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A new insight into the species barrier of Mammalian Prions obtained from structure-based conservation analysis
Yaofeng Wang 1,Bingjie Hu 2,Yuan Liu 2,Huili Zhang 2,Youtao Song 2 * #
1.Department of Cell and Molecular Biology, Uppsala University
2.Life Science College, Liaoning University
*Correspondence author
#Submitted by
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Funding: 国家自然基金,辽宁省教育厅(No.30600113,05L156)
Opened online:17 December 2007
Accepted by: none
Citation: Yaofeng Wang,Bingjie Hu,Yuan Liu.A new insight into the species barrier of Mammalian Prions obtained from structure-based conservation analysis[OL]. [17 December 2007] http://en.paper.edu.cn/en_releasepaper/content/17036
 
 
In the previous study done by Scott, M.R. et al, residues 184, 203 and 205 were predicted to contribute to an epitope modulating prion transmission, however, the evolutionary features of these residues were still unknown. To explore that, the functional domains (121-231) of 8 mammalian prions were examined by an informative and sensitive structural conservation analysis in this study. The results identified the three residues as highly structure-conserved but sequence-nonconserved. This suggested us the residues with these features may play an important role in modulating the transmission of prion diseases. Based on our hypothesis, residue 215 with the same structure feature was also predicted to involve in prion transmission. Subsequently, a phylogenetic tree was reconstructed. The topology of the tree can explain the mystery of species barrier occurred between the mammalian prions which cannot be deduced by simply sequence phylogenetic tree.
Keywords:Mammalian prions; Structural conservation analysis; Phylogenetic trees; Species barrier.
 
 
 

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