Nearly Scale-Invariant Spectrum of Adiabatic Fluctuations May be from a Very Slowly Expanding Phase of the Universe

In this paper we construct an expanding phase with phantom matter, in which the scale factor expands very slowly but the Hubble parameter increases gradually, and assume that this expanding phase could be matched to our late observational cosmology by the proper mechanism. We obtain the nearly scale-invariant spectrum of adiabatic fluctuations in this scenario, different from the simplest inflation and usual ekpyrotic/cyclic scenario, the tilt of nearly scale-invariant spectrum in this scenario is blue. Although there exists an uncertainty surrounding the way in which the perturbations propagate through the transition in our scenario, which is dependent on the detail of possible "bounce" physics, compared with inflation and ekpyrotic/cyclic scenario, our work may provide another feasible cosmological scenario generating the nearly scale-invariant perturbation spectrum.Comment: 4 pages, no figures, to appear in Phys. Rev. D. Many thanks for referee's kind comments and criticism

Hepatitis C virus 3'UTR regulates viral translation through direct interactions with the host translation machinery.

The 3' untranslated region (3'UTR) of hepatitis C virus (HCV) messenger RNA stimulates viral translation by an undetermined mechanism. We identified a high affinity interaction, conserved among different HCV genotypes, between the HCV 3'UTR and the host ribosome. The 3'UTR interacts with 40S ribosomal subunit proteins residing primarily in a localized region on the 40S solvent-accessible surface near the messenger RNA entry and exit sites. This region partially overlaps with the site where the HCV internal ribosome entry site was found to bind, with the internal ribosome entry site-40S subunit interaction being dominant. Despite its ability to bind to 40S subunits independently, the HCV 3'UTR only stimulates translation in cis, without affecting the first round translation rate. These observations support a model in which the HCV 3'UTR retains ribosome complexes during translation termination to facilitate efficient initiation of subsequent rounds of translation