Abstract:

【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.

Key words: PPRV, phosphoprotein, cloning, structure and function, analysis