Effect of Lactobacillus delbrueckii cell wall hydrolysate on immune protection processes
Abstract
Fragments of peptidoglycans, namely muramyl peptides, induce a complex cellular response through the activation of pattern recognition receptors. Over the past two decades, many structural sequences have been discovered that bind PG (proteins containing LysM; intracellular regulatory proteins of NOD-like receptors; proteins that bind the domain with penicillins and Ser / Thr-kinases; peptidoglycan recognition proteins; lectin-like receptors of C -type; eukaryotic cytosolic hexonicases). It has been shown that the use of muramyl peptides is an effective tool for modulating the cellular response, and for enhancing the production of proinflammatory cytokines in particular. The cytotoxicity of peptidoglycan fractions against various types of tumors, including sarcoma, leukemia, melanoma, and lung cancer, has been revealed. The tumor activity of muropeptides with antiproliferative and cytotoxic effects is associated with modulation of cytokine and chemokine production. It is especially significant that muramyl peptides are able to reduce the bioenergetic ratio of mitochondria as an anomaly of energy metabolism, associated with a tumor, may be the cause of suppression of cancer processes. Under natural conditions of environmental pollution, the immunomodulatory effect of the enzymatic hydrolyzate of the cell wall of Lactobacillus delbrueckiiis manifested the complex stimulation of the humoral and cellular links of the immune response, which was confirmed by an increase in the bactericidal and lysozyme activity of colostrum. The use of such immunomodulators can be a promising basis for regulation of the mechanisms of immune resistance, maintaining health and increasing the weight gain of animals for the first weeks of life.
About the Authors
E. V. Sukharenko
FSBEI HE «Moscow State Academy of Veterinary Medicine and Biotechnology - MBA by K.I.Scriabin
Russian Federation
Russian Federation
Moscow
V. S. Nedzvetsky
DNU by O. Honchara
Ukraine
Ukraine
Dnipro
V. I. Maksimov
FSBEI HE «Moscow State Academy of Veterinary Medicine and Biotechnology - MBA by K.I.Scriabin
Russian Federation
Russian Federation
Moscow
References
1. Григорьев, В.С. Особенности полового созревания чистопородных и помесных свинок / В.С. Григорьев, В.И. Максимов // Зоотехния. – 2006. – № 2. – С. 31.
2. Масюк, Д.Н. Влияние препарата «Иммунолак» на уровень факторов неспецифической иммунной защиты молозива свиноматок / Д.Н. Масюк, Е.В. Сухаренко, В.С. Недзвецкий, А.В. Кокарев, В.И. Максимов // Вестник АПК Ставрополья. – 2016. – № 1(21). – С. 66–72.
3. Масюк, Д.Н. Эффекты иммуномодулирующего препарата из бактериальных стенок лактобацилл на гематологические показатели и иммунологическую резистентность поросят / Д. Н. Масюк,Е.В. Сухаренко, В.С. Недзвецкий, А.В. Кокарев, В.И. Максимов // Ветеринария, зоотехния и биотехнология. – 2016. – № 2. – С. 23–30.
4. Akira, S. Pathogen recognition and innate immunity / S. Akira, S. Uematsu, O. Takeuchi // Cell. – 2006. – V. 124. – P. 783–801. doi: 10.1016/j.cell.2006.02.015.
5. Amrouche, T. Effects of bifidobacterial cytoplasm, cell wall and exopolysaccharide on mouse lymphocyte proliferation and cytokine production / T. Amrouche, Y. Boutin, G. Prioult, I. Fliss // Int Dairy J. – 2006. – V. 16(1). – P. 70–80.
6. Bock, F.J. RNA Regulation by Poly (ADP-Ribose) Polymerases / F.J. Bock, T.T. Todorova, P. Chang // Molecular Cell. – 2015. – V. 1. – P. 959–969.
7. Bock, F.J. New directions in poly(ADPribose) polymerase biology / F.J. Bock, P. Chang // FEBS J. – 2016. – V. 283(22). – P. 4017–4031.
8. Buist, G. LysM, a widely distributed protein motif for binding to (peptido) glycans / G. Buist, A. Steen, J. Kok, O.P. Kuipers // Mol. Microbiol. – 2008. – V. 68. – P. 838–847. doi: 10.1111/j.1365-2958.2008.06211.x.
