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Review
. 2013 Feb 20;436(2):255-67.
doi: 10.1016/j.virol.2012.11.017. Epub 2013 Jan 3.

Diversion of stress granules and P-bodies during viral infection

Lucas C Reineke  1 , Richard E Lloyd
Affiliations
Review

Diversion of stress granules and P-bodies during viral infection

Lucas C Reineke et al. Virology. .

Abstract

RNA granules are structures within cells that impart key regulatory measures on gene expression. Two general types of RNA granules are conserved from yeast to mammals: stress granules (SGs), which contain many translation initiation factors, and processing bodies (P-bodies, PBs), which are enriched for proteins involved in RNA turnover. Because of the inverse relationship between appearance of RNA granules and persistence of translation, many viruses must subvert RNA granule function for replicative purposes. Here we discuss the viruses and mechanisms that manipulate stress granules and P-bodies to promote synthesis of viral proteins. Several themes have emerged for manipulation of RNA granules by viruses: (1) disruption of RNA granules at the mid-phase of infection, (2) prevention of RNA granule assembly throughout infection and (3) co-opting of RNA granule proteins for new or parallel roles in viral reproduction. Viruses must employ one or multiple of these routes for a robust and productive infection to occur. The possible role for RNA granules in promoting innate immune responses poses an additional reason why viruses must counteract the effects of RNA granules for efficient replication.

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Figures

Fig. 1
Fig. 1
Stress granule assembly and interference by viruses. Virus infection causes stress at multiple levels that reduces host translation through activation of eIF2 kinases or other means and converts active polysome mRNPs into stalled translation initiation complex mRNPs. A complex series of events involving nucleation of several stress granule proteins such as G3BP1, Tia-1/TIAR, and HDAC6 plus transport on microtubules leads to aggregates of translation initiation complex mRNPs in stress granules. Specific points/proteins where viruses interact with and inhibit or divert the RNA granule assembly pathway are shown. Several viral proteins (VPs) interact with G3BP1 in complexes, some of which localize to novel viral foci. Note that many viruses control PKR activation; only those discussed in the text are indicated.
Fig. 2
Fig. 2
P-body assembly and interference by viruses. P-bodies form via a complex series of events involving stripping of mRNPs of initiation factors and ribosome subunits, association with GW182, undergoing Pan2/3-mediated deadenylation, MT transport, and association of other RNA decay factors (e.g., Xrn1, Dcp1a, DDX6, GW182 and Lsm components of the exosome), and final concentration in P-bodies. Decapping and decay occurs both in and outside P-bodies. The order of association of factors with mRNPs in PBs is arbitrary. For HCV, novel viral foci containing P-body components also contain some SG components including G3BP.
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