Wahid AA(1), Doekhie A(2), Sartbaeva A(3), van den Elsen JMH(4).
(1) Department of Biology and Biochemistry, University of Bath, Bath, UK.
(2) Department of Chemistry, University of Bath, Bath, UK.
(3) Department of Chemistry, University of Bath, Bath, UK. A.Sartbaeva@bath.ac.uk.
(4) Department of Biology and Biochemistry, University of Bath, Bath, UK.
There is an urgent need for the development of vaccine thermostabilisation methodologies as the maintenance of a continuous and reliable cold chain remains a major hurdle to the global distribution of safe and effective vaccines. Ensilication, a method that encases proteins in a resistant silica cage has been shown to physically prevent the thermal denaturation of a number of model proteins. In this study we investigate the utility of this promising approach in improving the thermal stability of antigens and vaccine conjugates highly relevant to the development of candidate tuberculosis vaccines, including antigen 85b conjugated with the Staphylococcus aureus-protein based adjuvant Sbi. Here we analyse the sensitivity of these constructs to thermal denaturation and demonstrate for the first time the benefits of ensilication in conferring these vaccine-relevant proteins with protection against temperature-induced loss of structure and function without the need for refrigeration. Our results reveal the potential of ensilication in facilitating the storage and transport of vaccines at ambient temperatures in the future and therefore in delivering life-saving vaccines globally, and in particular to remote areas of developing countries where disease rates are often highest.