Literature DB >> 31802690

Phosphorylation of nucleopolyhedrovirus 39K is essential for the regulation of viral gene transcription in silkworm cells.

H Yan, J Shobahah, M Wei, E Obeng, S Xue, D Hu, Y Quan, W Yu.   

Abstract

39K protein was proven to be the most notable hyperphosphorylated protein of Bombyx mori nucleopolyhedrovirus (BmNPV), since its amino acid 136 has the highest phosphorylation ratio (16.683) among all of BmNPV phosphorylated proteins (Shobahah et al., 2017). Therefore, we inserted positive (mimicking phosphorylation) and negative (mimicking dephosphorylation) mutants of the highest phosphorylated site of 39K and the wild type 39k into the 39k-ko-Bacmid using the Bac-to-Bac system. These three kinds of recombinant Bacmids along with wild type and knocked-out Bacmid were then transfected into the Bombyx mori cells (BmN) and further investigated by qPCR analysis. The results of the qPCR showed that 39K phosphorylation had no significant effect on viral genome replication, unlike the positive mutation that reduced the viral gene transcription drastically compared to the wild type. Thus, phosphorylation of BmNPV 39K protein does not appear to be the essential mechanism for viral genome replication, even though it has an important role in the viral gene transcription. Keywords: BmNPV; 39K; phosphorylation; virus replication; virus transcription.

Entities:  

Year:  2019        PMID: 31802690     DOI: 10.4149/av_2019_414

Source DB:  PubMed          Journal:  Acta Virol        ISSN: 0001-723X            Impact factor:   1.162


  1 in total

1.  Systematic analysis and comparison of O-glycosylation of five recombinant spike proteins in β-coronaviruses.

Authors:  Xuefang Dong; Xiuling Li; Cheng Chen; Xiaofei Zhang; Xinmiao Liang
Journal:  Anal Chim Acta       Date:  2022-09-16       Impact factor: 6.911

  1 in total

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