Quantitative phosphoproteome on the silkworm (Bombyx mori) cells infected with baculovirus

Abstract

Background Bombyx mori has become an important model organism for many fundamental studies. Bombyx mori nucleopolyhedrovirus (BmNPV) is a significant pathogen to Bombyx mori, yet also an efficient vector for recombinant protein production. A previous study indicated that acetylation plays many vital roles in several cellular processes of Bombyx mori while global phosphorylation pattern upon BmNPV infection remains elusive.MethodEmploying tandem mass tag (TMT) labeling and phosphorylation affinity enrichment followed by high-resolution LC-MS/MS analysis and intensive bioinformatics analysis, the quantitative phosphoproteome in Bombyx mori cells infected by BmNPV at 24 hpi with an MOI of 10 was extensively examined.ResultsTotally, 6480 phosphorylation sites in 2112 protein groups were identified, among which 4764 sites in 1717 proteins were quantified. Among the quantified proteins, 81 up-regulated and 25 down-regulated sites were identified with significant criteria (the quantitative ratio above 1.3 was considered as up-regulation and below 0.77 was considered as down-regulation) and with significant p-value (p < 0.05). Some proteins of BmNPV were also hyperphosphorylated during infection, such as P6.9, 39 K, LEF-6, Ac58-like protein, Ac82-like protein and BRO-D.ConclusionThe phosphorylated proteins were primary involved in several specific functions, out of which, we focused on the binding activity, protein synthesis, viral replication and apoptosis through kinase activity.

Insights into the Temporal Gene Expression Pattern in Lymantria dispar Larvae During the Baculovirus Induced Hyperactive Stage

“…5B-5D). A similar GO enrichment pattern of differentially expressed host genes upon BmNPV infection in host cells (Shobahah et al 2017) as well as in Zika virus infected Aedes aegypti (Etebari et al 2017) had been reported. Maximum distribution of DEGs in the molecular functions category associated with binding activity had also been reported by Wang et al (2015) on the transcriptome of the brain of B. mori larvae infected with BmNPV, where its significance on mediating neuroactive steroids to activate membrane receptors had been discussed.…”

Comparative phosphoproteome analysis to identify candidate phosphoproteins involved in blue light-induced brown film formation in Lentinula edodes

“…To analyze the density levels of the phosphorylation sites in each protein, the phosphorylated proteome of L. edodes was compared with those of other species. The average number of phosphorylation sites per protein in L. edodes is 3.22, which is similar to the numbers in Bombyx mori (3.07), Nicotiana tabacum (3.05), and Physcomitrella patens (3.44) ( Fig.2b) [34][35][36].…”

The phosphoproteomic responses of duck (Cairna moschata) to classical/novel duck reovirus infections in the spleen tissue

“…Protein phosphorylation is a universal PTM; however, the abundance of phosphorylation largely varies among different species. In C. moschata, the abundance of phosphorylated protein (2,853 phosphorylated proteins) was higher than most of the published species, such as Sus domesticus (966 phosphorylated proteins), Bombyx mori (2,112 phosphorylated proteins), Kandelia candel (1,516 phosphorylated proteins), Nicotiana tabacum (1,311 phosphorylated proteins), Lotus japonicus (1,154 phosphorylated proteins), Ammopiptanthus mongolicus (2,019 phosphorylated proteins), Catalpa fargesii (1,646 phosphorylated proteins), Abelmoschus esculentus (2,550 phosphorylated proteins), and Physcomitrella patens (1,873 phosphorylated proteins) 35,43,45,[50][51][52][53] . High-throughput method gives us an opportunity to screen potential phosphorylated proteins and reveal the involvement of protein phosphorylation in the responses to the C/NDRV infections.…”