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Article

A Nonoligomerizing Mutant Form of Helicobacter pylori VacA Allows Structural Analysis of the p33 Domain.

Infection and immunity - 1 Sept 2016

González-Rivera Christian, Campbell Anne M, Rutherford Stacey A, Pyburn Tasia M, Foegeding Nora J, Barke Theresa L, Spiller Benjamin W, McClain Mark S, Ohi Melanie D, Lacy D Borden, Cover Timothy L

Abstract excerpt

Helicobacter pylori secretes a pore-forming VacA toxin that has structural features and activities substantially different from those of other known bacterial toxins. VacA can assemble into multiple types of water-soluble flower-shaped oligomeric structures, and most VacA activities are dependent on its capacity to oligomerize. The 88-kDa secreted VacA protein can undergo limited proteolysis to yield two domains,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 27382020
DOI: 10.1128/IAI.00254-16
PMCID: PMC4995914

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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