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The 5�-terminal region of the Aichi virus genome encodes cis-acting replication elements required for positive- and negative-strand RNA synthesis
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, 2005
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Bakkali Kassimi L. Encephalomyocarditis virus, in Molecular Detection of Human Viral Pathogens. 1st Ed
, 2010
"... TNFa, tumor necrosis factor a; NO, nitric oxide; iNOS, inducible nitric oxide synthase; RIG-I, retinoic acid-inducible gene 1 protein; MDA-5, melanoma differentiation-associated gene-5 The encephalomyocarditis virus (EMCV) is a small non-enveloped single-strand RNA virus, the causative agent of not ..."
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TNFa, tumor necrosis factor a; NO, nitric oxide; iNOS, inducible nitric oxide synthase; RIG-I, retinoic acid-inducible gene 1 protein; MDA-5, melanoma differentiation-associated gene-5 The encephalomyocarditis virus (EMCV) is a small non-enveloped single-strand RNA virus, the causative agent of not only myocarditis and encephalitis, but also neurological diseases, reproductive disorders and diabetes in many mammalian species. EMCV pathogenesis appears to be viral strain- and host-specific, and a better understanding of EMCV virulence factors is increasingly required. Indeed, EMCV is often used as a model for diabetes and viral myocarditis, and is also widely used in immunology as a double-stranded RNA stimulus in the study of Toll-like as well as cytosolic receptors. However, EMCV virulence and properties have often been neglected. Moreover, EMCV is able to infect humans albeit with a low morbidity. Progress on xenografts, such as pig heart
Interaction between polypeptide 3ABC and the 5�-terminal structural elements of the genome of Aichi virus: implication for negative-strand RNA synthesis
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, 2008
"... Secondary structural elements at the 5 end of picornavirus genomic RNA function as cis-acting replication elements and are known to interact specifically with viral P3 proteins in several picornaviruses. In poliovirus, ribonucleoprotein complex formation at the 5 end of the genome is required for ..."
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Secondary structural elements at the 5 end of picornavirus genomic RNA function as cis-acting replication elements and are known to interact specifically with viral P3 proteins in several picornaviruses. In poliovirus, ribonucleoprotein complex formation at the 5 end of the genome is required for negative-strand synthesis. We have previously shown that the 5-end 115 nucleotides of the Aichi virus genome, which are predicted to fold into two stem-loops (SL-A and SL-C) and one pseudoknot (PK-B), act as a cis-acting replication element and that correct folding of these structures is required for negative-strand synthesis. In this study, we investigated the interaction between the 5-terminal 120 nucleotides of the genome and the P3 proteins, 3AB, 3ABC, 3C, and 3CD, by gel shift assay and Northwestern analysis. The results showed that 3ABC and 3CD bound to the 5-terminal region specifically. The binding of 3ABC was observed on both assays, while that of 3CD was detected only on Northwestern analysis. No binding of 3AB or 3C was observed. Binding assays using mutant RNAs demonstrated that disruption of the base pairings of the stem of SL-A and one of the two stem segments of PK-B (stem-B1) abolished the 3ABC binding. In addition, the specific nucleotide sequence of stem-B1 was responsible for the efficient 3ABC binding. These results suggest that the interaction of 3ABC with the 5-terminal region of the genome is involved in negative-strand synthesis. On the other hand, the ability of 3CD to interact with the 5-terminal region did not correlate with the RNA replication ability.
Kobuvirus and Proposed Salivirus and Paraturdivirus Genera
, 2016
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All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately.
A Distinct Class of Internal Ribosomal Entry Site in Members of the Kobuvirus and Proposed
"... The 5=-untranslated regions (5=UTRs) of picornavirus genomes contain an internal ribosomal entry site (IRES) that promotes the end-independent initiation of translation. Picornavirus IRESs are classified into four structurally distinct groups, each with different initiation factor requirements. Here ..."
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The 5=-untranslated regions (5=UTRs) of picornavirus genomes contain an internal ribosomal entry site (IRES) that promotes the end-independent initiation of translation. Picornavirus IRESs are classified into four structurally distinct groups, each with different initiation factor requirements. Here, we identify a fifth IRES class in members ofKobuvirus, Salivirus, and Paraturdivi-rus genera of Picornaviridae: Aichi virus (AV), bovine kobuvirus (BKV), canine kobuvirus (CKoV), mouse kobuvirus (MKoV), sheep kobuvirus (SKV), salivirus A (SV-A), turdivirus 2 (TV2), and TV3. The 410-nucleotide (nt)-long AV IRES comprises four domains (I to L), including a hairpin (L) that overlaps a Yn-Xm-AUG (pyrimidine tract/spacer/initiation codon) motif. SV-A, CKoV, andMKoV also contain these four domains, whereas BKV, SKV, and TV2/TV3 5=UTRs contain domains that are related to domain I and equivalent to domains J and K but lack an AV-like domain L. These IRESs are located at different relative posi-tions between a conserved 5=-terminal origin of replication and divergent coding sequences. Elements in these IRESs also occur elsewhere: domain J’s apical subdomain, which contains a GNRA tetraloop, matches an element in type 1 IRESs, and eIF4G-binding motifs in domain K and in type 2 IRESs are identical. Other elements are unique, and their presence leads to unique ini-tiation factor requirements. In vitro reconstitution experiments showed that like AV, but in contrast to other currently charac-terized IRESs, SV-A requires the DExH-box protein DHX29 during initiation, which likely ensures that the initiation codon sequestered in domain L is properly accommodated in the ribosomal mRNA-binding cleft. The genomes of RNA viruses contain structural elements thathave important roles in translation, replication, and encapsi-
Virology Journal BioMed Central
, 2009
"... The complete genome of klassevirus – a novel picornavirus in pediatric stool ..."
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The complete genome of klassevirus – a novel picornavirus in pediatric stool
RESEARCH ARTICLE Open Access Distribution of
"... mutational fitness effects and of epistasis in the 5 ’ untranslated region of a plant RNA virus ..."
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mutational fitness effects and of epistasis in the 5 ’ untranslated region of a plant RNA virus
Structure of Ljungan virus provides insight into genome packaging of this picornavirus
"... Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are those that lack the internal coat protein, VP4. Here we report the atomic structure of one such virus, L ..."
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Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are those that lack the internal coat protein, VP4. Here we report the atomic structure of one such virus, Ljungan virus, the type member of the genus Parechovirus B, which has been linked to diabetes and myocarditis in humans. The 3.78-Å resolution cryo-electron microscopy structure shows remarkable features, including an extended VP1 C terminus, forming a major protuberance on the outer surface of the virus, and a basic motif at the N terminus of VP3, binding to which orders some 12 % of the viral genome. This apparently charge-driven RNA attachment suggests that this branch of the picornaviruses uses a different mechanism of genome encapsidation, perhaps explored early in the evolution of picornaviruses.
CONTENT ALERTS
, 2007
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