Cloning of the phosphoprotein gene of peste des petits ruminants and analysis of its structure and function.

【Objective】 The objective of the present study was to clone the gene of PPRV phosphoprotein and analyze the structure-function relationship of phosphoprotein.【Method】 The phosphoprotein entire gene of PPRV was cloned by RT-PCR,in addition,the nucleotide and a mino acid sequences were analyzed and compared with other members of Morbillivirus through bioinformatics methods,and the protein tertiary structure was predicted using I-TASSER.【Result】 Sequence analysis showed that the homologies of nucleotide sequences between PPRV and MV,CDV,RPV,DMV and PDV were 62.9%,63.3%,64.4%,65.1%,and 60.4%,respectively,and the homologies of the deduced amino acid sequences were 45.9%,46.2%,50.6%,50.3%,and 47.0%,respectively.The tertiary structure and analysis indicated that the phosphoprotein was composed of three distinct structural domains:an N-terminal hydrophilic domain,a central domain,and a C-terminal hydrophilic domain.In addition,the central hydrophobic domain of phosphoprotein had lots of alpha helix with the potential to bind both of the large protein and RNA.The C-terminal hydrophilic domain was composed of three alpha helix,and they lay in 458-468aa,492-499aa and 503-505aa,respectively,and might play a role in their binding of alpha helix of the nucleoprotein.【Conclusion】 The phosphoprotein gene from PPRV was successfully cloned.Furthermore,the structure and function of this gene were analyzed and predicted.