Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its EPIYA-D motif to potentiate the oncogenicity

References

• Warren JR, Marshall B. Unidentified curved bacilli on gastric epithelium in active chronic gastritis. Lancet. 1983;1(8336):1273–17. doi: 10.1016/S0140-6736(83)92719-8
   PubMed Web of Science ®Google Scholar
• Hooi JKY, Lai WY, Ng WK, et al. Global Prevalence of Helicobacter pylori Infection: Systematic Review and Meta-Analysis. Gastroenterology. 2017;153(2):420–429. doi: 10.1053/j.gastro.2017.04.022
   PubMed Web of Science ®Google Scholar
• Jiang J, Chen Y, Shi J, et al. Population attributable burden of Helicobacter pylori-related gastric cancer, coronary heart disease, and ischemic stroke in China. Eur J Clin Microbiol Infect Dis. 2017;36(2):199–212. doi: 10.1007/s10096-016-2810-x
   PubMed Web of Science ®Google Scholar
• de Brito BB, Silva FAFD, Soares AS, et al. Pathogenesis and clinical management of Helicobacter pylori gastric infection. World J Gastroenterol. 2019;25(37):5578–5589. doi: 10.3748/wjg.v25.i37.5578
   PubMed Web of Science ®Google Scholar
• Ansari S, Yamaoka Y. Helicobacter pylori virulence factors exploiting gastric colonization and its pathogenicity. Toxins (Basel). 2019;11(11):677. doi: 10.3390/toxins11110677
   PubMed Web of Science ®Google Scholar
• Backert S, Blaser MJ. The Role of CagA in the gastric biology of helicobacter pylori. Cancer Res. 2016;76(14):4028–4031. doi: 10.1158/0008-5472.CAN-16-1680
   PubMed Web of Science ®Google Scholar
• Hatakeyama M. Oncogenic mechanisms of the Helicobacter pylori CagA protein. Nat Rev Cancer. 2004;4(9):688–694. doi: 10.1038/nrc1433
   PubMed Web of Science ®Google Scholar
• Backert S, Tegtmeyer N, Fischer W. Composition, structure and function of the Helicobacter pylori cag pathogenicity island encoded type IV secretion system. Future Microbiol. 2015;10(6):955–965. doi: 10.2217/fmb.15.32
   PubMed Web of Science ®Google Scholar
• Backert S, Tegtmeyer N, Selbach M. The versatility of Helicobacter pylori CagA effector protein functions: The master key hypothesis. Helicobacter. 2010;15(3):163–176. doi: 10.1111/j.1523-5378.2010.00759.x
   PubMed Web of Science ®Google Scholar
• Hayashi T, Senda M, Suzuki N, et al. Differential mechanisms for SHP2 Binding and activation are exploited by geographically distinct Helicobacter pylori CagA Oncoproteins. Cell Rep. 2017;20(12):2876–2890. doi: 10.1016/j.celrep.2017.08.080
   PubMed Web of Science ®Google Scholar
• Pesesse X, Deleu S, De Smedt F, et al. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997;239(3):697–700. doi: 10.1006/bbrc.1997.7538
   PubMed Web of Science ®Google Scholar
• Thomas MP, Erneux C, Potter BV. SHIP2: Structure, function and inhibition. Chembiochem. 2017;18(3):233–247. doi: 10.1002/cbic.201600541
   PubMed Web of Science ®Google Scholar
• Fu M, Fan W, Pu X, et al. Elevated expression of SHIP2 correlates with poor prognosis in non-small cell lung cancer. Int J Clin Exp Pathol. 2013;6(10):2185–2191.
