Our patented lichenase booster molecule, LickM, is a modified thermostable variant of the lichenase protein from the thermophilic bacterium Clostridium thermocellum. LicKM may be effective in addressing issues with subunit vaccines which, while having a track record in protecting humans against deadly diseases, may be insufficiently stable and require the use of a strong adjuvant to boost their immunogenicity.
Additionally, our patented LicKM protein fusions have been shown to be more soluble and expressed at higher levels than antigens alone.1 The protein itself may confer its thermostability onto fusion proteins, allowing for easy and cost-effective recovery of target proteins following heat treatment.2 With three available insertion sites (N-terminus, C-terminus, and internal loop), LicKM allows the integration of three antigens (or multiple copies of the same antigen) within a single stable fusion protein as well as identification of the optimal insertion location.3
