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Water Accessibility, Aggregation, and Motional Features of Polysaccharide-Protein Conjugate Vaccines

Francesco Berti ^*, Paolo Costantino ^*, Marco Fragai  and Claudio Luchinat 

^* IRIS, Chiron SPA, 53100 Siena, Italy; CERM and Department of Chemistry, University of Florence, 50019 Sesto Fiorentino, Italy; and CERM and Department of Agricultural Biotechnology, University of Florence, 50019 Sesto Fiorentino, Italy

Correspondence: Address reprint requests to Claudio Luchinat, Fax: +39-055-4574253; E-mail: luchinat{at}cerm.unifi.it.

A relaxometric investigation of a nontoxic mutant of diphtheria toxin and of its conjugates with capsular polysaccharides of different groups of Neisseria meningitidis was performed. The insertion of polysaccharides chains alters dramatically the hydrodynamic properties of the protein. The model-free analysis of the ¹H nuclear magnetic relaxation dispersion profiles of their water solutions shows: i), a reduced protein hydration with respect to the carrier protein alone; ii), a much larger flexibility of the conjugates with respect to a compact macromolecule of the same molecular weight; and iii), a strong tendency to aggregate. The above findings are largely independent on the nature of the polysaccharide and thus provide a fairly general picture of the dynamic properties of glycoconjugate proteins.