Key result
Phosphorylation of Tyr611 and Thr674 of the IBDV-encoded VP4 protein affects its serine-protease activity and partially contributes to the cleavage of the intermediate precursor VP4-VP3 polyprotein.
IBDV-encoded VP4 protein is a phosphoprotein, and phosphorylation of Tyr611 and Thr674 affects its serine-protease activity.
Birnavirus-encoded viral protein 4 (VP4) utilizes a Ser/Lys catalytic dyad mechanism to process polyprotein. Here three phosphorylated amino acid residues Ser538, Tyr611 and Thr674 within the VP4 protein of the infectious bursal disease virus (IBDV), a member of the genus Avibirnavirus of the family Birnaviridae, were identified by mass spectrometry. Anti-VP4 monoclonal antibodies finely mapping to phosphorylated (p)Ser538 and the epitope motif 530PVVDGIL536 were generated and verified. Proteomic analysis showed that in IBDV-infected cells the VP4 was distributed mainly in the cytoskeletal fraction and existed with different isoelectric points and several phosphorylation modifications. Phosphorylation of VP4 did not influence the aggregation of VP4 molecules. The proteolytic activity analysis verified that the pTyr611 and pThr674 sites within VP4 are involved in the cleavage of viral intermediate precursor VP4-VP3. This study demonstrates that IBDV-encoded VP4 protein is a unique phosphoprotein and that phosphorylation of Tyr611 and Thr674 of VP4 affects its serine-protease activity.
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Wang et al. (2015) studied Infectious bursal disease virus (IBDV) infection. VP4 protein phosphorylation site mutations (Ser538, Tyr611, Thr674) vs. Wild-type VP4 was evaluated on Proteolytic cleavage of intermediate precursor VP4-VP3. Phosphorylation of Tyr611 and Thr674 of the IBDV-encoded VP4 protein affects its serine-protease activity and partially contributes to the cleavage of the intermediate precursor VP4-VP3 polyprotein.
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