Cloning and expression of the phosphoprotein gene of Newcastle disease virus in Escherichia coli.
The phosphoprotein ( P) gene of a heat stable Newcastle disease virus (NDV) was cloned, sequenced and expressed in Escherichia coli. SDS-PAGE analysis of the recombinant P protein (395 amino acids) and a C-terminal extension derivative (424 amino acids), gave rise to two distinct protein bands with molecular masses of approximately 53-55 and 56-58 kDa, respectively, which are approximately 26-30% heavier than those calculated from the deduced amino acid sequences. The differences in molecular mass on SDS-PAGE are thought to be attributed to the acidic nature of the P protein (pI=6.27) and also the different degrees of phosphorylation in the prokaryotic cell. Amino acid sequence comparison of the P protein among the published NDV strains showed that they were highly conserved particularly at the putative phosphorylation sites.[1]References
- Cloning and expression of the phosphoprotein gene of Newcastle disease virus in Escherichia coli. Kho, C.L., Tan, W.S., Yusoff, K. J. Biochem. Mol. Biol. Biophys. (2002) [Pubmed]
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