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High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy

scientific article published on September 2005

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Europe PubMed Central

5 October 2017

High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy (English)

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Europe PubMed Central

5 October 2017

cryogenic electron microscopy

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Jacques Dubochet

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Europe PubMed Central

5 October 2017

Timothy L Cover

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Catherine El-Bez

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1

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Europe PubMed Central

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16125415

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5 October 2017

Marc Adrian

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Europe PubMed Central

5 October 2017

1 September 2005

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Europe PubMed Central

5 October 2017

Journal of Structural Biology

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Europe PubMed Central

5 October 2017

151

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Europe PubMed Central

5 October 2017

3

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215-228

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5 October 2017

Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin

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Lipid interaction of the 37-kDa and 58-kDa fragments of the Helicobacter pylori cytotoxin.

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Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells

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A 12-amino-acid segment, present in type s2 but not type s1 Helicobacter pylori VacA proteins, abolishes cytotoxin activity and alters membrane channel formation

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The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.

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Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: possible implications for the mechanism of cellular vacuolation.

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Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity.

1 reference

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A dominant negative mutant of Helicobacter pylori vacuolating toxin (VacA) inhibits VacA-induced cell vacuolation

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Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin

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Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization.

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Oligomeric and subunit structure of the Helicobacter pylori vacuolating cytotoxin

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The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release

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Multiple oligomeric states of the Helicobacter pylori vacuolating toxin demonstrated by cryo-electron microscopy

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Structure and interaction of VacA of Helicobacter pylori with a lipid membrane

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Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion

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10.1016/J.JSB.2005.07.001

1 reference

stated in

Europe PubMed Central

5 October 2017

1 reference

Europe PubMed Central

PubMed ID

16125415

retrieved

5 October 2017

(Q41626935)

High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy

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