Abstract
A hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.
Highlights
Group/species A rotaviruses (RVAs) belong to the Reoviridae family and are one of the major causes of gastroenteritis in infants and young children (Anonymous 2008)
Recombinant non-structural protein 1 (NSP1) expressed in a vaccinia system localises to the cytoplasm with a diffuse and granular appearance - To determine the intracellular distribution of NSP1 in the absence of other viral proteins and/or viral RNAs, we infected the vervet monkey kidney cell line BSC-1 with the recombinant vaccinia virus vNSP1, which had previously been developed to express rhesus rotavirus (RRV) NSP1 (Pina-Vazquez et al 2007)
Because a detailed study of NSP1 expression throughout the infection process was lacking, our first aim was to determine the intracellular distribution of NSP1 in MA-104 cells infected with RRV
Summary
Group/species A rotaviruses (RVAs) belong to the Reoviridae family and are one of the major causes of gastroenteritis in infants and young children (Anonymous 2008). NSP1 is a 53-kDa RNA-binding protein that localises to the cytoplasm of infected cells (Hua & Patton 1994, Hua et al 1994). It is the most variable viral protein, NSP1 contains a conserved set of seven cysteines and one histidine near the N-terminus (residues 44-74 of RRV gene 5), which has been proposed to be a really interesting new gene (RING) domain, which is characteristic of E3 ubiquitin-protein ligases (Graff et al 2007, Pina-Vazquez et al 2007).
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