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Molecular and genetic aspects of the Helicobacter pylori interaction with cells of the gastric mucosaReview [Free Full Text (pdf)] ![]() SUMMARY. The modern views on the classical determinants of Helicobacter pylori virulence, the pathogenetic effects of phosphorylation and the process of translocation of CagA into the cells of the gastric mucosa (GM) were analyzed, and the surface membrane receptors of VacA binding to the epithelial cells of the GM were characterized in this study. The necessity of carrying out genetic typing of Helicobacter pylori to determine the potential virulence of a microorganism in order to predict the course of H. pylori-associated diseases and to select targeted therapy has been substantiated. Key words: Helicobacter pylori, CagA, VacA, gastric pathology
Tsitologiya i Genetika 2019, vol. 53, no. 6, pp. 71-78
E-mail: d.suxan
References1. Kurinna, Y.G. Report on the Kyoto International Consensus on Gastritis Associated with Helicobacter pylori,Mod. Gastroenterol., 2016, vol. 86, no. 1, pp. 36–53. 2. Lind, J., Backert, S., and Hoffmann, R., Systematic analysis of phosphotyrosine antibodies recognizing single phosphorylated EPIYA-motifs in CagA of East Asian-type Helicobacter pylori strains, BMC Microbiol., 2016, vol. 16, no. 1, https://doi.org/10.1186/s12866-016-0820-6 3. Pachathundikandi, S. K., Lind, J., and Tegtmeyer, N., Interplay of the gastric pathogen Helicobacter pylori with Toll-like receptors, BioMed. Res. Int., 2015, pp. 1–12. https://doi.org/10.1155/2015/192420 4. Salama, N.R., Hartung, M.L., and Müller, A., Life in the human stomach: persistence strategies of the bacterial pathogen Helicobacter pylori,Nat. Rev. Microbiol., 2013, vol. 11, no. 6, pp. 385–399. https://doi.org/10.1038/nrmicro3016 5. Linz, B., Balloux, F., and Moodley, Y., An African origin for the intimate association between humans and Helicobacter pylori,Nature, 2007, vol. 445, no. 7130, pp. 915–918. https://doi.org/10.1038/nature05562 6. Backert, S. and Tegtmeyer, N., Type IV secretion and signal transduction of Helicobacter pylori CagA through Interactions with host cell receptors, Toxins, 2017, vol. 9, no. 4, p. 115. https://doi.org/10.3390/toxins9040115 7. Maixner, F., Krause-Kyora, B., and Turaev, D., The 5300-year-old Helicobacter pylori genome of the Iceman, Science, 2016, vol. 351, no 6269, pp. 162–165. https://doi.org/10.1126/science.aad2545 8. Amieva, M., and Peek, R.M., Pathobiology of Helicobacter pylori-induced gastric cancer, Gastroenterology, 2016, vol. 150, no. 1, pp. 64–78. https://doi.org/10.1053/j.gastro.2015.09.004 9. Moodley, Y., Linz, B., and Bond, R.P., Age of the association between Helicobacter pylori and man, PLoS Pathogens, 2012, vol. 8, no. 5. https://doi.org/10.1371/journal.ppat.1002693 10. Kodaman, N., Sobota, R.S. and Mera, R., Disrupted human–pathogen co-evolution: a model for disease, Front. Genetics, 2014, no. 5. https://doi.org/10.3389/fgene.2014.00290 11. Yamaoka, Y., Graham, D.Y., Helicobacter pylori virulence and cancer pathogenesis, Future Oncol., 2014, vol. 10, no. 8, pp. 1487–1500. https://doi.org/10.2217/fon 12. Westmeier, D., Posselt, G., and Hahlbrock, A., Nanoparticle binding