Abstract:Lumazine synthase (LS) is widely distributed in animals, plants and microbes, and is one of the important synthesizing enzymes that catalyze the biosynthesis of riboflavin. One of the most remarkable characteristics of LS is that it has different spatial structures in different species. Brucella lumazine synthase (BLS), which has a stable structure of decamer consisting of two pentamers, is a dominant antigen of Brucella. BLS is a common antigen existing in both smooth type and rough type Brucella, and it can improve the sensitivity of diagnostic assays for Brucellosis; BLS is capable of stimulating antigen-specific cellular responses, resulting in production of IFN-γ, which consequently provides protection for the host. Therefore, BLS is an ideal candidate protein for development of subunit vaccine against Brucellosis. In this paper, the structural features of BLS protein and its application are reviewed, aiming at providing reference for in-depth studies and application of BLS.
