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    Online Resource
    The Internal Ribosome Entry Site of Dengue Virus mRNA Is Active When Cap-Dependent Translation Initiation Is Inhibited
    American Society for Microbiology ; 2021
    In:  Journal of Virology Vol. 95, No. 5 ( 2021-02-10)
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 95, No. 5 ( 2021-02-10)
    Abstract: Dengue virus (DENV) is an enveloped, positive-sense, single-stranded RNA virus belonging to the Flaviviridae family. Translation initiation of DENV mRNA can occur by a cap-dependent or a cap-independent mechanism. Two non-mutually exclusive cap-independent mechanisms of translation initiation have been described for DENV mRNA. The first corresponds to a 5′-end-dependent, internal ribosome entry site (IRES)-independent mechanism, while the second relies on IRES-dependent initiation. In this report, we study the recently discovered DENV IRES. The results show that the DENV IRES is functional in the rabbit reticulocyte lysate (RRL). In accordance, the activity of the DENV IRES was resistant to the cleavage of eukaryotic initiation factor 4G (eIF4G) by the Foot-and-mouth disease virus leader protease in RRL. In cells, the DENV IRES exhibited only marginal activity under standard culture conditions. The DENV IRES showed weak activity in HEK 293T cells; however, DENV IRES activity was significantly enhanced in HEK 293T cells expressing Human rhinovirus 2A protease. These findings suggest that the DENV IRES enables viral protein synthesis under conditions that suppress canonical translation initiation. IMPORTANCE Dengue virus (DENV), the etiological agent of dengue, a febrile and hemorrhagic disease, infects millions of people per year in tropical and subtropical countries. When infecting cells, DENV induces stress conditions known to inhibit canonical protein synthesis. Under these conditions, DENV mRNA thrives using noncanonical modes of translation initiation. In this study, we characterize the mechanism dependent on an internal ribosome entry site (IRES). Here, we describe the activity of the DENV IRES in vitro and cells. We show that in cells, the DENV IRES enables the viral mRNA to translate under conditions that suppress canonical translation initiation.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.01998-20
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2021
    detail.hit.zdb_id: 1495529-5
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  • 2
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    Post-translational modifications of hnRNP A1 differentially modulate retroviral IRES-mediated translation initiation
    Oxford University Press (OUP) ; 2020
    In:  Nucleic Acids Research Vol. 48, No. 18 ( 2020-10-09), p. 10479-10499
    Details
    In: Nucleic Acids Research, Oxford University Press (OUP), Vol. 48, No. 18 ( 2020-10-09), p. 10479-10499
    Abstract: The full-length mRNAs of the human immunodeficiency virus type-1 (HIV-1), the human T-cell lymphotropic virus type-1 (HTLV-1), and the mouse mammary tumor virus (MMTV) harbor IRESs. The activity of the retroviral-IRESs requires IRES-transacting factors (ITAFs), being hnRNP A1, a known ITAF for the HIV-1 IRES. In this study, we show that hnRNP A1 is also an ITAF for the HTLV-1 and MMTV IRESs. The MMTV IRES proved to be more responsive to hnRNP A1 than either the HTLV-1 or the HIV-1 IRESs. The impact of post-translational modifications of hnRNP A1 on HIV-1, HTLV-1 and MMTV IRES activity was also assessed. Results show that the HIV-1 and HTLV-1 IRESs were equally responsive to hnRNP A1 and its phosphorylation mutants S4A/S6A, S4D/S6D and S199A/D. However, the S4D/S6D mutant stimulated the activity from the MMTV-IRES to levels significantly higher than the wild type hnRNP A1. PRMT5-induced symmetrical di-methylation of arginine residues of hnRNP A1 enabled the ITAF to stimulate the HIV-1 and HTLV-1 IRESs while reducing the stimulatory ability of the ITAF over the MMTV IRES. We conclude that retroviral IRES activity is not only dependent on the recruited ITAFs but also relies on how these proteins are modified at the post-translational level.
    Type of Medium: Online Resource
    ISSN: 0305-1048 , 1362-4962
    URL: Article
    DOI: 10.1093/nar/gkaa765
    RVK:
    WA 15000
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2020
    detail.hit.zdb_id: 1472175-2
    SSG: 12
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