CagA phosphorylation in Helicobacter pylori infection

January 14, 2013

CagA phosphorylation in Helicobacter pylori infection

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Title:	CagA phosphorylation in Helicobacter pylori infection
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Article_Title:	CagA phosphorylation in Helicobacter pylori infection
Authors:	Ioana Lancrajan, Monica Horge, Doru Ardelean, Ioan Puscas
Affiliation:	„Vasile Goldiş” Western University of Arad, Faculty of Life Sciences, Romania Prof. Dr. Ioan Puscas” City Hospital Simleul-Silvaniei, Cosbuc Str. 29, Simleul Silvaniei, Romania
Abstract:	The ability of CagA, the most studied bacterial virulence factor of Helicobacter pylori to act in both phosphorylated and non phosphorylated form in order to activate multiple signal transduction pathways, promoting disruption of cell-cell contacts, migration and the typical hummingbird phenotype are under inverstigations. The wide variety of cagA effects, a different molecular forms phosphorylated/ nonphosphorylated, lead us to investigate the location of phosphorylation immediately after infection. The cytosolic (cyt) and non cytosolic (noncyt) fractions of host cells were investigated for the ability to phosphorylate cagA, in order to establish the location of components implied in phosphorylation. The results indicate that recombinant FL-cagA can not be phosphorylated only by cytosol or Non-cytosol from MDCK cells. The phosphorylation take place with phosphorylation reaction buffer (ATP, Mg+2, phosphatase inhibitors). That is an evidence for supporting hypothesis that specific kinases located on cell membranes are needed to perform phosphorylation.
Keywords:	infection, kinase, membrane, virulence factor, cagA, Helicobacter pylori
References:	R. H. , Kidd M, Owen R.J., Thomas R. J., Limb M.C., Atherton J.C., Determinants and consequences of different levels of CagA phosphorylation for clinical isolates of Helicobacter pylori, Gastroenterology, 2004,127 (2):514-523 Bronte-Tinkew D, Mechanism of Helicobacter pylori Induced Gastric Cancer: Role of the Signal Transducer and Activator of Transcription Pathway, https://tspace.library.utoronto.ca/handle/1807/24694, Bronte-Tinkew_Dana_M_201006_PhD_thesis.pdf Bourzac, K. M., and Guillemin, K., 2005, Helicobacter pylori- host cell interactions mediated by type IV secretion. Cellular Microbiology, 7, 911-919. Calder P C.and Yaqoob P, Lipid Rafts—Composition, Characterization, and Controversies, 2007, Nutr. 137-3: 548–553 Covacci, A., Censini, S., Bugnoli, M., Petracca, R., Burroni, D., Macchia, G., Massone, A., Papini, E., Xiang, Z., Figura, N., and Rappouli, R., 1993, Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer., PNAS, 90, 5791-5795 Chitsazi MT, Fattahi E, Farahani R, Fattahi S 2006, Helicobacter pylori in the dental plaque: is it of diagnostic value for gastric infection?, Oral medicine and Pathology, 11: E325-8. Crew K, Neugut A, 2006, Epidemiology of gastric cancer, World J Gastroenterol January 21; 12(3): 354-362 Churin Y, Al-Ghoul L, Keep O, Meyer TF, Birchmeier, W Naumann M, 2003, Helicobacter pylori cagA protein targets the c-Met receptor and enhances the motogenic response, J Cell Biol 161, p. 249-255 Ernst P, 2000, The disease spectrum of Helicobacter pylori: The Immunopathogenesis of Gastroduodenal Ulcer and Gastric Cancer, Annual Review of Microbiology, Vol. 54: 615-640 Gauthier, N. C., Monzo, P., Gonzalez, T., Doye, A., Oldani, A., Gounon, P., Ricci, V., Cormont, M., and Boquet, P. , 2007, Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin, J. Cell Biol. 177, 343–354. Tegtmeyer N., Backert S., 2010, Role of Abl and Src family kinases in actin-cytoskeletal rearrangements induced by the Helicobacter pylori CagA protein, European Journal of Cell Biology, in press Odenbreit S, Püls J, Sedlmaier B, Gerland E, Fischer W and Haas R, Translocation of Helicobacter pylori CagA into Gastric Epithelial Cells by Type IV Secretion, Science, 2000, 287 (5457):1497-1500 Suzuki M, Mimuro H., Kiga K, Fukumatsu M, Ishijima N, Morikawa H, Nagai S, Koyasu S, Gilman H., Kersulyte D, Berg D E., Sasakawa C, 2009, Helicobacter pylori CagA Phosphorylation-Independent Function in Epithelial Proliferation and Inflammation, Cell Host & Microbe 5: 23–34. Yamasaki, E., Wada, A., Kumatori, A., Nakagawa, I., Funao, J., Nakayama, M., Hisatsune, J., Kimura, M., Moss, J., and Hirayama, T. , 2006, Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins Bax and Bak, leading to cytochrome c release and cell death, independent of vacuolation, J. Biol. Chem. 281, 11250–11259. Zhang Y, Argent R H., P D. Letley, J. R Thomas, and C. J Atherton, Tyrosine Phosphorylation of CagA from Chinese Helicobacter pylori Isolates in AGS Gastric Epithelial Cells. Journal Of Clinical Microbiology, 2005, 43 (2): 786–790
Read_full_article:	pdf/22-2012/22-4-2012/SU22-4-2012-Lancrajan.pdf
Correspondence:	Ioana Lancrajan, „Vasile Goldiş” Western University of Arad, Faculty of Life Sciences, Rebreanu str. 91-93; email: lancrajan _ioana@yahoo.com

