Modern subcellular vaccines are based on glycoconjugates prepared from pathogen surface saccharides and a protein carrier. Immunological efficiency of glycoconjugate vaccines is highly dependent on their construct architecture. Low efficiency of short oligosaccharide antigens is usually overcome by their multivalent attachment onto a dendrimeric scaffold construct. Here we propose alternative solution to avoid that demanding approach. First we changed the functionality of the protein terminal amino groups. This resulted in highly carboxylated protein with no amino groups exposed which also eliminates unwanted protein cross-linking during the conjugation reaction that follows. The model studies revealed that bovine serum albumin treated this way is capable to bind as many as 40 molecules of aminosaccharides. The resultant glycoconjugate products were analysed by using MALDI-TOF mass spectrometry for details of their structure.
Acknowledgement
The work was supported by the Grant Agency VEGA , grant No.2/0026/13
