micpath.2018.07.006
Nyssa, C., Camila Azevedo, A., Ravid, S., Christoph, K. S.-T., & Eran, E. (2021). Microbiome and cancer. Cancer Cell, 39, 1317-1341. https://doi.org/10.1016/j.ccell.2021.08.006
O'Connor, P. M., Kuniyoshi, T. M., Oliveira, R. P., Hill, C., Ross, R. P., & Cotter, P. D. (2020). Antimicrobials for food and feed; a bacteriocin perspective. Current Opinion in Biotechnology, 61, 160-167. https://doi.org/10.1016/j.copbio.2019.12.023
Oh, Y. J., Kim, H. J., Kim, T. S., Yeo, I. H., & Ji, G. E. (2019). Effects of Lactobacillus plantarum pmo 08 alone and combined with chia seeds on metabolic syndrome and parameters related to gut health in high-fat diet-induced obese mice. Journal of Medicinal Food, 22(12), 1199-1207. https://doi.org/10.1089/jmf.2018.4349
Paik, S. H., Chakicherla, A., & Hansen, J. N. (1998). Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168. The Journal of Biological Chemistry, 273(36), 23134-23142. https://pubmed.ncbi.nlm.nih.gov/9722542
Pan, S. J., & Link, A. J. (2011). Sequence diversity in the lasso peptide framework: Discovery of functional microcin j25 variants with multiple amino acid substitutions. Journal of the American Chemical Society, 133(13), 5016-5023. https://doi.org/10.1021/ja1109634
Paone, P., & Cani, P. D. (2020). Mucus barrier, mucins and gut microbiota: The expected slimy partners? Gut, 69(12), 2232-2243. https://doi.org/10.1136/gutjnl-2020-322260
Parada, J. L., Caron, C. R., Medeiros, A. B. P., & Soccol, C. R. (2007). Bacteriocins from lactic acid bacteria: Purification, properties and use as biopreservatives. Brazilian Archives of Biology and Technology, 50(3), 512-542. https://doi.org/10.1590/S1516-89132007000300018
Patzer, S. I., Baquero, M. R., Bravo, D., Moreno, F., & Hantke, K. (2003). The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN. Microbiology (Reading, England), 149(Pt 9), 2557-2570. https://doi.org/10.1099/mic.0.26396-0
Petit, V. W., Zirah, S., Rebuffat, S., & Tabet, J.-C. (2008). Collision induced dissociation-based characterization of nucleotide peptides: Fragmentation patterns of microcin C7-C51, an antimicrobial peptide produced by Escherichia coli. Journal of the American Society for Mass Spectrometry, 19(8), 1187-1198. https://doi.org/10.1016/j.jasms.2008.04.020
Pell, T. J., Gray, M. B., Hopkins, S. J., Kasprowicz, R., Porter, J. D., & Reeves, T., Rowan, W. C., Singh, K., Tvermosegaard, K. B., Yaqub, N., & Wayne, G. J. (2021). Epithelial barrier integrity profiling: Combined approach using cellular junctional complex imaging and transepithelial electrical resistance. SLAS Discovery, 26(7), 909-921. https://doi.org/10.1177/24725552211013077
Pieterse, R. (2008). Control of bacterial pathogens associated with mastitis in dairy cows with natural antimicrobial peptides produced by lactic acid bacteria. Stellenbosch Stellenbosch University. https://scholar.sun.ac.za/handle/10019.1/2323
Pugsley, A. P., & Reeves, P. (1977). Comparison of colicins B-K260 and D-CA23: Purification and characterization of the colicins and examination of colicin immunity in the producing strains. Antimicrobial Agents and Chemotherapy, 11(2), 345-358. https://pubmed.ncbi.nlm.nih.gov/403857
Qi, F., Chen, P., & Caufield, P. W. (2001). The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV. Applied and Environmental Microbiology, 67(1), 15-21. https://pubmed.ncbi.nlm.nih.gov/11133423