	Read full article
Article Title:	CagA phosphorylation in Helicobacter pylori infection
Authors:	Ioana Lancrajan, Monica Horge, Doru Ardelean, Ioan Puscas
Affiliation:	„Vasile Goldiş” Western University of Arad, Faculty of Life Sciences, Romania Prof. Dr. Ioan Puscas” City Hospital Simleul-Silvaniei, Cosbuc Str. 29, Simleul Silvaniei, Romania
Abstract:	The ability of CagA, the most studied bacterial virulence factor of Helicobacter pylori to act in both phosphorylated and non phosphorylated form in order to activate multiple signal transduction pathways, promoting disruption of cell-cell contacts, migration and the typical hummingbird phenotype are under inverstigations. The wide variety of cagA effects, a different molecular forms phosphorylated/ nonphosphorylated, lead us to investigate the location of phosphorylation immediately after infection. The cytosolic (cyt) and non cytosolic (noncyt) fractions of host cells were investigated for the ability to phosphorylate cagA, in order to establish the location of components implied in phosphorylation. The results indicate that recombinant FL-cagA can not be phosphorylated only by cytosol or Non-cytosol from MDCK cells. The phosphorylation take place with phosphorylation reaction buffer (ATP, Mg+2, phosphatase inhibitors). That is an evidence for supporting hypothesis that specific kinases located on cell membranes are needed to perform phosphorylation.
Keywords:	infection, kinase, membrane, virulence factor, cagA, Helicobacter pylori
References:	R. H. , Kidd M, Owen R.J., Thomas R. J., Limb M.C., Atherton J.C., Determinants and consequences of different levels of CagA phosphorylation for clinical isolates of Helicobacter pylori, Gastroenterology, 2004,127 (2):514-523 Bronte-Tinkew D, Mechanism of Helicobacter pylori Induced Gastric Cancer: Role of the Signal Transducer and Activator of Transcription Pathway, https://tspace.library.utoronto.ca/handle/1807/24694, Bronte-Tinkew_Dana_M_201006_PhD_thesis.pdf Bourzac, K. M., and Guillemin, K., 2005, Helicobacter pylori- host cell interactions mediated by type IV secretion. Cellular Microbiology, 7, 911-919. Calder P C.and Yaqoob P, Lipid Rafts—Composition, Characterization, and Controversies, 2007, Nutr. 137-3: 548–553 Covacci, A., Censini, S., Bugnoli, M., Petracca, R., Burroni, D., Macchia, G., Massone, A., Papini, E., Xiang, Z., Figura, N., and Rappouli, R., 1993, Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer., PNAS, 90, 5791-5795 Chitsazi MT, Fattahi E, Farahani R, Fattahi S 2006, Helicobacter pylori in the dental plaque: is it of diagnostic value for gastric infection?, Oral medicine and Pathology, 11: E325-8. Crew K, Neugut A, 2006, Epidemiology of gastric cancer, World J Gastroenterol January 21; 12(3): 354-362 Churin Y, Al-Ghoul L, Keep O, Meyer TF, Birchmeier, W Naumann M, 2003, Helicobacter pylori cagA protein targets the c-Met receptor and enhances the motogenic response, J Cell Biol 161, p. 249-255 Ernst P, 2000, The disease spectrum of Helicobacter pylori: The Immunopathogenesis of Gastroduodenal Ulcer and Gastric Cancer, Annual Review of Microbiology, Vol. 54: 615-640 Gauthier, N. C., Monzo, P., Gonzalez, T., Doye, A., Oldani, A., Gounon, P., Ricci, V., Cormont, M., and Boquet, P. , 2007, Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin, J. Cell Biol. 177, 343–354. Tegtmeyer N., Backert S., 2010, Role of Abl and Src family kinases in actin-cytoskeletal rearrangements induced by the Helicobacter pylori CagA protein, European Journal of Cell Biology, in press Odenbreit S, Püls J, Sedlmaier B, Gerland E, Fischer W and Haas R, Translocation of Helicobacter pylori CagA into Gastric Epithelial Cells by Type IV Secretion, Science, 2000, 287 (5457):1497-1500 Suzuki M, Mimuro H., Kiga K, Fukumatsu M, Ishijima N, Morikawa H, Nagai S, Koyasu S, Gilman H., Kersulyte D, Berg D E., Sasakawa C, 2009, Helicobacter pylori CagA Phosphorylation-Independent Function in Epithelial Proliferation and Inflammation, Cell Host & Microbe 5: 23–34. Yamasaki, E., Wada, A., Kumatori, A., Nakagawa, I., Funao, J., Nakayama, M., Hisatsune, J., Kimura, M., Moss, J., and Hirayama, T. , 2006, Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins Bax and Bak, leading to cytochrome c release and cell death, independent of vacuolation, J. Biol. Chem. 281, 11250–11259. Zhang Y, Argent R H., P D. Letley, J. R Thomas, and C. J Atherton, Tyrosine Phosphorylation of CagA from Chinese Helicobacter pylori Isolates in AGS Gastric Epithelial Cells. Journal Of Clinical Microbiology, 2005, 43 (2): 786–790
*Correspondence:	Ioana Lancrajan, „Vasile Goldiş” Western University of Arad, Faculty of Life Sciences, Rebreanu str. 91-93; email: lancrajan _ioana@yahoo.com

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