The effect of infectious bursal disease virus (IBDV)
infection on cellular
protein expression is essential for viral pathogenesis. To characterize the cellular response to IBDV
infection, the differential
proteomes of chicken embryo fibroblasts, with and without IBDV
infection, were analyzed at different time points with two-dimensional gel electrophoresis (2-DE) followed by MALDI-TOF/TOF identification. Comparative analysis of multiple 2-DE
gels revealed that the majority of
protein expression changes appeared at 48 and 96 h after IBDV
infection. Mass spectrometry identified 51 altered cellular
proteins, including 13 up-regulated
proteins and 38 down-regulated
proteins 12-96 h after
infection. Notably 2-DE analysis revealed that IBDV
infection induced the increased expression of
polyubiquitin,
apolipoprotein A-I, heat shock 27-kDa
protein 1,
actins, tubulins, eukaryotic translation
initiation factor 4A
isoform 2, acidic ribosomal
phosphoprotein, and
ribosomal protein SA
isoform 2. In addition, IBDV
infection considerably suppressed those cellular
proteins involved in
ubiquitin-mediated protein degradation, energy metabolism, intermediate filaments, host translational apparatus, and signal transduction. Moreover 38 corresponding genes of the differentially expressed
proteins were quantitated by real time RT-PCR to examine the transcriptional profiles between infected and uninfected chicken embryo fibroblasts. Western blot further confirmed the inhibition of Rho
protein GDP dissociation inhibitor expression and the induction of
polyubiquitin during IBDV
infection. Subcellular distribution analysis of the
cytoskeletal proteins vimentin and
beta-tubulin clearly demonstrated that IBDV
infection induced the disruption of the
vimentin network and microtubules late in IBDV
infection. Thus, this work effectively provides useful dynamic
protein-related information to facilitate further investigation of the underlying mechanism of IBDV
infection and pathogenesis.