Translation initiation of the HIV-1 mRNA

Ohlmann, Théophile; Mengardi, Chloé; López-Lastra, Marcelo

doi:10.4161/2169074x.2014.960242

Cited by 17 publications

(14 citation statements)

References 167 publications

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“…Due to the apparent relevance in driving HIV‐1 Gag protein synthesis when cap‐dependent translation initiation is hindered , in this study, we focused on understanding the mechanism of translation driven by the IRES that is located within the 5′ UTR of the HIV‐1 full length mRNA (HIV IRES), . To date, the molecular basis of HIV‐1 IRES‐mediated translation initiation remains poorly understood (reviewed in ). The HIV‐1 IRES is active in HeLa and COS‐7 cells (Figs ), although, relative to other viral IRESs, its activity is low in HeLa cells (Fig.…”

Section: Discussionmentioning

confidence: 99%

Structural domains within the HIV‐1 mRNA and the ribosomal protein S25 influence cap‐independent translation initiation

et al. 2016

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The 5′leader of the HIV-1 genomic RNA is a multifunctional region that folds into secondary/tertiary structures that regulate multiple processes during viral replication including translation initiation. In this work we examine the internal ribosome entry site (IRES) located in the 5′leader that drives translation initiation of the viral Gag protein under conditions that hinder cap-dependent translation initiation. We show that activity of the HIV-1 IRES relies on ribosomal protein S25 (eS25). Additionally, a mechanistic and mutational analysis revealed that the HIV-1 IRES is modular in nature and that once the 40S ribosomal subunit is recruited to the IRES, translation initiates without the need of ribosome scanning. These findings elucidate a mechanism of initiation by the HIV-1 IRES whereby a number of highly structured sites present within the HIV-1 5′leader leads to the recruitment of the 40S subunit directly at the site of initiation of protein synthesis.

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Section: Discussionmentioning

confidence: 99%

Structural domains within the HIV‐1 mRNA and the ribosomal protein S25 influence cap‐independent translation initiation

et al. 2016

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“…Other IRESs are more challenging to classify. For example, the leader sequence of HIV-1 RNAs alone can stimulate translation in a cell-type-specific manner 83 , but different HIV-1 transcripts contain different IRES structures and splice site variations 84 , and the viral transcripts are capped. In HIV-1 and other retroviruses, the contributions of IRES-dependent and cap-dependent translation during infection remain the subject of debate 85 .…”

Section: Viral Internal Ribosome Entry Sitesmentioning

confidence: 99%

Viral RNA structure-based strategies to manipulate translation

2018

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Viruses are obligate cellular parasites that must co-opt the cellular translation machinery. Eukaryote-infecting viruses have evolved a variety of ways to manipulate the cellular translation apparatus, in many cases using elegant RNA-centered strategies. These viral RNAs can alter or control every phase of the protein-making process, are very diverse in terms of target, mechanism, and the RNA structural characteristics, and are found in a wide range of viruses. In addition, as cells often attempt to limit infection by inhibiting translation, some of these viral RNAs act to overcome the cell’s antiviral response or even take advantage of it to further viral infection. Here, we present important illustrative examples of viral RNA-based strategies to exploit the translation machinery. We briefly describe what is understood of the structure and mechanism of diverse RNA elements, the advantages conferred to the virus, and some of the key unknowns that provide motivation for further exploration.

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“…In this process, the 43S initiation complex is recruited at the internal ribosome entry site (IRES) containing mRNA stem loops to initiate the translation in a cap-independent manner. The HIV-1 virus, in the first 24-48 h of viral replication, uses cap-dependent translation process, whereas after 48 h, it opts for the IRES-dependent translation process to produce viral particles (Amorim et al, 2014;Ohlmann et al, 2014). For further understanding of the molecular mechanism of translation initiation, elongation, and completion, readers are encouraged to follow the articles by Ohlmann et al (2014) and Guerrero et al (2015).…”

Section: Cytoplasm: the Site Of Viral Protein Translation And Interacmentioning

confidence: 99%

From Entry to Egress: Strategic Exploitation of the Cellular Processes by HIV-1

et al. 2020

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HIV-1 employs a rich arsenal of viral factors throughout its life cycle and co-opts intracellular trafficking pathways. This exquisitely coordinated process requires precise manipulation of the host microenvironment, most often within defined subcellular compartments. The virus capitalizes on the host by modulating cell-surface proteins and cleverly exploiting nuclear import pathways for post entry events, among other key processes. Successful virus–cell interactions are indeed crucial in determining the extent of infection. By evolving defenses against host restriction factors, while simultaneously exploiting host dependency factors, the life cycle of HIV-1 presents a fascinating montage of an ongoing host–virus arms race. Herein, we provide an overview of how HIV-1 exploits native functions of the host cell and discuss recent findings that fundamentally change our understanding of the post-entry replication events.

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Translation initiation of the HIV-1 mRNA

Cited by 17 publications

References 167 publications

Structural domains within the HIV‐1 mRNA and the ribosomal protein S25 influence cap‐independent translation initiation

Structural domains within the HIV‐1 mRNA and the ribosomal protein S25 influence cap‐independent translation initiation

Viral RNA structure-based strategies to manipulate translation

From Entry to Egress: Strategic Exploitation of the Cellular Processes by HIV-1

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