In vitro translation of mengovirus RNA deprived of the terminally‐linked (capping?) protein

Bercoff, R. Perez; Gander, M

doi:10.1016/0014-5793(78)80424-4

Cited by 33 publications

(14 citation statements)

References 18 publications

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“…but is instead covalently linked to a small virus-encoded protein (GOLINI et al 1978;HRUBY and ROBERTS 1978;VARTAPETIAN et al 1980) Removal of the VPg moiety from mengovirus RNA does not affect its ability to initiate translation (PEREZ-BERCOFF and GANDER 1978); similar results have been obtained using FMDV RNA (SANGAR et al 1980). These properties are common to all picornaviruses (WIMMER 1982).…”

Section: Primary Structure Of the Encephalomyocarditis Virus S'nermentioning

confidence: 57%

Translation of Encephalomyocarditis Virus RNA by Internal Ribosomal Entry

Hellen

Wimmer

1995

Current Topics in Microbiology and Immunology

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Section: Primary Structure Of the Encephalomyocarditis Virus S'nermentioning

confidence: 57%

Translation of Encephalomyocarditis Virus RNA by Internal Ribosomal Entry

Hellen

Wimmer

1995

Current Topics in Microbiology and Immunology

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“…Clearly, VPg is not essential for the translation of incoming viral RNA because proteinase K treatment of genomic viral RNA, thereby truncating the VPg peptide, did not affect translation efficiency (16,22). Moreover, in vitro transcribed RNA, consequently lacking VPg, is translated and replicated efficiently.…”

Section: Introductionmentioning

confidence: 99%

Modification of picornavirus genomic RNA using ‘click’ chemistry shows that unlinking of the VPg peptide is dispensable for translation and replication of the incoming viral RNA

Langereis

Qian

Nelissen

et al. 2013

Nucleic Acids Research

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Picornaviruses constitute a large group of viruses comprising medically and economically important pathogens such as poliovirus, coxsackievirus, rhinovirus, enterovirus 71 and foot-and-mouth disease virus. A unique characteristic of these viruses is the use of a viral peptide (VPg) as primer for viral RNA synthesis. As a consequence, all newly formed viral RNA molecules possess a covalently linked VPg peptide. It is known that VPg is enzymatically released from the incoming viral RNA by a host protein, called TDP2, but it is still unclear whether the release of VPg is necessary to initiate RNA translation. To study the possible requirement of VPg release for RNA translation, we developed a novel method to modify the genomic viral RNA with VPg linked via a ‘non-cleavable’ bond. We coupled an azide-modified VPg peptide to an RNA primer harboring a cyclooctyne [bicyclo[6.1.0]nonyne (BCN)] by a copper-free ‘click’ reaction, leading to a VPg-triazole-RNA construct that was ‘non-cleavable’ by TDP2. We successfully ligated the VPg-RNA complex to the viral genomic RNA, directed by base pairing. We show that the lack of VPg unlinkase does not influence RNA translation or replication. Thus, the release of the VPg from the incoming viral RNA is not a prerequisite for RNA translation or replication.

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“…They do not seem to be involved in the translation of the RNA of enteroviruses (Perez-Bercoff & Gander, 1978;Golini et al, 1980;Sangar et al, 1980), CPMV (Stanley et al, 1978), TBRV (Koenig, 1979;I. Koenig & C. Fritsch, personal communication) or TRSV (Chu et aL, 1981), and they have not been found in poliovirus messenger RNA .…”

Section: Discussionmentioning

confidence: 99%

“…wt. 2000 to 12000 are also known to be linked to the genome RNA of several viruses of vertebrates (Flanegan et al, 1977;Lee et al, 1977;Sangar et al, 1977, Burroughs & Brown, 1978Hruby & Roberts, 1978;Perez-Bercoff & Gander, 1978;Schaffer et al, 1980), and to that of cowpea mosaic virus (CPMV) (comovirus group; Daubert et al, 1978;Stanley et al, 1978) and southern bean mosaic virus (Ghosh et al, 1979). In those instances examined, the genome-linked protein (VPg) is attached at the 5'-end of the RNA Sangar et al, 1977;Golini et al, 1978;Stanley et al, 1978).…”

Section: Introductionmentioning

confidence: 99%

Specificity and Properties of the Genome-linked Proteins of Nepoviruses

Mayo¹,

Barker²,

Harrison³

1982

Journal of General Virology

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SUMMARYThe infectivity of the RNA of six nepoviruses was decreased or abolished by proteinase K treatment, whereas that of the RNA of cowpea mosaic virus (comovirus group) or tomato bushy stunt virus was unaffected. The extent of the decrease in infectivity was characteristic for each nepovirus and was independent of the plant species used as virus source or as assay host. The infectivity of raspberry ringspot virus (RRV) RNA was less affected than that of the other nepoviruses but treatment with Pronase decreased infectivity more than treatment with proteinase K. Proteinase K treatment also abolished the infectivity for tobacco mesophyll protoplasts of RNA of tobacco ringspot virus (TRSV) and tomato black ring virus (TBRV).Tests on virus RNA, labelled with ~25I by the chloramine T method, provided evidence that three nepoviruses and Echtes Ackerbohnenmosaik-Virus (EAMV; comovirus group) have genome-linked proteins (VPg). Pronase treatment rendered about half (RNA of strawberry latent ringspot virus; SLRV), or nearly all (RNA of the other nepoviruses and EAMV), of the '25I soluble in 70 % ethanol. Treatment of nepovirus RNA with ribonuclease P 1 yielded a product with an estimated mol. wt. of 4000 __+ 900. Mobilities in polyacrylamide gels of VPg from the RNA of different viruses differed slightly (SLRV > TBRV > TRSV > RRV). TRSV VPg yielded one ~25I-labelled tryptic peptide whereas the genome-linked proteins of RRV and TBRV both yielded two major products, of which one was resistant to further digestion and the other was converted, apparently via intermediates, to a second more stable product. No difference was detected between the tryptic peptides obtained from VPg of different strains of RRV, or of TBRV, or between those obtained from RNA-1, RNA-2 or RNA-3 (satellite RNA) of TBRV. Nepovirus VPg is therefore virus-specific. It seems to be coded on RNA-1 and probably has multiple functions.

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In vitro translation of mengovirus RNA deprived of the terminally‐linked (capping?) protein

Cited by 33 publications

References 18 publications

Translation of Encephalomyocarditis Virus RNA by Internal Ribosomal Entry

Translation of Encephalomyocarditis Virus RNA by Internal Ribosomal Entry

Modification of picornavirus genomic RNA using ‘click’ chemistry shows that unlinking of the VPg peptide is dispensable for translation and replication of the incoming viral RNA

Specificity and Properties of the Genome-linked Proteins of Nepoviruses

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