Structure et mode d’injection de l’oncoprotéine CagA d’Helicobacter pylori

Burcu Kaplan-Türköz; Laurent Terradot

doi:10.1051/medsci/2013291011

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Volume 29 / Numéro 1 (Janvier 2013)

Med Sci (Paris), 29 1 (2013) 33-36

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Numéro		Med Sci (Paris) Volume 29, Numéro 1, Janvier 2013


Page(s)		33 - 36
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2013291011
Publié en ligne		25 janvier 2013

Covacci A, Censini S, Bugnoli M, et al. Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer. Proc Natl Acad Sci USA 1993 ; 90 : 5791–5795. [CrossRef] [Google Scholar]
Ohnishi N, Yuasa H, Tanaka S, et al. Transgenic expression of Helicobacter pylori CagA induces gastrointestinal and hematopoietic neoplasms in mouse. Proc Natl Acad Sci USA 2008 ; 105 : 1003–1008. [CrossRef] [Google Scholar]
Backert S, Clyne M, Tegtmeyer N. Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori. Cell Commun Signal 2011 ; 9 : 28. [CrossRef] [PubMed] [Google Scholar]
Nesic D, Miller MC, Quinkert ZT, et al. Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nat Struct Mol Biol 2010 ; 17 : 130–132. [CrossRef] [PubMed] [Google Scholar]
Angelini A, Tosi T, Mas P, et al. Expression of Helicobacter pylori CagA domains by library-based construct screening. FEBS J 2009 ; 276 : 816–824. [CrossRef] [PubMed] [Google Scholar]
Kaplan-Turkoz B, Jimenez-Soto LF, Dian C, et al. Structural insights into Helicobacter pylori oncoprotein CagA interaction with beta1 integrin. Proc Natl Acad Sci USA 2012 ; 109 : 14640–14645. [CrossRef] [Google Scholar]
Murata-Kamiya N, Kikuchi K, Hayashi T, et al. Helicobacter pylori exploits host membrane phosphatidylserine for delivery, localization, and pathophysiological action of the CagA oncoprotein. Cell Host Microbe 2010 ; 7 : 399–411. [CrossRef] [PubMed] [Google Scholar]
Jimenez-Soto LF, Kutter S, Sewald X, et al. Helicobacter pylori type IV secretion apparatus exploits beta1 integrin in a novel RGD-independent manner. PLoS Pathog 2009 ; 5 : e1000684. [CrossRef] [PubMed] [Google Scholar]
Pulzova L, Kovac A, Mucha R, et al. OspA-CD40 dyad: ligand-receptor interaction in the translocation of neuroinvasive Borrelia across the blood-brain barrier. Sci Rep 2011 ; 1 : 86. [CrossRef] [PubMed] [Google Scholar]
Hayashi T, Senda M, Morohashi H, et al. Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. Cell Host Microbe 2012 ; 12 : 20–33. [CrossRef] [PubMed] [Google Scholar]
Foulongne V, Michaux-Charachon S, O’Callaghan D, Ramuz M. Systèmes de sécrétion des protéines de type IV et virulence bactérienne. Med Sci (Paris) 2002 ; 18 : 439–447. [CrossRef] [EDP Sciences] [Google Scholar]

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[1] Covacci A, Censini S, Bugnoli M, et al. Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer. Proc Natl Acad Sci USA 1993 ; 90 : 5791–5795. [CrossRef] [Google Scholar]

[2] Ohnishi N, Yuasa H, Tanaka S, et al. Transgenic expression of Helicobacter pylori CagA induces gastrointestinal and hematopoietic neoplasms in mouse. Proc Natl Acad Sci USA 2008 ; 105 : 1003–1008. [CrossRef] [Google Scholar]

[3] Backert S, Clyne M, Tegtmeyer N. Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori. Cell Commun Signal 2011 ; 9 : 28. [CrossRef] [PubMed] [Google Scholar]

[4] Nesic D, Miller MC, Quinkert ZT, et al. Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nat Struct Mol Biol 2010 ; 17 : 130–132. [CrossRef] [PubMed] [Google Scholar]

[5] Angelini A, Tosi T, Mas P, et al. Expression of Helicobacter pylori CagA domains by library-based construct screening. FEBS J 2009 ; 276 : 816–824. [CrossRef] [PubMed] [Google Scholar]

[6] Kaplan-Turkoz B, Jimenez-Soto LF, Dian C, et al. Structural insights into Helicobacter pylori oncoprotein CagA interaction with beta1 integrin. Proc Natl Acad Sci USA 2012 ; 109 : 14640–14645. [CrossRef] [Google Scholar]

[7] Murata-Kamiya N, Kikuchi K, Hayashi T, et al. Helicobacter pylori exploits host membrane phosphatidylserine for delivery, localization, and pathophysiological action of the CagA oncoprotein. Cell Host Microbe 2010 ; 7 : 399–411. [CrossRef] [PubMed] [Google Scholar]

[8] Jimenez-Soto LF, Kutter S, Sewald X, et al. Helicobacter pylori type IV secretion apparatus exploits beta1 integrin in a novel RGD-independent manner. PLoS Pathog 2009 ; 5 : e1000684. [CrossRef] [PubMed] [Google Scholar]

[9] Pulzova L, Kovac A, Mucha R, et al. OspA-CD40 dyad: ligand-receptor interaction in the translocation of neuroinvasive Borrelia across the blood-brain barrier. Sci Rep 2011 ; 1 : 86. [CrossRef] [PubMed] [Google Scholar]

[10] Hayashi T, Senda M, Morohashi H, et al. Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. Cell Host Microbe 2012 ; 12 : 20–33. [CrossRef] [PubMed] [Google Scholar]

[11] Foulongne V, Michaux-Charachon S, O’Callaghan D, Ramuz M. Systèmes de sécrétion des protéines de type IV et virulence bactérienne. Med Sci (Paris) 2002 ; 18 : 439–447. [CrossRef] [EDP Sciences] [Google Scholar]