9. Canas, M.A. Outer membrane vesicles from probiotic and commensal Escherichia coli activate NOD1-mediated immune responses in intestinal epithelial cells // M.A. Canas, M.J. Fabrega, R. Gimenez, J. Badia, L. Baldoma // Front. Microbiol. – 2018. – V. 9. – P. 498. doi: 10.3389/fmicb.2018.00498.
10. Chiarugi, A. Poly(ADP-ribose) polymerase-1 activity promotes NF-κB-driven transcription and microglial activation: Implication for neurodegenerative disorders / A. Chiarugi, M.A. Moskowitz // J Neurochem. – 2003. – V. 85(2). – P. 306–317.
11. Commane, D. The potential mechanisms involved in the anti- carcinogenic action of probiotics / D. Commane, R. Hughes, C. Shortt, I. Rowland // Mutation Research. - Fundamental and Molecular Mechanisms of Mutagenesis. – 2005. – V. 91. – P. 276–89.
12. El-Jamal, N. Effect of muramyl peptides on mitochondrial respiration / N. ElJamal, G.M. Bahr, K.S. Echtay // Clin Exp Immunol. – 2009. – V. 155(1). – P. 72–78.
13. Franchi, L Function of Nod-like receptors in microbial recognition and host defense // L. Franchi, N. Warner, K. Viani, G. Nunez // Immunol. Rev. – 2009. – V. 227. – P. 106–128. doi: 10.1111/j.1600-065X.2008.00734.x.
14. Furnari, F.B. Malignant astrocytic glioma: Genetics, biology, and paths to treatment / F.B. Furnari, T. Fenton, R.M. Bachoo, A. Mukasa, J.M. Stommel, A. Stegh, W.C. Hahn, K.L. Ligon, D.N. Louis, C. Brennan, L. Chin, R.A. DePinho, W.K. Cavenee // Genes and Development. – 2007. – V. 21. – P. 2683–2710.
15. Gibson, B.A. New insights into the molecular and cellular functions of poly(ADPribose) and PARPs / B.A. Gibson, W.L. Kraus // Nature Reviews Molecular Cell Biology. – 2012. – V. 13. – P. 411–124.
16. Gonet-Surówka, A.K. P1250 Infiuence of Lactobacilli probiotic strains on apoptosis of colon cancer cells lines / A.K. GonetSurówka, M. Strus, P.B. Heczko // Int J Antimicrob Agents. – 2007. – P. 343–344.
17. Horcajo, P. Peptidoglycan plasticity in bacteria: stress-induced peptidoglycan editing by noncanonical D-amino acids / P. Horcajo, M. A. de Pedro, F. Cava // Microb. Drug Resist. – 2012. – V. 18. – P. 306–313. doi: 10.1089/mdr.2012.0009.
18. Irazoki, O. Peptidoglycan Muropeptides: Release, Perception, and Functions as Signaling Molecules / O. Irazoki, S.B. Hernandez, F. Cava // Front. Microbiol. – 2019. – V. 10. – P. 500. doi: 10.3389/fmicb.2019.00500.
19. Kauppinen, T.M. Poly(ADP-ribose) polymerase-1-induced NAD+ depletion promotes nuclear factor-κB transcriptional activity by preventing p65 de-acetylation / T.M. Kauppinen, L. Gan, R.A. Swanson // Biochim Biophys Acta. – 2013. – V. 1833 (8). – P. 1985–1991.
20. Kim, J.Y. Screening for antiproliferative effects of cellular components from lactic acid bacteria against human cancer cell lines / J.Y. Kim, H.J. Woo, Y.S. Kim, H.J. Lee // Biotechnol Lett. – 2002. – V. 24 (17). – P. 1431–1436.
21. Kong, Y.C. Effects of natural or synthetic microbial adjuvants on induction of autoimmune thyroiditis / Y.C. Kong, F. Audibert, A.A. Giraldo, N.R. Rose, L. Chedid // Infect Immun. – 1985. – V. 49(1). – P. 40–45. doi: 10.1128/IAI.49.1.40-45.1985.