Ramachandran, C., Kandasamy, S., Eric Banan-Mwine, D., Joong-Hark, K., Jung-Kun, L., Hyeon-Yeong, J., Se-Hun, K., Sudha Rani, R., Inamul Hasan, M., Shuai, W., Momna, R., Kaliyan, B., Fred Kwame, O., Hwang, S., Park, E.-J., Jung Da, Y., Fazle, E., Myeong-Hyeon, W., Jong Hwan, P., … Deog-Hwan, O. (2019). Unveiling the potentials of bacteriocin (Pediocin L50) from Pediococcus acidilactici with antagonist spectrum in a Caenorhabditis elegans model. International Journal of Biological Macromolecules, 143, 555-572. https://doi.org/10.1016/j.ijbiomac.2019.10.196
Ramaswamy, V., Cresence, V. M., Rejitha, J. S., Lekshmi, M. U., Dharsana, K. S., Prasad, S. P., & Vijila, H. M. (2007). Listeria-Review of epidemiology and pathogenesis. Journal of Microbiology, Immunology, and Infection = Wei Mian Yu Gan Ran Za Zhi, 40(1), 4-13. https://pubmed.ncbi.nlm.nih.gov/17332901
Rea, M. C., Sit, C. S., Clayton, E., O'Connor, P. M., Whittal, R. M., Zheng, J., Vederas, J. C., Ross, R. P., & Hill, C. (2010). Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile. Proceedings of the National Academy of Sciences of the United States of America, 107(20), 9352-9357. https://doi.org/10.1073/pnas.0913554107
Risøen, P. A., Brurberg, M. B., Eijsink, V. G., & Nes, I. F. (2000). Functional analysis of promoters involved in quorum sensing-based regulation of bacteriocin production in Lactobacillus. Molecular Microbiology, 37(3), 619-628. https://pubmed.ncbi.nlm.nih.gov/10931355
Roberts, N. J., Zhang, L., Janku, F., Collins, A., Bai, R. Y., Staedtke, V., Rusk, A. W., Tung, D., Miller, M., Roix, J., Khanna, K. V., Murthy, R., Benjamin, R. S., Helgason, T., Szvalb, A. D., Bird, J. E., Roy-Chowdhuri, S., Zhang, H. H., Qiao, Y., … Zhou, S. (2014). Intratumoral injection of Clostridium novyi-NT spores induces antitumor responses. Science Translational Medicine, 6, 249ra111. https://doi.org/10.1126/scitranslmed.3008982
Roh, E., Park, T.-H., Kim, M.-I., Lee, S., Ryu, S., Oh, C.-S., Rhee, S., Kim, D.-H., Park, B.-S., & Heu, S. (2010). Characterization of a new bacteriocin, carocin D, from Pectobacterium carotovorum subsp. carotovorum Pcc21. Applied and Environmental Microbiology, 76(22), 7541-7549. https://doi.org/10.1128/AEM.03103-09
Saito, H., & Watanabe, T. (1979). Effect of a bacteriocin produced by Mycobacterium smegmatis on growth of cultured tumor and normal cells. Cancer Research, 39, 5114-5117.
Saito, H., Watanabe, T., & Tomioka, H. (1979). Purification, properties, and cytotoxic effect of a bacteriocin from Mycobacterium smegmatis. Antimicrobial Agents and Chemotherapy, 15(4), 504-509. https://doi.org/10.1128/aac.15.4.504
Salomón, R. A., & Farías, R. N. (1992). Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. Journal of Bacteriology, 174(22), 7428-7435. https://pubmed.ncbi.nlm.nih.gov/1429464
Sareh Sadat, H., Bahareh, H., Ebrahim, F., & Hossein, G. (2020). Increased expression of caspase genes in colorectal cancer cell line by nisin. Archives of Clinical Infectious Diseases, 15, e97734. https://doi.org/10.5812/archcid.97734
Schwartz, S. A., & Helinski, D. R. (1971). Purification and characterization of colicin E1. The Journal of Biological Chemistry, 246(20), 6318-6327. https://pubmed.ncbi.nlm.nih.gov/5001789
Servin, A. L. (2004). Antagonistic activities of lactobacilli and bifidobacteria against microbial pathogens. FEMS microbiology reviews, 28(4), 405-440. https://doi.org/10.1016/j.femsre.2004.01.003
