Structures of the tumor necrosis factor α inducing protein Tipα: A novel virulence factor from Helicobacter pylori

FEBS Letters

Volumn 583, Issue 10, 2009, Pages 1581-1585

  Tosi, Tommaso ^a   Cioci, Gianluca ^a   Jouravleva, Karina ^a   Dian, Cyril ^a   Terradot, Laurent ^a  

^a EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

Bacterial toxin; Helicobacter pylori; Inflammatory response; Nucleus import; Stomach cancer; X ray crystallography

Indexed keywords

DISULFIDE; MONOMER; TUMOR NECROSIS FACTOR ALPHA INDUCING PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HELICOBACTER PYLORI; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; STOMACH; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HELICOBACTER PYLORI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; VIRULENCE FACTORS;

BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI;

EID: 65549100550     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.04.033     Document Type: Article

References (23)

1. IARC. Schistosomes, liver flukes and Helicobacter pylori. IARC Working Group on the evaluation of carcinogenic risks to humans. Lyon, 7-14 June 1994. IARC Monogr. Eval. Carcinog. Risks Hum. 61 (1994) 1-241
2. Franco A.T., et al. Regulation of gastric carcinogenesis by Helicobacter pylori virulence factors. Cancer Res. 68 (2008) 379-387
3. Ferreira A.C., Isomoto H., Moriyama M., Fujioka T., Machado J.C., and Yamaoka Y. Helicobacter and gastric malignancies. Helicobacter 13 Suppl. 1 (2008) 28-34
4. McNamara D., and El-Omar E. Helicobacter pylori infection and the pathogenesis of gastric cancer: a paradigm for host-bacterial interactions. Dig. Liver Dis. 40 (2008) 504-509
5. Yoshida M., et al. Cloning and characterization of a novel membrane-associated antigenic protein of Helicobacter pylori. Infect. Immun. 67 (1999) 286-293
6. Suganuma M., Kurusu M., Suzuki K., Nishizono A., Murakami K., Fujioka T., and Fujiki H. New tumor necrosis factor-alpha-inducing protein released from Helicobacter pylori for gastric cancer progression. J. Cancer Res. Clin. Oncol. 131 (2005) 305-313
7. Suganuma M., Kurusu M., Okabe S., Sueoka N., Yoshida M., Wakatsuki Y., and Fujiki H. Helicobacter pylori membrane protein 1: a new carcinogenic factor of Helicobacter pylori. Cancer Res. 61 (2001) 6356-6359
8. Cheng P., Shi R.H., Zhang H.J., Yu L.Z., Zhang G.X., and Hao B. Effects of tumor necrosis factor-alpha inducing protein-alpha secreted by Helicobacter pylori on human gastric epithelial cells. Zhonghua Yi Xue Za Zhi 88 (2008) 1528-1532
9. Kuzuhara T., Suganuma M., Kurusu M., and Fujiki H. Helicobacter pylori-secreting protein Tipalpha is a potent inducer of chemokine gene expressions in stomach cancer cells. J. Cancer Res. Clin. Oncol. 133 (2007) 287-296
10. Suganuma M., et al. TNF-alpha-inducing protein, a carcinogenic factor secreted from H. pylori, enters gastric cancer cells. Int. J. Cancer 123 (2008) 117-122
11. Kuzuhara T., Suganuma M., Tsuge H., and Fujiki H. Presence of a motif conserved between Helicobacter pylori TNF-alpha inducing protein (Tipalpha) and penicillin-binding proteins. Biol. Pharm. Bull. 28 (2005) 2133-2137
12. Godlewska R., Pawlowski M., Dzwonek A., Mikula M., Ostrowski J., Drela N., and Jagusztyn-Krynicka E.K. Tip-alpha (hp0596 gene product) is a highly immunogenic Helicobacter pylori protein involved in colonization of mouse gastric mucosa. Curr. Microbiol. 56 (2008) 279-286
13. Suganuma M., Kuzuhara T., Yamaguchi K., and Fujiki H. Carcinogenic role of tumor necrosis factor-alpha inducing protein of Helicobacter pylori in human stomach. J. Biochem. Mol. Biol. 39 (2006) 1-8
14. Kuzuhara T., Suganuma M., Oka K., and Fujiki H. DNA-binding activity of TNF-alpha inducing protein from Helicobacter pylori. Biochem. Biophys. Res. Commun. 362 (2007) 805-810
15. de La Fortelle, E. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods.
16. Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
17. Murshudov G.N., Vagin A.A., Lebedev A., Wilson K.S., and Dodson E.J. Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 247-255
18. McCoy A.J., Grosse-Kunstleve R.W., Adams P.D., Winn M.D., Storoni L.C., and Read R.J. Phaser crystallographic software. J. Appl. Crystallogr. 40 (2007) 658-674
19. Holm L., and Sander C. Dictionary of recurrent domains in protein structures. Proteins 33 (1998) 88-96
20. Grininger M., Seiler F., Zeth K., and Oesterhelt D. Dodecin sequesters FAD in closed conformation from the aqueous solution. J. Mol. Biol. 364 (2006) 561-566
21. Grant R.P., et al. Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2. J. Mol. Biol. 376 (2008) 1048-1059
22. Ponting C.P. SAM: a novel motif in yeast sterile and Drosophila polyhomeotic proteins. Protein Sci. 4 (1995) 1928-1930
23. Kim C.A., and Bowie J.U. SAM domains: uniform structure, diversity of function. Trends Biochem. Sci. 28 (2003) 625-628