Abstract
The recombinant heat shock protein (18 kDa-hsp) from Mycobacterium leprae was studied as a T-epitope model for vaccine development. We present a structural analysis of the stability of recombinant 18 kDa-hsp during different processing steps. Circular dichroism and ELISA were used to monitor protein structure after thermal stress, lyophilization and chemical modification. We observed that the 18 kDa-hsp is extremely resistant to a wide range of temperatures (60% of activity is retained at 80 degrees C for 20 min). N-Acylation increased its ordered structure by 4% and decreased its beta-T1 structure by 2%. ELISA demonstrated that the native conformation of the 18 kDa-hsp was preserved after hydrophobic modification by acylation. The recombinant 18 kDa-hsp resists to a wide range of temperatures and chemical modifications without loss of its main characteristic, which is to be a source of T epitopes. This resistance is probably directly related to its lack of organization at the level of tertiary and secondary structures.
Highlights
Modern vaccinology combines recombinant DNA technology and protein chemistry to obtain safe subunit vaccines
It is known that the heat shock proteins are involved in immunity [3] and in T cell stimulation [4]
We developed the large-scale production of 18 kDa-hsp at low cost in order to be able to introduce this T cell stimulation into our vaccines [7,8]
Summary
Modern vaccinology combines recombinant DNA technology and protein chemistry to obtain safe subunit vaccines. We developed the large-scale production of 18 kDa-hsp at low cost in order to be able to introduce this T cell stimulation into our vaccines [7,8]. Our main goal was to co-encapsulate the 18 kDa-hsp together with poor antigens within safe and pluripotent supports, such as liposomes [9,10] or biodegradable microspheres [11]. The liposomes containing the 18 kDa-hsp are prepared in a stable condition by lyophilization [10].
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