Shankar, N., Coburn, P., Pillar, C., Haas, W., & Gilmore, M. (2004). Enterococcal cytolysin: Activities and association with other virulence traits in a pathogenicity island. International Journal of Medical Microbiology: IJMM, 293(7-8), 609-618. https://pubmed.ncbi.nlm.nih.gov/15149038
Shih-Chun, Y., Chih-Hung, L., Calvin, T. S., & Jia-You, F. (2014). Antibacterial activities of bacteriocins: Application in foods and pharmaceuticals. Frontiers in Microbiology, 5, 241. https://doi.org/10.3389/fmicb.2014.00241
Shiva, A., Marzieh, G., & Hamideh Mahmoodzadeh, H. (2017). The apoptotic impact of nisin as a potent bacteriocin on the colon cancer cells. Microbial Pathogenesis, 111, 193-197. https://doi.org/10.1016/j.micpath.2017.08.037
Simons, A., & Alhanout, K. (2020). Bacteriocins, antimicrobial peptides from bacterial origin: Overview of their biology and their impact against multidrug-resistant bacteria. Microorganisms, 8(8), 639. https://doi.org/10.3390/microorganisms8050639
Simova, E. D., Beshkova, D. B., & Zh, P. D. (2009). Characterization and antimicrobial spectrum of bacteriocins produced by lactic acid bacteria isolated from traditional Bulgarian dairy products. Journal of Applied Microbiology, 106, 692-701. https://doi.org/10.1111/j.1365-2672.2008.04052.x
Skender, T., Luigi, S., Lucrezia, B., Andrea, B., Alessio Danilo, I., Gianna, D., Ioannis Alexandros, C., & Francesco, I. (2020). Gastric cancer in history: A perspective interdisciplinary study. Cancers, 12, 264. https://doi.org/10.3390/cancers12020264
Soderholm, A. T., & Pedicord, V. A. (2019). Intestinal epithelial cells: At the interface of the microbiota and mucosal immunity. Immunology, 158, 267-280. https://doi.org/10.1111/imm.13117
Sosunov, V., Mischenko, V., Eruslanov, B., Svetoch, E., Shakina, Y., Stern, N., Majorov, K., Sorokoumova, G., Selishcheva, A., & Apt, A. (2007). Antimycobacterial activity of bacteriocins and their complexes with liposomes. The Journal of Antimicrobial Chemotherapy, 59(5), 919-925. https://pubmed.ncbi.nlm.nih.gov/17347179
Stern, N. J., Svetoch, E. A., Eruslanov, B. V., Perelygin, V. V., Mitsevich, E. V., Mitsevich, I. P., Pokhilenko, V. D., Levchuk, V. P., Svetoch, O. E., & Seal, B. S. (2006). Isolation of a Lactobacillus salivarius strain and purification of its bacteriocin, which is inhibitory to Campylobacter jejuni in the chicken gastrointestinal system. Antimicrobial Agents and Chemotherapy, 50, 3111-3116. https://doi.org/10.1128/aac.00259-06
Sumanpreet, K., & Sukhraj, K. (2015). Bacteriocins as potential anticancer agents. Frontiers in Pharmacology, 6, 272. https://doi.org/10.3389/fphar.2015.00272
Rebuffat, S., Blond, A., Destoumieux-Garzón, D., Goulard, C., & Peduzzi, J. (2004). Microcin j25, from the macrocyclic to the lasso structure: Implications for biosynthetic, evolutionary and biotechnological perspectives. Current Protein & Peptide Science, 5(5), 383-391. https://doi.org/10.2174/1389203043379611
Tae-Seok, K. I. M., Ji-Woon, H. U. R., Myeong-Ae, Y. U., Chan-Ick, C., Kyung-Nam, K. I. M., Jae-Kwan, H., & Yu-Ryang, P. (2003). Antagonism of Helicobacter pylori by bacteriocins of lactic acid bacteria. Journal of Food Protection, 66, 3-12. https://doi.org/10.4315/0362-028x-66.1.3
Tahara, T., Oshimura, M., Umezawa, C., & Kanatani, K. (1996). Isolation, partial characterization, and mode of action of Acidocin J1132, a two-component bacteriocin produced by Lactobacillus acidophilus JCM 1132. Applied and Environmental Microbiology, 62(3), 892-897. https://pubmed.ncbi.nlm.nih.gov/8975617
