Gao Hongwei

Mapping the interaction site of prion protein and Sho

The cellular prion protein (PrPC) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrPC remains unclear. Sho (Shadoo, shadow of prion protein) and PrPC have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61–77 and PrPC 108–126 domains. This indicates that Sho may play a role in the physiological function of PrPC and prion pathogenesis.

Properties of a Novel α-galactosidase from B.Fragilis and Its Potential for Human Blood-type B to O Conversion

Enzymatic removal of blood group B antigen is an effective method to develop universal red blood cells (RBCs) by α-galactosidase. Here we investigated the physicochemical properties of a novel α-galactosidase from B. Fragilis and the optimization of enzymatic conversion for RBC of blood group B to O. The results showed that α-galactosidase exhibited maximum activity at a broad optimal pH of 5.6-6.0 and an optimum temperature of 41°C. Furthermore, the enzyme was efficient in complete removal of B antigen. The conditions for B to O blood group conversion were 26°C, pH 6.8 (250 mmol/L glycine and 3 mmol/L NaCl) for 1 h. The structure and function indexes of the converted red blood cells showed no significant difference from those of normal RBCs. Consequently, the novel α-galactosidase described here was more suitable for enzymatic conversion for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions.