Oligomerisation of pneumolysin on cholesterol crystals: similarities to the behaviour of polyene antibiotics.
Pneumolysin is a cytolytic toxin of Streptococcus pneumoniae, a causative agent of pneumonia and meningitis. The prepore and pore states of pneumolysin have recently been investigated by cryo-electron microscopy and atomic force microscopy, confirming the existence of arc-shaped as well as ring-form oligomers. Here we provide further insights into the pneumolysin oligomer by studying the interaction of pneumolysin with cholesterol crystals, comparing the results to those obtained for polyene antibiotics, which also bind cholesterol.
Sonnen
Andreas F-P
AF
Division of Structural Biology, The Henry Wellcome Building for Human Genetics, University of Oxford, Oxford, UK.
Rowe
Arthur J
AJ
Andrew
Peter W
PW
Gilbert
Robert J C
RJ
D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D002784:Cholesterol / Q000737:chemistry*; D021621:Imaging, Three-Dimensional; D008854:Microscopy, Electron; D008958:Models, Molecular; D011090:Polyenes / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013296:Streptococcus pneumoniae / Q000472:pathogenicity; D013301:Streptolysins / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D011090:Polyenes; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; D002784:Cholesterol