Tal, D., Arthur, P., Jeff, H., & Sangeeta, B. (2013). Measuring growth and gene expression dynamics of tumor-targeted S. typhimurium bacteria. Journal of Visualized Experiments, (77), e50540. https://doi.org/10.3791/50540
Techo, S., Visessanguan, W., Vilaichone, R.-K., & Tanasupawat, S. (2019). Characterization and antibacterial activity against Helicobacter pylori of lactic acid bacteria isolated from Thai fermented rice noodle. Probiotics and Antimicrobial Proteins, 11(1), 92-102. https://doi.org/10.1007/s12602-018-9385-z
Thaiss, C. A., Zmora, N., Levy, M., & Elinav, E. (2016). The microbiome and innate immunity. Nature, 535(7610), 65-74. https://doi.org/10.1038/nature18847
Timmis, K. (1972). Purification and characterization of colicin D. Journal of Bacteriology, 109(1), 12-20. https://pubmed.ncbi.nlm.nih.gov/4621624
Troselj, V., Cao, P., & Wall, D. (2018). Cell-cell recognition and social networking in bacteria. Environmental Microbiology, 20(3), 923-933. https://doi.org/10.1111/1462-2920.14005
Tsung-Lin, T., An-Chieh, L., Yi-Chieh, C., Yi-Shun, L., & Thy-Hou, L. (2015). Antimicrobial peptide m2163 or m2386 identified from Lactobacillus casei ATCC 334 can trigger apoptosis in the human colorectal cancer cell line SW480. Tumor Biology, 36, 3775-3789. https://doi.org/10.1007/s13277-014-3018-2
Umu, Ö. C. O., Bäuerl, C., Oostindjer, M., Pope, P. B., Hernández, P. E., Pérez-Martínez, G., & Diep, D. B. (2016). The potential of class II bacteriocins to modify gut microbiota to improve host health. PLoS One, 11(10), e0164036. https://doi.org/10.1371/journal.pone.0164036
Umu, Ö. C. O., Rudi, K., & Diep, D. B. (2017). Modulation of the gut microbiota by prebiotic fibres and bacteriocins. Microbial Ecology in Health and Disease, 28(1), 1348886. https://doi.org/10.1080/16512235.2017.1348886
Valdés-Stauber, N., & Scherer, S. (1994). Isolation and characterization of linocin M18, a bacteriocin produced by Brevibacterium linens. Applied and Environmental Microbiology, 60(10), 3809-3814. https://pubmed.ncbi.nlm.nih.gov/7986050
van de Kamp, M., Horstink, L. M., van den Hooven, H. W., Konings, R. N., Hilbers, C. W., Frey, A., Sahl, H. G., Metzger, J. W., & van de Ven, F. J. (1995). Sequence analysis by NMR spectroscopy of the peptide lantibiotic epilancin K7 from Staphylococcus epidermidis K7. European Journal of Biochemistry, 227(3), 757-771. https://pubmed.ncbi.nlm.nih.gov/7867636
van Heel, A. J., de Jong, A., Montalbán-López, M., Kok, J., & Kuipers, O. P. (2013). BAGEL3: Automated identification of genes encoding bacteriocins and (non-)bactericidal posttranslationally modified peptides. Nucleic Acids Research, 41(Web Server issue), W448-W453. https://doi.org/10.1093/nar/gkt391
Varadé, J., Magadán, S., & González-Fernández, Á. (2020). Human immunology and immunotherapy: Main achievements and challenges. Cellular & Molecular Immunology, 18, 805-828. https://doi.org/10.1038/s41423-020-00530-6
Varas, M. A., Muñoz-Montecinos, C., Kallens, V., Simon, V., Allende, M. L., Marcoleta, A. E., & Lagos, R. (2020). Exploiting zebrafish xenografts for testing the in vivo antitumorigenic activity of microcin E492 against human colorectal cancer cells. Frontiers in Microbiology, 11, 405. https://doi.org/10.3389/fmicb.2020.00405
Villarante, K. I., Elegado, F. B., Iwatani, S., Zendo, T., Sonomoto, K., & de Guzman, E. E. (2010). Purification, characterization and in vitro cytotoxicity of the bacteriocin from Pediococcus acidilactici K2a2-3 against human colon adenocarcinoma (HT29) and human cervical carcinoma (HeLa) cells. World Journal of Microbiology and Biotechnology, 27(4), 975-980. https://doi.org/10.1007/s11274-010-0541-1
Vincent, P. A., & Morero, R. D. (2009). The structure and biological aspects of peptide antibiotic microcin J25. Current Medicinal Chemistry, 16(5), 538-549. https://pubmed.ncbi.nlm.nih.gov/19199920
Walsh, C. J., Guinane, C. M., O' Toole, P. W., & Cotter, P. D. (2017). A profile hidden markov model to investigate the distribution and frequency of LanB-encoding lantibiotic modification genes in the human oral and gut microbiome. PeerJ, 5, e3254. https://doi.org/10.7717/peerj.3254
Wang, S., Ye, Q., Wang, K., Zeng, X., Huang, S., Yu, H., Ge, Q., Qi, D., & Qiao, S. (2019). Enhancement of macrophage function by the antimicrobial peptide sublancin protects mice from methicillin-resistant Staphylococcus aureus. Journal of Immunology Research, 2019, 3979352-3979352. https://doi.org/10.1155/2019/3979352
Wang, T., Fu, J., Xiao, X., Lu, Z., Wang, F., Jin, M., Wang, Y., & Zong, X. (2021). CBP22, a novel bacteriocin isolated from Clostridium butyricum ZJU-F1, protects against LPS-induced intestinal injury through maintaining the tight junction complex. Mediators of Inflammation, 2021, 8032125. https://doi.org/10.1155/2021/8032125
Weber, T., Blin, K., Duddela, S., Krug, D., Kim, H. U., Bruccoleri, R., Lee, S. Y., Fischbach, M. A., Müller, R., Wohlleben, W., Breitling, R., Takano, E., & Medema, M. H. (2015). antiSMASH 3.0-a comprehensive resource for the genome mining of biosynthetic gene clusters. Nucleic Acids Research, 43(W1), W237-W243. https://doi.org/10.1093/nar/gkv437
Weil, H. P., Beck-Sickinger, A. G., Metzger, J., Stevanovic, S., Jung, G., Josten, M., & Sahl, H. G. (1990). Biosynthesis of the lantibiotic Pep5. Isolation and characterization of a prepeptide containing dehydroamino acids. European Journal of Biochemistry, 194(1), 217-223. https://pubmed.ncbi.nlm.nih.gov/2253617
Xiao, H., Chen, X., Chen, M., Tang, S., Zhao, X., & Huan, L. (2004). Bovicin HJ50, a novel lantibiotic produced by Streptococcus bovis HJ50. Microbiology (Reading, England), 150(Pt 1), 103-108. https://doi.org/10.1099/mic.0.26437-0
Xiaoyan, D., Ping, C., Xiaoxia, X., Meiling, H., & Jianbo, L. (2022). Role of gastric microorganisms other than Helicobacter pylori in the development and treatment of gastric diseases. BioMed Research International, 2022, 6263423. https://doi.org/10.1155/2022/6263423
Xu, L., Zhou, J., Qu, G., Lin, Z., Fan, Q., Wang, C., & Wang, Q. (2020). Recombinant lactobacillin PlnK adjusts the gut microbiome distribution in broilers. British Poultry Science, 61(4), 390-399. https://doi.org/10.1080/00071668.2020.1752911
Xu, Y., Wang, N., Tan, H.-Y., Li, S., Zhang, C., Zhang, Z., & Feng, Y. (2020). saponins modulate the gut microbiota to promote thermogenesis and beige adipocyte reconstruction leptin-mediated AMPKα/STAT3 signaling in diet-induced obesity. Theranostics, 10(24), 11302-11323. https://doi.org/10.7150/thno.47746
Yamada, T., Christov, K., Shilkaitis, A., Bratescu, L., Green, A., Santini, S., Bizzarri, A. R., Cannistraro, S., Gupta, T. K. D., & Beattie, C. W. (2013). p28, a first in class peptide inhibitor of cop1 binding to p53. British Journal of Cancer, 108, 2495-2504. https://doi.org/10.1038/bjc.2013.266
Ye, P., Wang, J., Liu, M., Li, P., & Gu, Q. (2021). Purification and characterization of a novel bacteriocin from Lactobacillus paracasei ZFM54. LWT- Food Science and Technology, 143(1), 111125.
