The research group lead by Prof. LIN Donghai in Shanghai Institute of Materia Medica,CAS has been studying on the solution structure and dynamics of the rabbit prion protein using multi-dimensional heteronuclear NMR techniques, and their latest findings has been published in the famous journal PLoS ONE (2010 Oct 7, 5: e13273;http://www.ncbi.nlm.nih.gov/pubmed/20949107).

Rabbits appear to be resistant to the infection of transmissible spongiform encephalopathies (TSEs). LIN and his colleagues had reported the unique structural characteristics of the rabbit prion protein and the structural changes caused by the S173N substitution in a previous work (J. Biol. Chem., 2010 Oct 8, 285: 31682;http://www.ncbi.nlm.nih.gov/pubmed/20639199). Now the group has further investigated the differences between the wild-type protein and the I214V mutant, suggesting that the surface charge distribution and the intrinsic backbone flexibility greatly contribute to the inability of the conformational conversion for rabbit prion protein. These findings provide valuable clues for better understanding the species barriers of TSEs.

LIN’s research has received grants from the National Natural Science Foundation of China (Nos. 30730026, 30570352) andNational Programs for Science and Technology Development“Key New Drug Creation and Manufacturing Program” (No. 2009ZX09301-001).