Localization of CagA effector protein of Helicobacter pylori in infected epithelial cells

January 1, 2012

Localization of CagA effector protein of Helicobacter pylori in infected epithelial cells

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Title:	Localization of CagA effector protein of Helicobacter pylori in infected epithelial cells
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Article_Title:	Localization of CagA effector protein of Helicobacter pylori in infected epithelial cells
Authors:	Ioana Lancrajan, Svetlana Kogalniceanu, Doru Ardelean, Gavril Ardelean
Affiliation:	“Vasile Goldis” Western University Arad, Romania
Abstract:	Epidemiological studies have shown the role of CagA-positive Helicobacter pylori (Hp) in development of atrophic gastritis, peptic ulcer disease and gastric carcinoma. CagA effector protein of bacterial pathogen Helicobacter pylori is translocated in host cell via TFSS and subsequently tyrosine phosphorylated. Both phosphorylated and non phosphorylated CagA activate multiple signal transduction pathways promoting disruption of cell-cell contacts, migration and the typical hummingbird phenotype (Bouzrac, Highasi). This study proposed to establish the location of CagA in epithelial cell in culture after infection with Hp. The interaction of extracellular protein CagA from Hp with membrane and cytoskeletal proteins of host cell is to expected, taking in account the multiple contribution of cagA in signal transduction and cell shape modifications, that implied membrane respectively cytoskeletal proteins. The experimental results give one image regarding the traffic of CagA in host cells. According to these data we conclude that Cag A is first, predominantly associated with membranes and cytoskeleton.
Keywords:	infection, cell culture, effector, membranes
References:	Bourzac, K. M., and Guillemin, K. 2005, Helicobacter pylori- host cell interactions mediated by type IV secretion . Cellular Microbiology, 7, 911-919. 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 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 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 Covacci, A., and R. Rappuoli. 2000., Tyrosinephosphorylated bacterial proteins:Trojan horses for the host cell. J. Exp. Med. 191:587–592. Dequiedt F, Van Lint J, Lecomte et al., 2005, Phosphorylation of histone deacetylase 7 by protein kinase D mediates Tcell receptor-induced Nurr77 expression and apoptosis., Exp.Med 201, p. 793-804 Hatekayama M 2009, Helicobacter pylori and gastric carcinogenesis, J. Gastroenterol 44: 239-248 Stein M, Rappouli R, Covvaci A 2000, Tyrosine phosphorylation of the Helicobacter pylori cagA antigen after cagA-driven host cell translocation, PNAS, 97(3): 1263-1268 Higashi, H., Tsutsumi, R., Fujita, A., Yamazaki, S., Asaka, M., Azuma, T., and Hatakeyama M., 2002, Biological activity of the Helicobacter pylori virulence factor CagA is determined by variation in the tyrosine phosphorylation sites. PNAS, 99, 14428-14433. Highasi H, Yokoyama K, Fujii Y, Ren S, et al, 2005, EPIYA motif is a membrane targeting signal of Helicobacter pylori virulence factor cagA in mammalian cells, J.Cell Biol, vol 280, no.24, pp. 23130-23137. Jones K, Whitmire M, Merrell S 2010, A tsle of two toxins: Helicobacter pylori cagA and VacA modulate host pathways that impact disease, Frontiers in Microbiology, vol 1, 1-15. Lindkvist B, Johansen D, Borgstrom A, Manjer J, 2008, A prospective study of Helicobacter pylori in relation toi the risk for pancreatic cancer, BioMed Central Cancer 8: 1-9 Martin J, Blaser F., 1998, Helicobacter pylori and gastric diseases, BMJ. 316(7143): 1507–1510. Phillips N, Hayward R. and Koronakis V., 2004, Phosphorylation of the enteropathogenic E. coli receptor by the Src-family kinase c-Fyn triggers actin pedestal formation, Nature cell biology 6(7), 618-626. Selbach M, Moese S, Hauck C, Meyer T, Backert S 2002, Src is the kinase of Helicobacter pylori CagA protein in vitro and in vivo, The Journal of Biological Chemistry, vol 277, no 9, pp.6775-6778.
Read_full_article:	pdf/21-2011/21-4-2011/SU21-4-2011-Lancrajan.pdf
Correspondence:	Ioana Lancrajan, Department of Toxicology, “Vasile Goldis” Western University Arad, Faculty of Natural Sciences, 93-95 Rebreanu St., 310396, Arad, Romania, email: Lancrajan_ioana @yahoo.com

	Read full article
Article Title:	Localization of CagA effector protein of Helicobacter pylori in infected epithelial cells
Authors:	Ioana Lancrajan, Svetlana Kogalniceanu, Doru Ardelean, Gavril Ardelean
Affiliation:	“Vasile Goldis” Western University Arad, Romania
Abstract:	Epidemiological studies have shown the role of CagA-positive Helicobacter pylori (Hp) in development of atrophic gastritis, peptic ulcer disease and gastric carcinoma. CagA effector protein of bacterial pathogen Helicobacter pylori is translocated in host cell via TFSS and subsequently tyrosine phosphorylated. Both phosphorylated and non phosphorylated CagA activate multiple signal transduction pathways promoting disruption of cell-cell contacts, migration and the typical hummingbird phenotype (Bouzrac, Highasi). This study proposed to establish the location of CagA in epithelial cell in culture after infection with Hp. The interaction of extracellular protein CagA from Hp with membrane and cytoskeletal proteins of host cell is to expected, taking in account the multiple contribution of cagA in signal transduction and cell shape modifications, that implied membrane respectively cytoskeletal proteins. The experimental results give one image regarding the traffic of CagA in host cells. According to these data we conclude that Cag A is first, predominantly associated with membranes and cytoskeleton.
Keywords:	infection, cell culture, effector, membranes
References:	Bourzac, K. M., and Guillemin, K. 2005, Helicobacter pylori- host cell interactions mediated by type IV secretion . Cellular Microbiology, 7, 911-919. 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 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 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 Covacci, A., and R. Rappuoli. 2000., Tyrosinephosphorylated bacterial proteins:Trojan horses for the host cell. J. Exp. Med. 191:587–592. Dequiedt F, Van Lint J, Lecomte et al., 2005, Phosphorylation of histone deacetylase 7 by protein kinase D mediates Tcell receptor-induced Nurr77 expression and apoptosis., Exp.Med 201, p. 793-804 Hatekayama M 2009, Helicobacter pylori and gastric carcinogenesis, J. Gastroenterol 44: 239-248 Stein M, Rappouli R, Covvaci A 2000, Tyrosine phosphorylation of the Helicobacter pylori cagA antigen after cagA-driven host cell translocation, PNAS, 97(3): 1263-1268 Higashi, H., Tsutsumi, R., Fujita, A., Yamazaki, S., Asaka, M., Azuma, T., and Hatakeyama M., 2002, Biological activity of the Helicobacter pylori virulence factor CagA is determined by variation in the tyrosine phosphorylation sites. PNAS, 99, 14428-14433. Highasi H, Yokoyama K, Fujii Y, Ren S, et al, 2005, EPIYA motif is a membrane targeting signal of Helicobacter pylori virulence factor cagA in mammalian cells, J.Cell Biol, vol 280, no.24, pp. 23130-23137. Jones K, Whitmire M, Merrell S 2010, A tsle of two toxins: Helicobacter pylori cagA and VacA modulate host pathways that impact disease, Frontiers in Microbiology, vol 1, 1-15. Lindkvist B, Johansen D, Borgstrom A, Manjer J, 2008, A prospective study of Helicobacter pylori in relation toi the risk for pancreatic cancer, BioMed Central Cancer 8: 1-9 Martin J, Blaser F., 1998, Helicobacter pylori and gastric diseases, BMJ. 316(7143): 1507–1510. Phillips N, Hayward R. and Koronakis V., 2004, Phosphorylation of the enteropathogenic E. coli receptor by the Src-family kinase c-Fyn triggers actin pedestal formation, Nature cell biology 6(7), 618-626. Selbach M, Moese S, Hauck C, Meyer T, Backert S 2002, Src is the kinase of Helicobacter pylori CagA protein in vitro and in vivo, The Journal of Biological Chemistry, vol 277, no 9, pp.6775-6778.
*Correspondence:	Ioana Lancrajan, Department of Toxicology, “Vasile Goldis” Western University Arad, Faculty of Natural Sciences, 93-95 Rebreanu St., 310396, Arad, Romania, email: Lancrajan_ioana @yahoo.com

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