Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Toxins
Share to Biopolymers

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Heat-Shock Proteins

Share to Hemolysin Proteins

Share to Hydrogen-Ion Concentration

Share to Listeria

Share to Molecular Structure

Source

Identifiers

PMID: 24751541
DOI: 10.1038/ncomms4690

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.PMID 24751541Read ↗

Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].Semantic proximity Read ↗

Listeriolysin O: a genuine cytolysin optimized for an intracellular parasite.Semantic proximity Read ↗

A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity.Semantic proximity Read ↗

Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.Semantic proximity Read ↗

The relationship between Listeria infections and host immune responses: Listeriolysin O as a potential targetSemantic proximity Read ↗

Mutants of listeriolysin O for enhanced liposomal delivery of macromolecules.Semantic proximity Read ↗

Structural basis for tuning activity and membrane specificity of bacterial cytolysins.Semantic proximity Read ↗

The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells.Semantic proximity Read ↗

Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.Semantic proximity Read ↗

Structural insights into loss of function of a pore forming toxin and its role in pneumococcal adaptation to an intracellular lifestyleSemantic proximity Read ↗

Critical role of the N-terminal residues of listeriolysin O in phagosomal escape and virulence of Listeria monocytogenes.Semantic proximity Read ↗

Structural insights into loss of function of a pore forming toxin and its role in pneumococcal adaptation to an intracellular lifestyleSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.