Pneumolysin activates the NLRP3 inflammasome and promotes proinflammatory cytokines independently of TLR4.

Pneumolysin (PLY) is a key Streptococcus pneumoniae virulence factor and potential candidate for inclusion in pneumococcal subunit vaccines. Dendritic cells (DC) play a key role in the initiation and instruction of adaptive immunity, but the effects of PLY on DC have not been widely investigated. Endotoxin-free PLY enhanced costimulatory molecule expression on DC but did not induce cytokine secretion.

Humoral autoimmune responses to the squamous cell carcinoma antigen protein family in psoriasis.

Substantial evidence indicates that psoriasis is a T-lymphocyte-mediated autoimmune disease. However, longstanding data also indicate IgG and complement deposition in upper epidermis of psoriasis plaques. This led us to propose that autoantigen-autoantibody interactions in the skin may also be of pathogenic importance.

Pneumolysin generates multiple conductance pores in the membrane of nucleated cells.

Patch clamping was used to investigate, for the first time, the electrophysiological properties of pores formed by a cholesterol-dependent cytolysin in the membrane of nucleated cells rather than in artificial membranes as previously. Pneumolysin pores in inside-out patches of CHO cell membranes had a broad range of conductance classified into small (<200 pS), medium (>200 pS and <1 nS) and large (>1 nS). A lytic-deficient mutant of pneumolysin (W433F) induced a similar spectrum of channels but there were more small channels than with wild-type (WT) toxin and the number of events was decreased.

Increased blood levels of IgG reactive with secreted Streptococcus pyogenes proteins in chronic plaque psoriasis.

A pathogenic role for Streptococcus (S) pyogenes infections in chronic plaque psoriasis is suspected but poorly defined. We separated cellular and supernatant proteins from S. pyogenes cultures by high-resolution two-dimensional gel electrophoresis, and used immunoblotting to demonstrate the diversity of serum or plasma IgGs that react with elements of the proteome of this bacterium.