   PubMed Web of Science ®Google Scholar
• Ye Y, Ge YM, Xiao MM, et al. Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt. J Gastroenterol. 2016;51(3):230–240. doi: 10.1007/s00535-015-1101-0
   PubMed Web of Science ®Google Scholar
• Fujii Y, Murata-Kamiya N, Hatakeyama M. Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells. Cancer Sci. 2020;111(5):1596–1606. doi: 10.1111/cas.14391
   PubMed Web of Science ®Google Scholar
• Ji X, Zhao H, Zhang Y, et al. Construction of novel plasmid vectors for gene knockout in Helicobacter pylori. Curr Microbiol. 2016;73(6):897–903. doi: 10.1007/s00284-016-1140-7
   PubMed Web of Science ®Google Scholar
• Ji X, Wang Y, Li J, et al. Application of FLP-FRT System to construct unmarked deletion in helicobacter pylori and functional study of gene hp0788 in pathogenesis. Front Microbiol. 2017;8:2357. doi: 10.3389/fmicb.2017.02357
   PubMed Web of Science ®Google Scholar
• Galindo-Murillo R, Robertson JC, Zgarbová M, et al. Assessing the current state of amber force field modifications for DNA. J Chem Theory Comput. 2016;12(8):4114–4127. doi: 10.1021/acs.jctc.6b00186
   PubMed Web of Science ®Google Scholar
• Bryant P, Pozzati G, Elofsson A. Improved prediction of protein-protein interactions using AlphaFold2. Nat Commun. 2022;13(1):1265. doi: 10.1038/s41467-022-28865-w
   PubMed Web of Science ®Google Scholar
• Friedrichs MS, Eastman P, Vaidyanathan V, et al. Accelerating molecular dynamic simulation on graphics processing units. J Comput Chem. 2009;30(6):864–872. doi: 10.1002/jcc.21209
   PubMed Web of Science ®Google Scholar
• Zhao H, Ji X, Chen X, et al. Functional study of gene hp0169 in Helicobacter pylori pathogenesis. Microb Pathog. 2017;104:225–231. doi: 10.1016/j.micpath.2017.01.039
   PubMed Web of Science ®Google Scholar
• Sousa da Silva AW, Vranken WF. ACPYPE - AnteChamber python parser interface. BMC Res. 2016;5:367. doi: 10.1186/1756-0500-5-367
   Google Scholar
• Wang J, Wolf RM, Caldwell JW, Kollman PA, Case D A. Development and testing of a general amber force field. J Comput Chem. 2004;25:1157–1174. doi: 10.1002/jcc.20035
   PubMed Web of Science ®Google Scholar
• Hess B, Bekker H, Berendsen HJC, et al. LINCS: A linear constraint solver for molecular simulations. J Comput Chem. 1997;18(12):1463–1472. doi: 10.1002/(SICI)1096-987X(199709)18:12<1463:AID-JCC4>3.0.CO;2-H
   Web of Science ®Google Scholar
• Kräutler V, Gunsteren WFV, Hünenberger PH. A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J Comput Chem. 2001;22(5):501–508. doi: 10.1002/1096-987X(20010415)22:5<501:AID-JCC1021>3.0.CO;2-V
   Web of Science ®Google Scholar
• Lu H, Hsu PI, Graham DY, et al. Duodenal ulcer promoting gene of Helicobacter pylori. Gastroenterology. 2005;128(4):833–848. doi: 10.1053/j.gastro.2005.01.009
   PubMed Web of Science ®Google Scholar
• Zhao Q, Busch B, Jiménez-Soto LF, et al. Integrin but not CEACAM receptors are dispensable for Helicobacter pylori CagA translocation. PLOS Pathog. 2018;14(10):e1007359. doi: 10.1371/journal.ppat.1007359
   PubMed Web of Science ®Google Scholar
• Xu L, Shao Y, Ren L, et al. IQGAP2 inhibits migration and invasion of gastric cancer cells via elevating SHIP2 phosphatase activity. Int J Mol Sci. 2020;21(6):1968. doi: 10.3390/ijms21061968
   PubMed Web of Science ®Google Scholar
• Pedicone C, Meyer ST, Chisholm JD, et al. Targeting SHIP1 and SHIP2 in Cancer. Cancers (Basel). 2021;13(4):890. doi: 10.3390/cancers13040890
   PubMed Web of Science ®Google Scholar
• Zhou X, Li T-M, Luo J-Z, et al. CYP2C8 suppress proliferation, migration, invasion and sorafenib resistance of hepatocellular carcinoma via PI3K/Akt/p27(kip1) Axis. J Hepatocell Carcinoma. 2021;8:1323–1338. doi: 10.2147/JHC.S335425
   PubMed Web of Science ®Google Scholar
• Brandt S, Kwok T, Hartig R, et al. NF-κB activation and potentiation of proinflammatory responses by the Helicobacter pylori CagA protein. Proc Natl Acad Sci USA. 2005;102(26):9300–9305. doi: 10.1073/pnas.0409873102
   PubMed Web of Science ®Google Scholar
• Azuma T, Yamazaki S, Yamakawa A, et al. Association between diversity in the Src homology 2 domain–containing tyrosine phosphatase binding site of Helicobacter pylori CagA protein and gastric atrophy and cancer. J Infect Dis. 2004;189(5):820–827. doi: 10.1086/381782
   PubMed Web of Science ®Google Scholar
• Lang BJ, Gorrell RJ, Tafreshi M, et al. The Helicobacter pylori cytotoxin CagA is essential for suppressing host heat shock protein expression. Cell Stress Chaperones. 2016;21(3):523–533. doi: 10.1007/s12192-016-0680-x
   PubMed Web of Science ®Google Scholar
• Higashi H, Tsutsumi R, Muto S, et al. SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science. 2002;295(5555):683–686. doi: 10.1126/science.1067147
   PubMed Web of Science ®Google Scholar
• Elong Edimo W, Schurmans S, Roger PP, et al. SHIP2 signaling in normal and pathological situations: Its impact on cell proliferation. Adv Biol Regul. 2014;54:142–151. doi: 10.1016/j.jbior.2013.09.002
   PubMedGoogle Scholar
• Wang Z, Shan Y, Wang R, et al. Structural Insights into the Binding Propensity of Human SHIP2 SH2 to Oncogenic CagA Isoforms from Helicobacter pylori. Int J Mol Sci. 2022;23(19):11299. doi: 10.3390/ijms231911299
   PubMed Web of Science ®Google Scholar