22. Masjuk, D.M. A method of enhancing the natural resistance of newborn piglets. Ukraine Patent 118400 / D.M. Masjuk, V.S. Nedzvetsky KAV. August 10, 2017.
23. Mayer, S. C-type lectins: their network and roles in pathogen recognition and immunity / S. Mayer, M.K. Raulf, B. Lepenies // Histochem. Cell Biol. – 2017. – V. 147, P. 223–237. doi: 10.1007/s00418-016-1523-7.
24. McAdam, K.P. Amyloidosis and the serum amyloid A protein response to muramyl dipeptide analogs and different mycobacterial species / K.P. McAdam, N.T. Foss, C. Garcia, R. DeLellis, L. Chedid, R.J. Rees // Infect Immun. – 1983. – V. 39 (3). – P. 1147–1154. doi: 10.1128/IAI.39.3.1147-1154.1983.
25. Mellroth, P. A scavenger function for a Drosophila peptidoglycan recognition protein / P. Mellroth, J. Karlsson, H. Steiner // J. Biol. Chem. – 2003. – V. 278. – P. 7059–7064. doi: 10.1074/jbc.M208900200.
26. Mesnage, S. Molecular basis for bacterial peptidoglycan recognition by LysM domains / S. Mesnage, M. Dellarole, N.J. Baxter, J.B. Rouget, J.D. Dimitrov, N. Wang // Nat. Commun. – 2014. – V. 5. – P. 4269. doi: 10.1038/ncomms5269.
27. Mir, M. The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization / M. Mir, J. Asong, X. Li, J. Cardot, G.J. Boons, R.N. Husson // LoS Pathog. – 2011. – V.7 (7). – P. e1002182. doi: 10.1371/journal.ppat.1002182
28. Nadesalingam, J. Mannose-binding lectin recognizes peptidoglycan via the Nacetyl glucosamine moiety, and inhibits ligand-induced proinflammatory effect and promotes chemokine production by macrophages / J. Nadesalingam, A.W. Dodds, K.B.M. Reid, N. Palaniyar // J. Immunol. – 2005. – V. 175. – P. 1785–1794. doi: 10.4049/jimmunol.175.3.1785.
29. Nedzvetsky, V.S. Neuroprotective Effect of Curcumin on LPS- activated Astrocytes Is Related to the Prevention of GFAP and NF-κB Upregulation / V.S. Nedzvetsky, C.A. Agca, S.V. Kyrychenko // Neurophysiology. – 2017. – V. 49(4). – P. 305–307.
30. Owens, R. Divergent neuroinflammatory regulation of microglial TREM expression and involvement of NF-κB / R. Owens, K. Grabert, C.L. Davies, A. Alfieri, J.P. Antel, L.M. Healy, B.W. McColl // Front Cell Neurosci. – 2017. – V. 2. – P. 11.
31. Płusa, T. The immunomodulatory proteins contained in the colostrum. / T. Płusa, P. Merkuriusz // Livestock Production Science. – 2009.– V. 25. – Р. 234–238.
32. Porter, P. Secretory IgА and antibodies to Escherichia Coli in porcine colostrum and milk and their significance in the alimentary tract of the young pig / P. Porter, D.E. Noakes, and W.D. Allen // Immunology. – 1970. – V. 18.– Р. 245-256.
33. Vaarala, O. Immunological effects of probiotics with special reference to lactobacilli / O.Vaarala // Clin. Exp. Allergy. – 2003. – V. 12(33). – P. 1634–1640.
34. Wolf, A.J. Peptidoglycan recognition by the innate immune system / A.J. Wolf, D.M. Underhill // Nat. Rev. Immunol. – 2018. V. 18. – P. 243–254. doi: 10.1038/nri.2017.136.
35. Zhang, X.C. Evolutionary genomics of LysM genes in land plants / X.C. Zhang, S.B. Cannon, G Stacey // BMC Evol. Biol. – V. 9(9). – P. 183. doi: 10.1186/1471-2148-9-183.
Review
For citations:
Sukharenko E.V., Nedzvetsky V.S., Maksimov V.I. Effect of Lactobacillus delbrueckii cell wall hydrolysate on immune protection processes. International Journal of Veterinary Medicine. 2021;(2):32-41. (In Russ.)
Views:
288
Email this article 