Two cellular proteins that interact with a stem loop in the simian hemorrhagic fever virus 3′(+)NCR RNA

Maines, Taronna R.; Young, Mary K.; Dinh, Nikita; Brinton, Margo A.

doi:10.1016/j.virusres.2004.11.014

Cited by 15 publications

(10 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Six predicted transmembrane-spanning domains (TM1-TM6) are numbered. Maines et al, 2005;Beerens and Snijder, 2006). The highly conserved nature of the ronivirus 3′-UTR RNA structure suggests it may also act as a polymerase recognition signal for minus-strand RNA synthesis.…”

Section: Discussionmentioning

confidence: 99%

Genetic diversity in the yellow head nidovirus complex

et al. 2008

View full text Add to dashboard Cite

Penaeus monodon shrimp collected from across the Indo-Pacific region during 1997-2004 were screened for the presence of yellow head-related viruses. Phylogenetic analyses of amplified ORF1b gene segments identified at least six distinct genetic lineages (genotypes). Genotype 1 (YHV) was detected only in shrimp with yellow head disease. Genotype 2 (GAV) was detected in diseased shrimp with the less severe condition described as mid-crop mortality syndrome and in healthy shrimp from Australia, Thailand and Vietnam. Other genotypes occurred commonly in healthy shrimp. Sequence comparisons of structural protein genes (ORF2 and ORF3), intergenic regions (IGRs) and the long 3'-UTR supported the delineation of genotypes and identified both conserved and variant structural features. In putative transcription regulating sequences (TRSs) encompassing the sub-genomic mRNA 5'-termini, a core motif (5'-GUCAAUUACAAC-3') is absolutely conserved. A small (83 nt) open reading frame (ORF4) in the 3'-UTR of GAV is variously truncated in all other genotypes and a TRS-like element preceding ORF4 is invariably corrupted by a A>G/U substitution in the central core motif (5'-UU(G/U)CAAC-3'). The data support previous evidence that ORF4 is a non-functional gene under construction or deconstruction. The 3'-UTRs also contain predicted 3'-terminal hairpin-loop structures that are preserved in all genotypes by compensatory nucleotide substitutions, suggesting a role in polymerase recognition for minus-strand RNA synthesis.

show abstract

Section: Discussionmentioning

confidence: 99%

Genetic diversity in the yellow head nidovirus complex

et al. 2008

View full text Add to dashboard Cite

show abstract

“…Little is known about host proteins that may interact with arterivirus RNA or transmembrane non-structural proteins, or that may be recruited to replication structures. Common sets of (as-yet unidentified) host proteins bind in vitro to the 3' end of the genome or anti-genome of SHFV, EAV and PRRSV, and were implicated in the initiation of arterivirus RNA synthesis (Hwang & Brinton, 1998;Maines et al, 2005). The RNA-synthesizing activity of EAV RTCs associated with crude membrane fractions from infected cells does depend on membrane integrity.…”

Section: Replication Structuresmentioning

confidence: 99%

Arterivirus molecular biology and pathogenesis

Snijder

Kikkert

Fāng

2013

Journal of General Virology

370

344

View full text Add to dashboard Cite

Arteriviruses are positive-stranded RNA viruses that infect mammals. They can cause persistent or asymptomatic infections, but also acute disease associated with a respiratory syndrome, abortion or lethal haemorrhagic fever. During the past two decades, porcine reproductive and respiratory syndrome virus (PRRSV) and, to a lesser extent, equine arteritis virus (EAV) have attracted attention as veterinary pathogens with significant economic impact. Particularly noteworthy were the 'porcine high fever disease' outbreaks in South-East Asia and the emergence of new virulent PRRSV strains in the USA. Recently, the family was expanded with several previously unknown arteriviruses isolated from different African monkey species. At the molecular level, arteriviruses share an intriguing but distant evolutionary relationship with coronaviruses and other members of the order Nidovirales. Nevertheless, several of their characteristics are unique, including virion composition and structure, and the conservation of only a subset of the replicase domains encountered in nidoviruses with larger genomes. During the past 15 years, the advent of reverse genetics systems for EAV and PRRSV has changed and accelerated the structure-function analysis of arterivirus RNA and protein sequences. These systems now also facilitate studies into host immune responses and arterivirus immune evasion and pathogenesis. In this review, we have summarized recent advances in the areas of arterivirus genome expression, RNA and protein functions, virion architecture, virus-host interactions, immunity, and pathogenesis. We have also briefly reviewed the impact of these advances on disease management, the engineering of novel candidate live vaccines and the diagnosis of arterivirus infection.

show abstract

“…This capacity might also explain many of the other functions of PTB, like its role in IRES-mediated translation initiation [43,44,46,47]. The structure of the complex also explains how several pyrimidine-rich pentaloops could create a PTB binding site in an IRES [50] or the 3'UTR of certain viral RNAs [95,96], since all four RRMs bind only three to five pyrimidines each. However, it remains to be determined which of the four RRMs can bind such pentaloops (Fig.…”

Section: How Can the Ptb Structures Explain Its Multiple Functionsmentioning

confidence: 99%

Structure-function relationships of the polypyrimidine tract binding protein

Auweter

Allain

2007

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

Abstract. The polypyrimidine tract binding protein (PTB) is a 58-kDa RNA binding protein involved in multiple aspects of mRNA metabolism including splicing regulation, polyadenylation, 3'end formation, internal ribosomal entry site-mediated translation, RNA localization and stability. PTB contains four RNA recognition motifs (RRMs) separated by three linkers. In this review we summarize structural information on PTB in solution that has been gathered during the past 7 years using NMR spectroscopy and small-angle X-ray scattering. The structures of all RRMs of PTB in their free state and in complex with short pyrimidine tracts, as well as a structural model of PTB RRM2 in complex with a peptide, revealed unusual structural features that provided new insights into the mechanisms of action of PTB in the different processes of RNA metabolism and in particular splicing regulation.

show abstract

Two cellular proteins that interact with a stem loop in the simian hemorrhagic fever virus 3′(+)NCR RNA

Cited by 15 publications

References 67 publications

Genetic diversity in the yellow head nidovirus complex

Genetic diversity in the yellow head nidovirus complex

Arterivirus molecular biology and pathogenesis

Structure-function relationships of the polypyrimidine tract binding protein

Contact Info

Product

Resources

About