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  • The P body protein LSm1 contributes to stimulation of hepatitis C virus translation, but not replication, by microRNA-122.

The P body protein LSm1 contributes to stimulation of hepatitis C virus translation, but not replication, by microRNA-122.

Nucleic acids research (2013-10-22)
Ashley P E Roberts, Rachel Doidge, Alexander W Tarr, Catherine L Jopling
ABSTRACT

The P body protein LSm1 stimulates translation and replication of hepatitis C virus (HCV). As the liver-specific microRNA-122 (miR-122) is required for HCV replication and is associated with P bodies, we investigated whether regulation of HCV by LSm1 involves miR-122. Here, we demonstrate that LSm1 contributes to activation of HCV internal ribosome entry site (IRES)-driven translation by miR-122. This role for LSm1 is specialized for miR-122 translation activation, as LSm1 depletion does not affect the repressive function of miR-122 at 3' untranslated region (UTR) sites, or miR-122-mediated cleavage at a perfectly complementary site. We find that LSm1 does not influence recruitment of the microRNA (miRNA)-induced silencing complex to the HCV 5'UTR, implying that it regulates miR-122 function subsequent to target binding. In contrast to the interplay between miR-122 and LSm1 in translation, we find that LSm1 is not required for miR-122 to stimulate HCV replication, suggesting that miR-122 regulation of HCV translation and replication have different requirements. For the first time, we have identified a protein factor that specifically contributes to activation of HCV IRES-driven translation by miR-122, but not to other activities of the miRNA. Our results enhance understanding of the mechanisms by which miR-122 and LSm1 regulate HCV.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-LSM1 antibody produced in chicken, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Monoclonal Anti-AGO2 antibody produced in rat, ~1.5 mg/mL, clone 11A9, purified immunoglobulin