Kim, Y. J., Kim, B. K., Park, S. J., & Kim, J. H. (2021). Impact of Fusobacterium nucleatum in the gastrointestinal tract on natural killer cells. World Journal of Gastroenterology, 27, 4879-4889. https://doi.org/10.3748/wjg.v27.i29.4879
Yi-bing, H., Xiao-fei, W., Hong-ye, W., Yu, L., & Yuxin, C. (2011). Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Molecular Cancer Therapeutics, 10, 416-426. https://doi.org/10.1158/1535-7163.mct-10-0811
Yi, L., Dang, Y., Wu, J., Zhang, L., Liu, X., Liu, B., Zhou, Y., & Lu, X. (2016). Purification and characterization of a novel bacteriocin produced by Lactobacillus crustorum MN047 isolated from koumiss from Xinjiang, China. Journal of Dairy Science, 99(9), 7002-7015. https://doi.org/10.3168/jds.2016-11166
Yi, L., Li, X., Luo, L., Lu, Y., Yan, H., Qiao, Z., & Lü, X. (2018). A novel bacteriocin BMP11 and its antibacterial mechanism on cell envelope of Listeria monocytogenes and Cronobacter sakazakii. Food Control, 91, 160-169.
Yi, L., Luo, L., & Lü, X. (2018). Efficient exploitation of multiple novel bacteriocins by combination of complete genome and peptidome. Frontiers In Microbiology, 9, 1567. https://doi.org/10.3389/fmicb.2018.01567
Yount, N. Y., Weaver, D. C., Anda, J. D., Lee, E. Y., Lee, M. W., & Wong, G. C. L., & Yeaman, M. R. (2020). Discovery of novel type ii bacteriocins using a new high-dimensional bioinformatic algorithm. Frontiers in Immunology, 11, 1873. https://doi.org/10.1016/j.ijbiomac.2019.10.196
Yu, H., Shang, L., Yang, G., Dai, Z., Zeng, X., & Qiao, S. (2022). Biosynthetic microcin j25 exerts strong antibacterial, anti-inflammatory activities, low cytotoxicity without increasing drug-resistance to bacteria target. Frontiers in Immunology, 13, 811378. https://doi.org/10.3389/fimmu.2022.811378
Yu, H., Wang, Y., Zeng, X., Cai, S., Wang, G., Liu, L., Huang, S., Li, N., Liu, H., Ding, X., Song, Q., & Qiao, S. (2020). Therapeutic administration of the recombinant antimicrobial peptide microcin J25 effectively enhances host defenses against gut inflammation and epithelial barrier injury induced by enterotoxigenic Escherichia coli infection. FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology, 34(1), 1018-1037. https://doi.org/10.1096/fj.201901717R
Zeinab, Y., Davoud, E., & Hossein, G. (2020). Cloning and the expression of the protein fusion enterocin-nisin-epidermicin as a candidate for the treatment of gastric cancer. Gene Reports, 20, 100751. https://doi.org/10.1016/j.genrep.2020.100751
Zhang, J. (2020). Effect of antimicrobial peptide microcin j25 on growth performance, immune regulation, and intestinal microbiota in broiler chickens challenged with Escherichia coli and Salmonella. Animals, 10, 345. https://doi.org/10.3390/ani10020345
Zheng, J., Gänzle, M. G., Lin, X. B., Ruan, L., & Sun, M. (2015). Diversity and dynamics of bacteriocins from human microbiome. Environmental Microbiology, 17(6), 2133-2143. https://doi.org/10.1111/1462-2920.12662
Zhou, Q., Xue, B., Gu, R., Li, P., & Gu, Q. (2021). Lactobacillus plantarum ZJ316 attenuates Helicobacter pylori-induced gastritis in C57BL/6 mice. Journal of Agricultural and Food Chemistry, 69, 6510-6523. https://doi.org/10.1021/acs.jafc.1c01070