7 infected cells compared to DMSO control. This effect may be due to antagonistic activity of the W-7 against the Ca2+-CaM complex which is required for efficient viral replication & assembly. Discussion The studies of the rotaviruses are mostly confined to either analysis of specific function of RV encoded proteins or epidemiology, or vaccine development. The RV induced alteration of host 
cell proteome was not studied extensively, until recently when Zambrano et. al. reported RV induced changes of cellular proteome in the context of IFN response. The results led to the identification of proteins related to the cell stress mediated by RV OSU strain in presence or in absence of IFN treatment. GRP78 and GRP 94 protein which were upregulated during RRV infection 11741928 were surprisingly found to be downregulated in OSU infected cells reflecting differences among various RV strains. This was consistent with previous observations that degradation of IRF3 by RV varies among different strains and cell lines. In the current study, an attempt has been made to identify host cellular proteins with altered expression level at early and late phase of RV infection using SA11 strain. 2D-DIGE analysis followed by mass spectrometry led to the identification of 11 Rotavirus Infection Induce Change in Host Proteome 22 unique proteins that had differential protein expression. Among the 22 unique proteins identified by MALDI-TOF/TOF MS, expression of 9 genes was validated by western blotting and 3 were validated by Real-time PCR. These were further confirmed using in vivo animal model. Though ligated intestinal loops in colostrumdeprived calves have been used previously to evaluate the effect of four isolates of bovine rotavirus, it has not been tested in other experimental animals like rabbit, mice etc.. An intestinal ligated loop model for RV infection in BALB/c mouse was established here as reported previously for Vibrio cholerae and Staphylococcus aureus. Accumulation of fluid and upregulation of NSP4 transcript in ligated loop of RV infected mice confirmed virus infection in BALB/c model. Expression of ANP32A, CaM and inorganic pyrophosphatase proteins in vivo were comparable Rotavirus Infection Induce Change in Host Proteome molecule due to its structural flexibility and highly adaptable nature of the binding surface. CaM contains four EFhand motifs which can bind four Ca2+ ions, resulting in huge structural shift of CaM from the unbounded state which enables binding of large number of proteins collectively termed CaM Binding Proteins. Ca2+/CaM have various downstream targets like serine/threonine phosphatase, calcineurin, multifunctional 23964788 Ca2+/CaM -dependent protein kinases, adenyl Tedizolid (phosphate) chemical information cyclases, ion channels, phosphodiesterases, myosin light chain kinases and protein phosphatases. Ca2+/CaM is also known to significantly enhance PI3-Kinase activity in vitro. Increased CaM causes differences in the organization of microfilaments, intermediate filaments, & microtubules; these changes are accompanied by differences in the cell-cycle dependent expression of some mRNAs. For efficient viral replication, viruses such as EBV, HIV-1 induce cell cycle transition from G1 to S phase. So it is possible that during early RV infection cell cycle progresses from G1 to S phase. Previous studies have shown that translation machinery and other cellular system are highly active during S phase which may benefit viruses as they can efficiently synthesize their proteins using host cell
