203
the identified glycation sites (30 lysine residues) being higher than the determined
(hapten: BSA ratio 5.4:1) of the tetrasaccharide-BSA neoglycoconjugate, it was
concluded that the vaccine is composed of a mixture of glycoforms.
11.9 Conclusion
The systematic investigations presented herein constitute a series of versatile examples for the identification of accurate quality control necessary in commercial production of glycoconjugate vaccines against infectious diseases. The glycopeptides
isolated and fully characterized during this work may well represent useful reference compounds to be used in standardization analyses.
Moreover, although BSA usually serves a universal model carrier protein for novel
conjugation chemistry, we found it perfectly legitimate as a vaccine in mouse
Fig. 11.9 (a) BSA sequence where the glycation sites are indicated by an asterisk (red = identified. on tryptic digests, blue = identified on GluC V8 digests and red and underlined = identified
on both tryptic and GluC V8 digests) and (b) 3D structure of the BSA. The glycated lysine residues
are highlighted in red (Swiss-Pdb Viewer software) [69]
11 Defense Against Biological Terrorism: Vaccines and Their Characterizations
Précédent

- 214/286

Suivant