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Broadly protective protein-based pneumococcal vaccine composed of pneumolysin toxoid-CbpA peptide recombinant fusion protein.
Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.
Preclinical in vitro and in vivo profile of a highly-attenuated, broadly efficacious pneumolysin genetic toxoid.
The impact of pneumolysin on the macrophage response to Streptococcus pneumoniae is strain-dependent.
Pneumolysin Induces 12-Lipoxygenase-Dependent Neutrophil Migration during Streptococcus pneumoniae Infection.
The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.
Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae.
Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.
Multivalent Pneumococcal Protein Vaccines Comprising Pneumolysoid with Epitopes/Fragments of CbpA and/or PspA Elicit Strong and Broad Protection.
Pore Formation by Cholesterol Dependent Cytolysins