Pneumolysin: stimulating protection [PDF]
Nature Reviews Microbiology, 2010 A new paper inPLoS Pathogens on Streptococcus pneumoniaepneumolysin provides the first example of the involvement of the NLRP3 inflammasome in protection against a Gram-positive bacterium.
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Incomplete pneumolysin oligomers form membrane pores [PDF]
Open Biology, 2014 Pneumolysin is a member of the cholesterol-dependent cytolysin (CDC) family of pore-forming proteins that are produced as water-soluble monomers or dimers, bind to target membranes and oligomerize into large ring-shaped assemblies comprising approximately 40 subunits and approximately 30 nm across.
Sonnen, Andreas F.-P. +2 more
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Toxicity of pneumolysin to pulmonary alveolar epithelial cells [PDF]
Infection and Immunity, 1993 Mortality during the first several days of pneumococcal pneumonia has not decreased appreciably over the past 30 years, despite the widespread use of antibiotics. Disruption of the alveolar epithelial barrier is likely an initial step in the pathogenesis of pneumococcal pneumonia.
Jeffrey B. Rubins +5 more
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Pneumolysin activates neutrophil extracellular trap formation [PDF]
Clinical and Experimental Immunology, 2016 Summary The primary objective of the current study was to investigate the potential of the pneumococcal toxin, pneumolysin (Ply), to activate neutrophil extracellular trap (NET) formation in vitro. Isolated human blood neutrophils were exposed to recombinant Ply (5-20 ng ml−1) for 30–90 min at 37°C and NET formation measured using the ...
Nel, Jan Gert +7 more
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Back in Person: Frontiers in Medicinal Chemistry 2023
ChemMedChem, Volume 18, Issue 19, October 4, 2023., 2023 The Frontiers in Medicinal Chemistry (FiMC) is the largest international Medicinal Chemistry conference in the German speaking area and took place from April 3rd to 5th 2023 in Vienna (Austria). In this conference report, we review the highlights of the 38 lectures and more than 100 posters that were presented during this outstanding meeting.
Matthias Gehringer +10 more
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Structural investigations of pneumolysin/lipid complexes [PDF]
Molecular Membrane Biology, 2000 Pneumolysin, a virulence factor from the human pathogen Streptococcus pneumoniae, is a water-soluble protein which forms ring-shaped oligomeric structures upon binding to cholesterol-containing lipid membranes. It induces vesicle aggregation, membrane pore formation and withdrawal of lipid material into non-bilayer proteolipid complexes.
Bonev, B, Gilbert, R, Watts, A
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Pneumolysin mediates platelet activationin vitro [PDF]
10.1 Respiratory Infections, 2016 This study has explored the role of the pneumococcal toxin, pneumolysin (Ply), in activating human platelets. Following exposure to Ply (10-80 ng/ml), platelet activation and cytosolic Ca(2+) concentrations were measured flow cytometrically according to the level of expression of CD62P (P-selectin) and spectrofluorimetrically, respectively. Exposure to
Nel, Jan Gert +5 more
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Immunizations with pneumococcal surface protein A and pneumolysin are protective against pneumonia in a murine model of pulmonary infection with Streptococcus pneumoniae [PDF]
, 2003 Intranasal infection of mice with certain strains of capsular group 19 Streptococcus pneumoniae can result in focal pneumonia in the absence of bacteremia.
Briles, D. +6 more
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Extracellular calcium reduction strongly increases the lytic capacity of pneumolysin from streptococcus pneumoniae in brain tissue [PDF]
, 2011 Background. Streptococcus pneumoniae causes serious diseases such as pneumonia and meningitis. Its major pathogenic factor is the cholesterol-dependent cytolysin pneumolysin, which produces lytic pores at high concentrations.
Asparouh I. Iliev +40 more
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The interrelationship between phagocytosis, autophagy and formation of neutrophil extracellular traps following infection of human neutrophils by Streptococcus pneumoniae [PDF]
, 2017 Neutrophils play an important role in the innate immune response to infection with Streptococcus pneumoniae, the pneumococcus. Pneumococci are phagocytosed by neutrophils and undergo killing after ingestion.
Evans, Tom J. +2 more
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