Sobemoviruses

Tamm, Tiina; Truve, Erkki

doi:10.1128/jvi.74.14.6231-6241.2000

Cited by 83 publications

(63 citation statements)

References 105 publications

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“…NMR studies on cowpea mosaic virus VPg suggested that it does not have any ordered structure (7). In Sobemoviruses, the size of VPg varies between 9 and 12 kDa (8), and it is 9 kDa in SeMV, consisting of 77 amino acid residues (1). The presence of VPg linked to the 5Ј end of the genomic RNA has been confirmed by determining the N-terminal amino acid sequence of VPg in Southern bean mosaic virus, Cocksfoot mottle virus, and SeMV genomic RNA (1, 9, 10).…”

mentioning

confidence: 95%

“Natively Unfolded” VPg Is Essential for Sesbania Mosaic Virus Serine Protease Activity

Satheshkumar

Gayathri

Prasad

et al. 2005

Journal of Biological Chemistry

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Polyprotein processing is a major strategy used by many plant and animal viruses to maximize the number of protein products obtainable from a single open reading frame. In Sesbania mosaic virus, open reading frame-2 codes for a polyprotein that is cleaved into different functional proteins in cis by the N-terminal serine protease domain. The soluble protease domain lacking 70-amino-acid residues from the N terminus (⌬N70Pro, where Pro is protease) was not active in trans. Interestingly, the protease domain exhibited trans-catalytic activity when VPg (viral protein genome-linked) was present at the C terminus. Bioinformatic analysis of VPg primary structure suggested that it could be a disordered protein. Biophysical studies validated this observation, and VPg resembled "natively unfolded" proteins. CD spectral analysis showed that the ⌬N70Pro-VPg fusion protein had a characteristic secondary structure with a 230 nm positive CD peak. Mutation of Trp-43 in the VPg domain to phenylalanine abrogated the positive peak with concomitant loss in cis-and trans-proteolytic activity of the ⌬N70Pro domain. Further, deletion of VPg domain from the polyprotein completely abolished proteolytic processing. The results suggested a novel mechanism of activation of the protease, wherein the interaction between the natively unfolded VPg and the protease domains via aromatic amino acid residues alters the conformation of the individual domains and the active site of the protease. Thus, VPg is an activator of protease in Sesbania mosaic virus, and probably by this mechanism, the polyprotein processing could be regulated in planta.

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mentioning

confidence: 95%

“Natively Unfolded” VPg Is Essential for Sesbania Mosaic Virus Serine Protease Activity

Satheshkumar

Gayathri

Prasad

et al. 2005

Journal of Biological Chemistry

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“…Based on organizational differences in the central part of the genome (encoding the virus polyprotein), the sobemoviruses were subdivided into Southern cowpea mosaic virus (SCPMV)-like and Cocksfoot mottle virus (CfMV)-like types (42,46). First reported to have an SCPMV-like organization (28), RYMV is now suspected to be of the CfMV type (12).…”

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confidence: 99%

Inferring the Evolutionary History of Rice Yellow Mottle Virus from Genomic, Phylogenetic, and Phylogeographic Studies

Fargette

Pinel

Abubakar

et al. 2004

J Virol

106

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Fourteen isolates of Rice yellow mottle virus (RYMV) were selected as representative of the genetic variability of the virus in Africa from a total set of 320 isolates serologically typed or partially sequenced. The 14 isolates were fully sequenced and analyzed together with two previously reported sequences. RYMV had a genomic organization similar to that of Cocksfoot mottle sobemovirus. The average nucleotide diversity among the 16 isolates of RYMV was 7%, and the maximum diversity between any two isolates was 10%. A strong conservative selection was apparent on both synonymous and nonsynonymous substitutions, through the amino acid replacement pattern, on the genome size, and through the limited number of indel events. Furthermore, there was a lack of positive selection on single amino acid sites and no evidence of recombination events. RYMV diversity had a pronounced and characteristic geographic structure. The branching order of the clades correlated with the geographic origin of the isolates along an east-to-west transect across Africa, and there was a marked decrease in nucleotide diversity moving westward across the continent. The insertion-deletion polymorphism was related to virus phylogeny. There was a partial phylogenetic incongruence between the coat protein gene and the rest of the genome. Overall, our results support the hypothesis that RYMV originated in East Africa and then dispersed and differentiated gradually from the east to the west of the continent.

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“…The virus disease was first recorded in 1966 at Otonglo near Lake Victoria, Kenya (Bakker, 1970) and until now the RYMV is present in most of the rice-growing countries in Africa and Madagascar (Abo et al, 1998;Kouassi et al, 2005;Séré et al, 2008;Traoré et al, 2009). The virus belongs to the genus Sobemovirus (Tamm and Truve, 2000; and is characterized by icosahedral particles of about 30 nm in diameter and one single strand positive sense genomic ribonucleic acid (RNA). The virus is associated with viroid-like satellite RNA ranging from 220 to 390 nucleotides (Tamm and Truve, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…The virus belongs to the genus Sobemovirus (Tamm and Truve, 2000; and is characterized by icosahedral particles of about 30 nm in diameter and one single strand positive sense genomic ribonucleic acid (RNA). The virus is associated with viroid-like satellite RNA ranging from 220 to 390 nucleotides (Tamm and Truve, 2000).…”

Section: Introductionmentioning

confidence: 99%

Immunocapture and simple-direct-tube-reverse transcriptase polymerase chain reaction (RT-PCR) for detection of Rice yellow mottle virus

Hubert¹,

Lyimo²,

Luzi-Kihupi³

et al. 2017

Afr. J. Biotechnol.

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This study aimed at optimizing the immunocapture (IC) and simple-direct-tube (SDT) -reverse transcriptase polymerase chain reaction (RT-PCR) techniques for detection ofThe results also show that these techniques are rapid methods for characterization of RYMV strains and may be recommended for use soon after periodical surveys to quickly identify new strains for breeding purposes at low cost. However, SDT protocol was easier and faster than IC and it was also cost-effective in terms of reagents for the detection of RYMV.

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Sobemoviruses

Cited by 83 publications

References 105 publications

“Natively Unfolded” VPg Is Essential for Sesbania Mosaic Virus Serine Protease Activity

“Natively Unfolded” VPg Is Essential for Sesbania Mosaic Virus Serine Protease Activity

Inferring the Evolutionary History of Rice Yellow Mottle Virus from Genomic, Phylogenetic, and Phylogeographic Studies

Immunocapture and simple-direct-tube-reverse transcriptase polymerase chain reaction (RT-PCR) for detection of Rice yellow mottle virus

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