|00:02:35||Application of DSC to structural studies on meningitis vaccines|
|00:16:02||Standard DSC service|
|00:19:20||Fit Model to Data|
|00:21:20||Differential Scanning Calorimetry|
|00:23:57||Jasco Circular Dichroism spectrometer|
|00:26:14||Protein Melt for HEL|
|00:30:59||A Model of FH Bound to C3b on self surface|
|00:34:00||Structure of fHbp|
|00:34:13||Structure of fHbp|
|00:34:36||Structure of fHbp|
|00:35:19||Structure of fHbp|
|00:36:20||Structure of fHbp|
|00:36:42||Structure of fHbp|
|00:38:04||Medical Research Council|
|00:38:18||Thank you for your attention|
Neisseria meningitidis is the leading cause of bacteraemia and sepsis in children and young adults due to the non-specific nature of the initial symptoms and rapid progress of the infection.
Vaccination is the best approach to protect individuals and progress has been made in their development. However the existing strategy cannot be used with serogroup B which is the commonest form of the disease in Europe and North America.
Efforts have been made to design functionally inactive but immunogenic fHbp as vaccine candidates. X-ray structures of V1 and 3 were obtained but only the carboxy beta barrel module was observed for V2.
Differential Scanning Calorimetry (DSC) was used to determine the folding stability of the fHbp variants to explain this observation. The advantages of DSC over other protein stability analyses will be discussed.