attenuates the pathobiology of gastric cancer-associated Helicobacter pylori,Nanoscale, 2018, 10, no. 3, pp. 1453–1463. https://doi.org/10.1039/c7nr06573f 13. Backert, S., Clyne, M., and Tegtmeyer, N., Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori,Cell Commun. Signal., 2011, 9, no. 1, p. 28. https://doi.org/10.1186/1478-811X-9-28 14. Amieva, M.R. and El-Omar, E.M., Host–bacterial interactions in Helicobacter pylori infection, Gastroenterology, 2008, 134, no 1, pp. 306–323. https://doi.org/10.1053/j.gastro.2007.11.009 15. Atherton, J.C. and Blaser, M.J., Coadaptation of Helicobacter pylori and humans: ancient history, modern implications, J. Clin. Invest., 2009, 119, no. 9, pp. 2475–2487. https://doi.org/10.1172/JCI38605 16. Polk, D.B. and Peek, R.M., Helicobacter pylori: gastric cancer and beyond, Nat. Rev. Cancer, 2010, vol. 10, no. 6, pp. 403–414. https://doi.org/10.1038/nrc2857 17. Schreiber, S., Konradt, M.C., and Grol, O., The spatial orientation of Helicobacter pylori in the gastric mucus, Proc. Natl. Acad. Sci. U. S. A., 2004, 101, no. 14, pp. 5024–5029. https://doi.org/10.1073/pnas.0308386101 18. Schreiber, S., Bucker, R., and Groll, C., Rapid loss of motility of Helicobacter pylori in the gastric lumen in vivo, Infect. Immun., 2005, vol. 73, no. 3, pp. 1584– 1589. https://doi.org/10.1128/IAI.73.3.1584-1589.2005 19. Backert, S. and Tegtmeyer, N., The versatility of the Helicobacter pylori vacuolating cytotoxin VacA in signal transduction and molecular crosstalk, Toxins, 2010, vol. 2, no. 1, pp. 69–92. https://doi.org/10.3390/toxins2010069 20. Hiroko, N. and Masanori, H., Sequence polymorphism and intrinsic structural disorder as related to pathobiological performance of the Helicobacter pylori CagA oncoprotein, Toxins, 2017, vol. 9, no. 4, pp. 136. https://doi.org/10.3390/toxins9040136 21. Kostiuk, O.V., Pathogenicity factors of H. pylori: genotypic bases and phenotypic manifestations, Prevent. Med., 2012, vol. 2, no. 18, pp. 65–70. 22. Backert, S. and Blaser, M.J., The role of CagA in the gastric biology of Helicobacter pylori, Am. Assoc. Cancer Res., 2016, vol. 76, no. 14, pp. 4028–4031. https://doi.org/10.1158/0008-5472.CAN-16-1680 23. Hayashi, T., Senda, M., Morohashi, H., Higashi, H., Horio, M., Kashiba, Y., Nagase, L., Sasaya, D., Shimizu, T., and Venugopalan, N., Tertiary structure–function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA, Cell Host Microbe, 2012, no. 12, pp. 20–33.https://doi.org/10.1016/j.chom.2012.05.010 24. Kostyuk, O.V., Factors of pathogenicity of H. pylori: genotypical bases and phenotypic manifestations, Profilakt. Med.: Sci. Pract. J., 2012, no. 2, pp. 65–70. 25. Shariq, M., Kumar, N., and Kumari, R., Biochemical Analysis of CagE: a VirB4 homologue of Helicobacter pylori Cag-T4SS, PLoS One, 2015, vol. 11, no. 10. https://doi.org/10.1371/journal.pone.0142606 26. Zhang, J., Fan, F., and Zhao, Y., Crystal structure of the type IV secretion system component CagX from Helicobacter pylori,Acta Crystallogr. F Struct. Biol. Commun., 2017, vol. 73, no. 3, pp. 167–173. https://doi.org/10.1107/S2053230X17001376 27. Merino, E., Flores-Encarnaciyn, M., and Aguilar-Gutierrez, G.R., Functional interaction and structural characteristics