Date recorded: June 25 2015

Duration: 45 minutes 41 seconds

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.

Table of contents
1. Welcome
02:35
2. Application of DSC to structural studies on meningitis vaccines
00:08
3. Content
00:14
4. Arbre
00:36
5. Equipment
00:39
6. Characterisation
00:40
7. Stability
01:06
8. Stability
03:31
9. VP-Capillary DSC
05:44
10. Applications
00:49
11. Standard DSC service
02:16
12. Raw Scans
00:43
13. Untitled
00:19
14. Fit Model to Data
00:34
15. Stability
00:06
16. Thermofluor Assays
00:16
17. Raw Data
01:04
18. Differential Scanning Calorimetry
00:23
19. Untitled
01:20
20. Raw Data
00:54
21. Jasco Circular Dichroism spectrometer
01:40
22. Circular Dichroism
00:37
23. Protein Melt for HEL
00:42
24. Limitations
01:27
25. Untitled
00:15
26. Neisseria Meningitidis
00:51
27. Vaccine candidates
01:30
28. A Model of FH Bound to C3b on self surface
00:47
29. fHbp
01:13
30. fHbp
00:40
31. fHbp
00:21
32. Structure of fHbp
00:13
33. Structure of fHbp
00:23
34. Structure of fHbp
00:43
35. Structure of fHbp
01:01
36. Structure of fHbp
00:22
37. Structure of fHbp
00:51
38. Conclusions
00:31
39. Medical Research Council
00:14
40. Thank you for your attention
06:43
41. Contact Information
00:40