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

• Published in: FEBS letters Vol. 583; no. 10; pp. 1581 - 1585
• Main Authors: Tosi, Tommaso, Cioci, Gianluca, Jouravleva, Karina, Dian, Cyril, Terradot, Laurent
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 19.05.2009
• Subjects: Bacterial toxin; Helicobacter pylori; Inflammatory response; MALT; mucosa-associated lymphoid tissue; Nucleus import; PBP; penicillin binding protein; SAD; single anomalous dispersion; Stomach cancer; TEV; tobacco etch virus; X-ray crystallography; X-ray crystallography; Bacterial toxin; TEV; Helicobacter pylori; Nucleus import; SAD; Inflammatory response; Stomach cancer; MALT; PBP
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2009.04.033

Helicobacter pylori secretes a unique virulence factor, Tipα, that enters gastric cells and both stimulates the production of the TNF-α and activates the NF-κB pathway. The structures of a truncated version of Tipα (TipαN34) in two crystal forms are presented here. Tipα adopts a novel β 1α 1α 2β 2β 3α 3α 4 topology that can be described as a combination of three domains. A first region consists in a short flexible extension, a second displays a dodecin-like fold and a third is a helical bundle domain similar to the sterile alpha motif (SAM). Analysis of the oligomerisation states of TipαN34 in the crystals and in solution suggests that the disulfide bridges could hold together Tipα monomers during their secretion in the gastric environment. MINT- 7033680: TIP alpha (uniprotkb: B2UTN0) and TIP alpha (uniprotkb:B2UTN0) bind (MI: 0407) by cosedimentation (MI: 0027)