Modification of the Leader Protein (Lb) of Foot-and-Mouth Disease Virus

Sangar, D. V.; Clark, Robin; Carroll, Anthony R.; Rowlands, David J.; Clarke, Berwyn

doi:10.1099/0022-1317-69-9-2327

Cited by 17 publications

(15 citation statements)

References 21 publications

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“…2; Belsham, 1992), the translational components (Kfihn et al, 1990) and on the salt concentrations (Sangar et al, 1988). The upstream A U G was more efficiently utilized in baby hamster kidney (BHK) cells than in reticulocyte lysates (Sangar et al, 1988). Our results and those of others (Dasso et al, 1990) suggest that the ratio of eIF-2-eIF-2B over other translational components is different in BHK cells fi'om that in reticulocyte lysates.…”

Section: Discussionmentioning

confidence: 52%

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Recognition of the initiation codon for protein synthesis in foot-and-mouth disease virus RNA

Thomas

Rijnbrand

Voorma

1996

Journal of General Virology

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Foot-and-mouth disease virus (FMDV) RNA utilizes two in-frame initiation codons to produce two precursor proteins with identical carboxy termini. The 5' untranslated region (5'UTR) directs the ribosome to internal sequences without the need for a cap structure as used in host mRNAs. The FMDV 5'UTR was cloned upstream of the reporter gene chloramphenicol acetyltransferase (CAT) in order to study the selection of initiation site and to facilitate quantification of the translation products. After in vitro transcription with T7 RNA polymerase and translation in rabbit reticulocyte lysate, the two CAT products, resulting from initiation from the two initiation codons, were quantified. The downstream initiator AUG (AUGLb) was selected more efficiently in the wild-type 5'UTR. In truncated RNA, the upstream initiation site (AUGL~b) was more efficiently utilized than in the wild-type 5'UTR. Protein synthesis initiation factors were added to translation assays to determine whether these factors influenced initiation site selection. Addition of eIF-2 and of eIF-2B changed the selection process for both types of RNA. These factors induced a 2.5-fold higher usage of the upstream AUGL~ b for wildtype and 5'UTR-truncated RNA. A change in mRNA concentration also induced a change in the usage of initiation codons; however, the effect of elF-2 was measured over a broad range of mRNA concentrations. In conclusion, elF-2 mediates the recognition of the initiation codon during both cap-dependent and internal ribosome entry site-dependent initiation.

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Section: Discussionmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Recognition of the initiation codon for protein synthesis in foot-and-mouth disease virus RNA

Thomas

Rijnbrand

Voorma

1996

Journal of General Virology

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“…However prolonged incubation did not result in further processing of P1 into the mature structural proteins. One new protein was observed after extended incubation (lane 3) but this has been recently identified as a modified version of Lb (Sangar et al, 1988) and is also observed in the protease-positive translation (lane 1). Therefore we can conclude that removal of the C terminus of 3C adjacent to His 182 inactivates the protease and is further indirect evidence that this residue is involved in the catalytic function.…”

Section: Resultsmentioning

confidence: 89%

“…However our data support those of Vakharia et al (1987) showing that these proteins are not involved in any of the other events in the proteolytic pathway of FMDV in vitro. One possible function which these proteins may perform is in the modification of the C termini of the leader proteins which has recently been described (Sangar et al, 1988). If so, these proteins would be bifunctional in nature.…”

Section: Studies On the Cleavage Specificity Of Fmd V 3c Proteasementioning

confidence: 99%

Processing and Assembly of Foot-and-Mouth Disease Virus Proteins Using Subgenomic RNA

Clarke

Sangar

1988

Journal of General Virology

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SUMMARYRecombinant DNA clones were constructed in order to study the mechanisms of proteolytic processing and assembly in foot-and-mouth disease virus (FMDV). RNA transcripts from these clones were synthesized using SP6 polymerase and translated in rabbit reticulocyte lysates. Efficient translation occurred in the absence of all 5" untranslated sequences and processing of the structural proteins occurred in the presence of functional 3C protease which can function in trans. The specificity of 3C protease activity is not limited to Glu-Gly bonds. Translation of correctly processed structural proteins leads to assembly of subviral structures resembling 'empty' particles. Further studies on the processing of the FMDV genome show that the primary cleavage (P l-P2) is mediated neither by 3C nor the second FMDV protease L. Preliminary evidence suggests that an initial very rapid cleavage occurs between 2A and 2B with subsequent cleavage of the P1/2A junction probably being carried out by 3C.

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“…degraded by FMDV protease [9], designated Lb [32]. The results show that in vitro translation of TPT is cap and p220 dependent.…”

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confidence: 99%

Dependence of the adenovirus tripartite leader on the p220 submit of eukaryotic initiation factor 4F during in vitro translation

Thomas

Scheper

Keleijn

et al. 1992

European Journal of Biochemistry

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The adenovirus tripartite leader (TPT) 5′ untranslated region (5′UTR) allows translation in poliovirus‐infected cells, in which the p220 subunit of eukaryotic initiation factor 4F is degraded. This p220‐independent translation was investigated by measuring in vitro translation in a reticulocyte lysate of a report gene, chloramphenicol acetyltransferase, coupled to the TPT 5′UTR. The p220 subunit was degraded by translation of a foot‐and‐mouth‐disease L‐protease construct. Surprisingly, the TPT 5′UTR was dependent on intact p220, as are other naturally capped mRNA species. Translation of encephalomyocarditis virus RNA was p220 independent, as expected from its ability to support internal, cap‐independent initiation. In vitro protein‐synthesis experiments with purified initiation factors confirmed the dependence of TPT mRNA translation on eukaryotic initiation factor 4F. The relationship between adenovirus TPT‐5′UTR‐directed translation and poliovirus‐induced host cell shut‐off is discussed.

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Modification of the Leader Protein (Lb) of Foot-and-Mouth Disease Virus

Cited by 17 publications

References 21 publications

Recognition of the initiation codon for protein synthesis in foot-and-mouth disease virus RNA

Recognition of the initiation codon for protein synthesis in foot-and-mouth disease virus RNA

Processing and Assembly of Foot-and-Mouth Disease Virus Proteins Using Subgenomic RNA

Dependence of the adenovirus tripartite leader on the p220 submit of eukaryotic initiation factor 4F during in vitro translation

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