scholarly journals Translation elongation after assembly of ribosomes on the Cricket paralysis virus internal ribosomal entry site without initiation factors or initiator tRNA

2003 ◽  
Vol 17 (2) ◽  
pp. 181-186 ◽  
Author(s):  
T. V. Pestova
Keyword(s):  
Internal Ribosomal Entry Site ◽  
Entry Site ◽  
Translation Elongation ◽  
Initiator Trna ◽  
Initiation Factors ◽  
Ribosomal Entry ◽  
Paralysis Virus

scholarly journals Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry.

1996 ◽  
Vol 16 (12) ◽  
pp. 6859-6869 ◽  
Author(s):  
T V Pestova ◽  
C U Hellen ◽  
I N Shatsky
Keyword(s):  
Internal Ribosomal Entry Site ◽  
Encephalomyocarditis Virus ◽  
Initiation Factor ◽  
Entry Site ◽  
Independent Manner ◽  
Initiation Factors ◽  
Virus Rna ◽  
Initiation Of Translation ◽  
Initiation Factor 2 ◽  
Ribosomal Entry

Translation of picornavirus RNA is initiated after ribosomal binding to an internal ribosomal entry site (IRES) within the 5' untranslated region. We have reconstituted IRES-mediated initiation on encephalomyocarditis virus RNA from purified components and used primer extension analysis to confirm the fidelity of 48S preinitiation complex formation. Eukaryotic initiation factor 2 (eIF2), eIF3, and eIF4F were required for initiation; eIF4B and to a lesser extent the pyrimidine tract-binding protein stimulated this process. We show that eIF4F binds to the IRES in a novel cap-independent manner and suggest that cap- and IRES-dependent initiation mechanisms utilize different modes of interaction with this factor to promote ribosomal attachment to mRNA.

scholarly journals CRISPR-Cas13a mediated targeting of hepatitis C virus internal-ribosomal entry site (IRES) as an effective antiviral strategy

2021 ◽  
Vol 136 ◽  
pp. 111239
Author(s):  
Muhammad Usman Ashraf ◽  
Hafiz Muhammad Salman ◽  
Muhammad Farhan Khalid ◽  
Muhammad Haider Farooq Khan ◽  
Saima Anwar ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Internal Ribosomal Entry Site ◽  
Entry Site ◽  
Ribosomal Entry

scholarly journals Riboproteomics of the Hepatitis C Virus Internal Ribosomal Entry Site

2004 ◽  
Vol 3 (5) ◽  
pp. 949-957 ◽  
Author(s):  
Henry Lu ◽  
Weiqun Li ◽  
William Stafford Noble ◽  
Donald Payan ◽  
D. C. Anderson
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Internal Ribosomal Entry Site ◽  
Entry Site ◽  
Ribosomal Entry

scholarly journals An internal ribosomal entry site mediates redox-sensitive translation of Nrf2

2009 ◽  
Vol 38 (3) ◽  
pp. 778-788 ◽  
Author(s):  
Wenge Li ◽  
Nehal Thakor ◽  
Eugenia Y. Xu ◽  
Ying Huang ◽  
Chi Chen ◽  
...  
Keyword(s):  
Internal Ribosomal Entry Site ◽  
Entry Site ◽  
Ribosomal Entry

scholarly journals Heat Shock Protein A6, a Novel HSP70, Is Induced During Enterovirus A71 Infection to Facilitate Internal Ribosomal Entry Site-Mediated Translation

2021 ◽  
Vol 12 ◽  
Author(s):  
Yu-Siang Su ◽  
Lih-Hwa Hwang ◽  
Chi-Ju Chen
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Neurological Diseases ◽  
Internal Ribosomal Entry Site ◽  
Viral Proteins ◽  
Cellular Protein ◽  
Encephalomyocarditis Virus ◽  
Entry Site ◽  
Enterovirus A71 ◽  
Ribosomal Entry

Enterovirus A71 (EV-A71) is a human pathogen causing hand, foot, and mouth disease (HFMD) in children. Its infection can lead to severe neurological diseases or even death in some cases. While being produced in a large quantity during infection, viral proteins often require the assistance from cellular chaperones for proper folding. In this study, we found that heat shock protein A6 (HSPA6), whose function in viral life cycle is scarcely studied, was induced and functioned as a positive regulator for EV-A71 infection. Depletion of HSPA6 led to the reductions of EV-A71 viral proteins, viral RNA and virions as a result of the downregulation of internal ribosomal entry site (IRES)-mediated translation. Unlike other HSP70 isoforms such as HSPA1, HSPA8, and HSPA9, which regulate all phases of the EV-A71 life, HSPA6 was required for the IRES-mediated translation only. Unexpectedly, the importance of HSPA6 in the IRES activity could be observed in the absence of viral proteins, suggesting that HSPA6 facilitated IRES activity through cellular factor(s) instead of viral proteins. Intriguingly, the knockdown of HSPA6 also caused the reduction of luciferase activity driven by the IRES from coxsackievirus A16, echovirus 9, encephalomyocarditis virus, or hepatitis C virus, supporting that HSPA6 may assist the function of a cellular protein generally required for viral IRES activities.

scholarly journals The non-primate hepacivirus 5′ untranslated region possesses internal ribosomal entry site activity

2013 ◽  
Vol 94 (12) ◽  
pp. 2657-2663 ◽  
Author(s):  
Hazel Stewart ◽  
Cheryl Walter ◽  
Dale Jones ◽  
Sinead Lyons ◽  
Peter Simmonds ◽  
...  
Keyword(s):  
Untranslated Region ◽  
Internal Ribosomal Entry Site ◽  
Rna Replication ◽  
Entry Site ◽  
Subgenomic Replicon ◽  
Stem Loop ◽  
Long Range Interactions ◽  
Ribosomal Entry ◽  
Internal Translation ◽  
And Function

The 5′ untranslated region (5′UTR) of the recently described non-primate hepacivirus (NPHV) contains a region with sequence homology to the internal ribosomal entry site (IRES) of hepatitis C virus (HCV) and GB virus B (GBV-B). Here, we demonstrated internal translation initiation by the NPHV 5′UTR in a bicistronic vector. An RNA stem–loop upstream of the NPHV IRES was structurally distinct from corresponding regions in HCV and GBV-B, and was not required for IRES function. Insertion of the NPHV stem–loop into the corresponding region of the HCV 5′UTR within the HCV subgenomic replicon significantly impaired RNA replication, indicating that long-range interactions between the 5′UTR and cis-acting downstream elements within the NPHV genome are not interchangeable with those of HCV. Despite similarities in IRES structure and function between hepaciviruses, replication elements in the NPHV 5′UTR appear functionally distinct from those of HCV.

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