of unique components of Helicobacter pylori T4SS, FEBS J., 2017, vol. 284, no. 21, pp. 3540–3549. https://doi.org/10.1111/febs.l4092 28. Sause, W. E., Keilberg, D., Aboulhouda, S., and Ottemann, K.M., The Helicobacter pylori autotransporter ImaA tempers the bacterium’s interaction with a5pi integrin, Infect. Immun., 2017, vol. 85, no. l. https://doi.org/10.1128/IAI.00450-16 29. Ko, S.H., Rho, D.J., Jeon, J.L., Kim, Y.J., Woo, H.A., Kim, N., and Kim, J.M., Crude preparations of Helicobacter pylori outer membrane vesicles induce upregulation of heme oxygenase-1 via activating Akt-Nrf2 and mTOR-IêB Kinase-NF-êB pathways in dendritic cells, Infect. Immun., 2016, vol. 84, no. 8, pp. 2162–2174. https://doi.org/10.1128/IAI.00190-16 30. Park, N.H., Song, M.S., Shin, S.Y., Jeong, J.-H., and Lee, H.Y., The effects of medication adherence and health literacy on health-related quality of life in older people with hypertension, Int. J. Older People Nurs., 2018, vol. 13, no. 3. https://doi.org/10.1111/opn.l2196 31. Jones, K.R., Whitmire, J.M., and Merrell, D.S., A tale of two toxins: Helicobacter pylori CagA and VacA modulate host pathways that impact disease, Front. Microbiol., 2010, vol. 1. https://doi.org/10.3389/fmicb.2010.00115 32. Nishikawa, H., Hatakeyama, M. Sequence polymorphism and intrinsic structural disorder as related to pathobiological performance of the Helicobacter pylori CagA oncoprotein, Toxins, 2017, vol. 9, no. 4, p. 136. https://doi.org/10.3390/toxins9040136 33. Palcev, M.A., Kaktursky, L.V., and Zayratyants, O.V., Pathological Anatomy: National Leadership, Moscow: GEOTAR-MEDIA, 2013. 34. Chomvarin, C., Phusri, K., Sawadpanich, K., Mairiang, P., Namwat, W., Wongkham, C., and Hahnvajanawong, C., Prevalence of cagA EPÃYA motifs in Helicobacter pylori among dyspeptic patients in Northeast Thailand, Southeast Asian J. Trop. Med. Public Health, 2012, vol. 42, no. 1, pp. 105–115. 35. Hatakeyama, M., Helicobacter pylori CagA and gastric cancer: a paradigm for hit-and-run carcinogenesis, Cell Host Microbe, 2014, vol. 15, no. 3, pp. 306–316.https://doi.org/10.1016/j.chom.2014.02.008 36. Buzas, G.M., Helicobacter pylori: A Worldwide Perspective 2014, Budapest: Bentham Science Publishers, 2014. 37. Wong, S.H.M., Fang, C.M., and Chuah, L.-H., E-cadherin: Its dysregulation in carcinogenesis and clinical implications, Crit. Rev. Oncol./Hematol., 2018, 121, pp. 11–22. https://doi.org/10.1016/j.critre-vonc.2017.11.010 38. Tegtmeyer, N. and Backert, S., Molecular Pathogenesis and Signal Transduction by Helicobacter pylori, Switzerland: Springer, 2017. 39. Wroblewski, L.E. and Peek, R.M., Targeted disruption of the epithelial-barrier by Helicobacter pylori,Cell Commun. Signal., 2011, vol. 9. https://doi.org/10.1186/1478-811X-9-29 40. Zhang, Y., Xia, M., and Jin, K., Function of the c-Met receptor tyrosine kinase in carcinogenesis and associated therapeutic opportunities, Mol. Cancer, 2018, vol. 17, no. 1. https://doi.org/10.1186/s12943-018-0796-y 41. Steffen, B. and Yoshio, Y. Helicobacter pylori Research: From Bench to Bedside, Japan: Springer, 2016. 42. Li, N., Tang, B., and Jia, Y., Helicobacter pylori CagA protein negatively regulates autophagy and promotes inflammatory response via c-Met-PI3K/Akt-mTOR signaling pathway, Front. Cell. Infect. Microbiol., 2017, no. 7. https://doi.org/10.3389/fcimb.2017.00417 43. Churin, Y., Al-Ghoul, L., Kepp, O., Meyer, T.F., Birchmeier, W., and Naumann, M., Helicobacter pylori CagA protein targets the c-Met receptor and enhances the mitogenic response, J. Cell Biol., 2003, vol. 161, no. 2, pp. 249–255. https://doi.org/10.1083/jcb.200208039 44. Huang, X., Wang, C., Sun, J., Luo, J., You, J., Liao, L., and Li, M., Clinical value of CagA, c-Met, PI3K and Beclin-1 expressed in gastric cancer and their association with prognosis, Oncol Lett., 2018, vol. 15, no. 1, pp. 947–955. https://doi.org/10.3892/ol.2017.7394 45. Hiroko, N. and Masanori, H., Sequence polymorphism and intrinsic structural disorder as related to pathobiological performance of the Helicobacter pylori CagA oncoprotein, Toxins, 2017, vol. 9, no. 4, p. 136. https://doi.org/10.3390/toxins9040136 46. Yamahashi, Y., Saito, Y., Murata-Kamiya, N., and Hatakeyama, M., Polarity-regulating kinase partitioning-defective 1b (PAR1b) phosphorylates guanine nucleotide exchange factor H1 (GEF-H1) to regulate RhoA-dependent actin cytoskeletal reorganization, J. Biol. Chem., 2011, vol. 286, no. 52, pp. 44 576–44 584. https://doi.org/10.1074/jbc.M111.267021 47. Nishikawa, H., Hayashi, T., and Arisaka, F., Impact of structural polymorphism for the Helicobacter pylori CagA oncoprotein on binding to polarity-regulating kinase PARlb, Sci. Rep., 2016, vol. 6, no. 1. https://doi.org/10.1038/srep30031 48. Fahimi, R, Tohidkia, M.R., and Fouladi, M., Pleiotropic cytotoxicity of VacA toxin in host cells and its impact on immunotherapy, BioImpacts, 2017, vol. 7, no. 1, pp. 59–71. https://doi.org/10.15171/bi.2017.08 49. Foegeding, N., Caston, R, and McClain, M., An overview of Helicobacter pylori VacA toxin biology, Toxins, 2016, vol. 8, no. 6, p. 173. https://doi.org/10.3390/toxins8060173 50. Chauhan, N., Tay, A.C.Y., Marshall, B.J., and Jain, U., Helicobacter pylori VacA, a distinct toxin exerts diverse functionalities in numerous cells: an overview, Helicobacter, 2018, no. 16. https://doi.org/10.1111/hel.12544 51. McClain, M.S., Beckett, A.C., and Cover, T.L. Helicobacter pylori vacuolating toxin and gastric cancer, Toxins, 2017, vol. 12, no. 10. https://doi.org/10.3390/toxins91003l6 52. Ivie, S.E, McClain, M.S., and Algood, H., Analysis of a p-helical region in the p55 domain of Helicobacter pylori vacuolating toxin, BMC Microbiol., 2010, vol. 10, no. 1, p. 60. https://doi.org/10.1186/1471-2180-10-60 53. Palframan, S. L., Kwok, T., and Gabriel, K., Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis, Front. Cell. Inf. Microbiol., 2012, vol. 2, p. 92. https://doi.org/10.3389/fcimb.2012.00092 54. Foo, H., Culvenor, J.G, and Ferrero, R.L., Both the p33 and p55 subunits of the Helicobacter pylori VacA toxin are targeted to mammalian mitochondria, J. Mol. Biol., 2010, vol. 401, no. 5, pp. 792–798.https://doi.org/10.1016/j.jmb.2010.06.065 55. Yahiro, K., Hirayama, T., and Moss, J., New insights into VacA intoxication mediated through its cell surface receptors, Toxins, 2016, vol. 8, no. 5, p. 152. https://doi.org/10.3390/toxins8050152 |
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