Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.

doi:10.1038/ncomms4690

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Article

Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.

Nature communications - 22 Apr 2014

Köster Stefan, van Pee Katharina, Hudel Martina, Leustik Martin, Rhinow Daniel, Kühlbrandt Werner, Chakraborty Trinad, Yildiz Özkan

Abstract excerpt

Listeriolysin O (LLO) is an essential virulence factor of Listeria monocytogenes that causes listeriosis. Listeria monocytogenes owes its ability to live within cells to the pH- and temperature-dependent pore-forming activity of LLO, which is unique among cholesterol-dependent cytolysins. LLO enables the bacteria to cross the phagosomal membrane and is also involved in activation of cellular processes, including...

Topics

Amino Acid Sequence
Bacterial Toxins
Biopolymers
Crystallography, X-Ray
Heat-Shock Proteins
Hemolysin Proteins
Hydrogen-Ion Concentration
Listeria
Molecular Sequence Data
Molecular Structure
Mutation
Sequence Homology, Amino Acid
Temperature

Source

Open in PubMed

Identifiers

PMID: 24751541
DOI: 10.1038/ncomms4690

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