RNA-Binding Proteins as Regulators of Internal Initiation of Viral mRNA Translation

López-Ulloa, Brenda; Fuentes, Yazmín; Pizarro-Ortega, Magdalena S.; López‐Lastra, Marcelo

doi:10.3390/v14020188

Cited by 13 publications

(14 citation statements)

References 441 publications

(946 reference statements)

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“…These strategies are in part facilitated by the delocalization of RBPs to the cytoplasm in infected cells, an event that increases the pool of functionally active factors for viral RNA translation. Soon after the discovery of picornavirus IRES elements in 1988 [5,6], it was found that full IRES activity required the action of host factors, as exemplified by the polypyrimidine tract‐binding protein (PTB), poly(rC)‐binding protein 2 (PCBP2), ErbB3‐binding protein 1 (Ebp1, also known as ITAF 45 and PA2G4), or the cold‐shock domain containing E1 (CSDE1, also known as Unr), among others [50–54], reviewed in [38,55].…”

Section: Host Factors Involved In Picornavirus Rna Translationmentioning

confidence: 99%

“…Hence, the first phase of the picornavirus infection cycle requires the translation of the viral RNA, which is governed by the IRES element. This property is shared with other RNA viruses, such as hepatitis C (HCV), a member of the Flaviviridae family, as well as members of the families Dicistroviridae (CrPV) and Retroviridae (HIV-1), reinforcing the fact that the use of IRES elements represents an optimized strategy for achieving successful viral infection [37,38]. A key feature of viral IRES elements is that they are active outside of its natural RNA background, promoting cap-independent activity in different genetic contexts.…”

Section: Picornavirus Translation Strategies For Evading Shutdown Of ...mentioning

confidence: 99%

“…In addition to eIFs, various ITAFs are targets of picornavirus proteases, such that the resulting cleavage products perform functions different from the uncleaved protein [42]. In other cases, posttranslational modification of the proteins or changes in the associated factors in response to stress play a role in modulating IRES activity, either directly or indirectly [38,43].…”

Section: Picornavirus Translation Strategies For Evading Shutdown Of ...mentioning

confidence: 99%

“…protein 2 (PCBP2), ErbB3-binding protein 1 (Ebp1, also known as ITAF 45 and PA2G4), or the cold-shock domain containing E1 (CSDE1, also known as Unr), among others [50][51][52][53][54], reviewed in [38,55].…”

Section: Host Factors Involved In Picornavirus Rna Translationmentioning

confidence: 99%

“…A large diversity of RBPs involved in nuclear and cytoplasmic RNA-dependent processes have been identified associated with viral IRES elements, as exemplified by Ebp1, the far upstream element-binding protein 1 (FBP1) and FBP2, the heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1), G3BP1, and Unr (reviewed in [38,55]). However, the number of host factors identified to be involved in viral RNA translation is constantly growing due to the development of new approaches for studying the function of traditional and non-conventional RNA binding proteins in infected cells [128,129].…”

Section: Mechanistic Attributes Of Picornavirus Ires Elements Modulat...mentioning

confidence: 99%

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Picornavirus translation strategies

et al. 2022

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The genome of viruses classified as picornaviruses consists of a single monocistronic positive strand RNA. The coding capacity of these RNA viruses is rather limited, and thus, they rely on the cellular machinery for their viral replication cycle. Upon the entry of the virus into susceptible cells, the viral RNA initially competes with cellular mRNAs for access to the protein synthesis machinery. Not surprisingly, picornaviruses have evolved specialized strategies that successfully allow the expression of viral gene products, which we outline in this review. The main feature of all picornavirus genomes is the presence of a heavily structured RNA element on the 5´UTR, referred to as an internal ribosome entry site (IRES) element, which directs viral protein synthesis as well and, consequently, triggers the subsequent steps required for viral replication. Here, we will summarize recent studies showing that picornavirus IRES elements consist of a modular structure, providing sites of interaction for ribosome subunits, eIFs, and a selective group of RNA‐binding proteins.

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Section: Host Factors Involved In Picornavirus Rna Translationmentioning

confidence: 99%

Section: Picornavirus Translation Strategies For Evading Shutdown Of ...mentioning

confidence: 99%

Section: Picornavirus Translation Strategies For Evading Shutdown Of ...mentioning

confidence: 99%

Section: Host Factors Involved In Picornavirus Rna Translationmentioning

confidence: 99%

Section: Mechanistic Attributes Of Picornavirus Ires Elements Modulat...mentioning

confidence: 99%

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Picornavirus translation strategies

et al. 2022

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Host–virus relationships: a sum of many battles

López‐Lastra

2022

FEBS Open Bio

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The spread of pathogenic viruses implies host infection, replication, and virus dissemination. In each step, viruses have to overcome the host defenses designed to neutralize the threat they pose. The host–virus relationship represents a constant multistage battle for power as the host/cell does not voluntarily give in to the viral enemy. Upon infection, cells recognize viral pathogen‐associated molecular patterns, activating the innate antiviral defenses. As such, during most of the replication cycle, the virus has to deal with the cellular antiviral response. At this point, it should not be forgotten that viruses are obligate intracellular parasites and thus are entirely dependent on the host cell for their replication. This dependency has pushed viruses to evolve unorthodox strategies to subvert and repurpose cellular factors and processes required for efficient replication. Even if a virus has the potential to be successful at each step necessary for its spread, this does not mean it has won the war against the host. Another threat to viruses is represented by antiviral drugs designed to diminish their survival and promote the host's wellbeing. This editorial outlines the contents of this special ‘In the Limelight’ issue of FEBS Open Bio focused on Virology. The section contains four review articles, each focused on a particular aspect of virus–host interaction, including the antiviral response, subversion of the host translational machinery, repurposing of cellular factors, and the development of antiviral drugs.

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Expansion Segment ES30L enriched in birds and mammals can potentially regulate protein synthesis

Hariharan

Ghosh

Nallan

et al. 2022

Preprint

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Ribosomes, the molecular machines that are central to protein synthesis, have gradually been gaining prominence for their potential regulatory role in translation. Eukaryotic cytosolic ribosomes are typically larger than the bacterial ones, partly due to multi-nucleotide insertions at specific conserved positions in the ribosomal RNAs (rRNAs). Such insertions called expansion segments (ESs) are present primarily on the ribosomal surface, with their role in translation and its regulation remaining under-explored. One such ES in the ribosomal large subunit (LSU) is ES30L, which is observed mostly in mammals and birds among eukaryotes. In this study, we show that ES30L possesses complementarity to many protein-coding transcripts in humans and that the complementarity is enriched around the start codon, indicating a possible role in translation regulation. Further, our in silico analysis analyses and in vitro pull-down assays show that ES30L may bind to secondary structures in the 5′ UTR of several transcripts and RNA binding proteins (RBPs) that are essential for translation. Thus, we have identified a potential regulatory role for ES30L in translation.

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RNA-Binding Proteins as Regulators of Internal Initiation of Viral mRNA Translation

Cited by 13 publications

References 441 publications

Picornavirus translation strategies

Picornavirus translation strategies

Host–virus relationships: a sum of many battles

Expansion Segment ES30L enriched in birds and mammals can potentially regulate protein synthesis

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