Abstract：In order to analyze the advanced structure of prion protein in Lohmann Brown laying hen,the species barriers in prion diseases and the mechanism of conformational transition,specific primers were designed based on the gene sequence of chicken prion protein in GenBank,and the ORFs of prion protein genes from eight Lohmann Brown laying hens were amplified.Results of sequence analysis showed that there were two base-pair substitutions(243C→T,296A→G)in ORFs,and synonymous mutation was on the site of 243.The genetic evolution information of Lohmann Brown laying hens and other 68 species was obtained based on the amino acid sequence of prion protein gene by bioinformatics analysis,and the three-dimensional structure modeling of prion protein from Lohmann Brown laying hens and human were predicted by homology modeling.It's suggested that conformation homology of different species would decide the species barrier mechanism of prion diseases in a great degree.Moreover,the transformation from normal type prion protein to pathotype one would be affected by many factors.
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