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

Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae.

Journal of structural biology - 1 Feb 2016

Park Seong Ah, Park Ye Song, Bong Seoung Min, Lee Ki Seog

Abstract excerpt

Cholesterol-dependent cytolysins (CDCs) contribute to various pathogenesis by Gram-positive bacterial pathogens. Among them, pneumolysin (PLY) produced by Streptococcus pneumoniae is a major contributor to pneumococcal infections. Despite numerous studies of the cytolytic mechanism of PLY, little structural information on its interactions with a specific receptor of the cell membrane is available. We report here...

Topics

Bacterial Proteins
Cell Membrane
Cholesterol
Crystallography, X-Ray
Hemolysis
Humans
Mannose
Models, Molecular
Molecular Docking Simulation
Mutation
Protein Structure, Tertiary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Streptolysins

Structure-Activity Relationship

Source

Identifiers

PMID: 26688057
DOI: 10.1016/j.jsb.2015.12.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae.PMID 26688057Read ↗

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Semantic proximity Read ↗

The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells.Semantic proximity Read ↗

Pneumolysin: Pathogenesis and Therapeutic TargetSemantic proximity Read ↗

The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.Semantic proximity Read ↗

Mapping of Recognition Sites of Monoclonal Antibodies Responsible for the Inhibition of Pneumolysin Functional ActivitySemantic 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 ↗

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

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

A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related ProteinsSemantic proximity Read ↗

Cytotoxic property of Streptococcus mitis strain producing two different types of cholesterol-dependent cytolysins.Semantic proximity Read ↗

Pneumolysin: A Double-Edged Sword During the Host-Pathogen InteractionSemantic proximity Read ↗

Crystal structure of cytotoxin protein suilysin from Streptococcus suisSemantic proximity Read ↗

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