About: Characterization of Ribosomal Frameshifting in Theiler's Murine Encephalomyelitis Virus

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About: Characterization of Ribosomal Frameshifting in Theiler's Murine Encephalomyelitis Virus Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Characterization of Ribosomal Frameshifting in Theiler's Murine Encephalomyelitis Virus
Creator	Ling, Roger Brierley, Ian Michiels, Thomas Bell, Susanne Napthine, Sawsan Olspert, Allan Loughran, Gary Lardinois, Cécile Firth, Andrew Finch, Leanne
source	Medline; PMC
abstract	Theiler's murine encephalomyelitis virus (TMEV) is a member of the genus Cardiovirus in the Picornaviridae, a family of positive-sense single-stranded RNA viruses. Previously, we demonstrated that in the related cardiovirus, Encephalomyocarditis virus, a programmed −1 ribosomal frameshift (−1 PRF) occurs at a conserved G_GUU_UUU sequence within the 2B-encoding region of the polyprotein open reading frame (ORF). Here we show that −1 PRF occurs at a similar site during translation of the TMEV genome. In addition, we demonstrate that a predicted 3′ RNA stem-loop structure at a noncanonical spacing downstream of the shift site is required for efficient frameshifting in TMEV and that frameshifting also requires virus infection. Mutating the G_GUU_UUU shift site to inhibit frameshifting results in an attenuated virus with reduced growth kinetics and a small-plaque phenotype. Frameshifting in the virus context was found to be extremely efficient at 74 to 82%, which, to our knowledge, is the highest frameshifting efficiency recorded to date for any virus. We propose that highly efficient −1 PRF in TMEV provides a mechanism to escape the confines of equimolar expression normally inherent in the single-polyprotein expression strategy of picornaviruses. IMPORTANCE Many viruses utilize programmed −1 ribosomal frameshifting (−1 PRF) to produce different protein products at a defined ratio, or to translate overlapping ORFs to increase coding capacity. With few exceptions, −1 PRF occurs on specific “slippery” heptanucleotide sequences and is stimulated by RNA structure beginning 5 to 9 nucleotides (nt) downstream of the slippery site. Here we describe an unusual case of −1 PRF in Theiler's murine encephalomyelitis virus (TMEV) that is extraordinarily efficient (74 to 82% of ribosomes shift into the alternative reading frame) and, in stark contrast to other examples of −1 PRF, is dependent upon a stem-loop structure beginning 14 nt downstream of the slippery site. Furthermore, in TMEV-based reporter constructs in transfected cells, efficient frameshifting is critically dependent upon virus infection. We suggest that TMEV evolved frameshifting as a novel mechanism for removing ribosomes from the message (a “ribosome sink”) to downregulate synthesis of the 3′-encoded replication proteins.
has issue date	2015-06-10(xsd:dateTime)
bibo:doi	10.1128/jvi.01043-15
bibo:pmid	26063423
has license	cc-by
sha1sum (hex)	975a7b5f0f9a7f9a03195cb5cd1a633ecd4e36f8
schema:url	https://doi.org/10.1128/jvi.01043-15
resource representing a document's title	Characterization of Ribosomal Frameshifting in Theiler's Murine Encephalomyelitis Virus
has PubMed Central identifier	PMC4524249
has PubMed identifier	26063423
schema:publication	J Virol
resource representing a document's body	covid:975a7b5f0f9a7f9a03195cb5cd1a633ecd4e36f8#body_text
is schema:about of	named entity 'stem-loop' named entity 'translation' named entity 'programmed' named entity 'RNA' covid:arg/975a7b5f0f9a7f9a03195cb5cd1a633ecd4e36f8 named entity 'sequence' named entity 'structure' named entity 'expression' named entity 'PRF' named entity 'murine' named entity 'spacing' named entity 'virus' named entity 'ribosomal frameshift' named entity 'genome' named entity 'inherent' named entity 'TMEV' named entity 'Frameshifting' named entity 'virus' named entity 'Encephalomyocarditis virus' named entity 'genome' named entity 'TMEV' named entity 'Cardiovirus' named entity 'frameshifting' named entity 'ribosomal frameshift' named entity 'growth kinetics' named entity 'frameshifting' named entity 'frameshifting' named entity 'stem-loop structure' named entity 'Virus' named entity 'Ribosomal Frameshifting' named entity 'Murine' named entity 'mRNA' named entity 'Agilent Technologies' named entity 'frameshifting' named entity 'Frameshifting' named entity 'Transfected' named entity 'subclone' named entity 'BHK-21 cells' named entity 'Frameshifting' named entity 'TMEV' named entity 'frameshift' named entity 'Encephalomyocarditis virus' named entity 'BHK-21 cells' named entity 'ribosomes' named entity 'downregulate' named entity 'protein synthesis' named entity 'virus' named entity 'cardiovirus' named entity 'metabolic' named entity 'TMEV' named entity 'virus' named entity 'EMCV' named entity 'VP3' named entity 'virus' named entity 'luciferase' named entity 'frameshifting' named entity 'ribosomes' named entity 'ribosomes' named entity 'mutagenesis' named entity 'ribosomes' named entity 'PBS' named entity 'mRNA' named entity 'subcloned' named entity 'TMEV' named entity 'TMEV' named entity 'Picornaviridae' named entity 'polyprotein' named entity 'firefly luciferase' named entity 'antibodies' named entity 'protein complex' named entity 'stem-loop' named entity 'gene'

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