Characterization of the solution properties and conformation of pneumolysin, the membrane-damaging toxin of Streptococcus pneumoniae.
Pneumolysin is a membrane-damaging toxin produced by Streptococcus pneumoniae. In order to understand fully the mode of action of this toxin, it is necessary to have an appreciation of the size, self-association behaviour and solution conformation of pneumolysin. A combination of analytical ultracentrifugation methodologies has shown that pneumolysin lacks self-association behaviour in solution and has provided a weight-average M(r) (M omega) of 52,000 +/- 2000, which was in agreement with that derived from the amino acid sequence. By determining a sedimentation coefficient (S20,w0) of 3.35 +/- 0.10 S, it was possible to suggest a model for the gross solution conformation of pneumolysin monomers. Spectroscopic methods provide additional secondary and tertiary structure information.
Morgan
P J
PJ
Department of Microbiology, University of Leicester, U.K.
Varley
P G
PG
Rowe
A J
AJ
Andrew
P W
PW
Mitchell
T J
TJ
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins; D002462:Cell Membrane / Q000187:drug effects; D002942:Circular Dichroism; D003603:Cytotoxins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013296:Streptococcus pneumoniae / Q000737:chemistry*; D013301:Streptolysins / Q000737:chemistry* / Q000633:toxicity; D014461:Ultracentrifugation
D000596:Amino Acids; D001426:Bacterial Proteins; D003603:Cytotoxins; D012996:Solutions; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae