Equine arteritis virus-induced polypeptide synthesis.
Abstract: Intracellular virus-specific proteins induced by equine arteritis virus (EAV) have been compared with in vitro translation products of virion and intracellular EAV RNAs. In infected BHK-21 cells, the two major virion proteins (C and E1) and polypeptides with mol. wt. of 60,000 (p60), 42,000 (p42) and 30,000 (p30) were found. There were no indications that the viral proteins were processed from a larger precursor as shown by pulse-chase, amino acid analogue and protease inhibitor experiments. The six polyadenylated RNAs that occur in EAV-infected cells were isolated and translated in an mRNA-dependent reticulocyte cell-free system. Translation of RNA6 resulted in the appearance of a product having the mol. wt. (14,000) of the nucleocapsid protein (C). EAV genomic RNA was translated into proteins of mol. wt. 30,000 and 200,000, while RNA1, the intracellular homologue of genomic RNA only encoded p30. The absence of large precursor molecules in infected cells and the results from the in vitro translation experiments both suggest that at least some of the proteins are primary translation products.
Publication Date: 1986-08-01 PubMed ID: 2426393DOI: 10.1099/0022-1317-67-8-1543Google Scholar: Lookup
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- Journal Article
Summary
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This research investigates the production of virus-specific proteins activated by the equine arteritis virus (EAV). It compares these in-vivo viral proteins with in-vitro end products of EAV RNA translations, and concludes that several proteins may be primary translation products, without needing to be processed from larger precursors.
Outline of the Research
- This research primarily aims to shed light on the synthesis of proteins activated by the equine arteritis virus (EAV).
- To do this, it examines the proteins produced within BHK-21 cells after infection by EAV.
- The examination identifies two major virion proteins – referred to as C and E1 – and other polypeptides of varying molecular weights.
Experimentation Process
- The researchers conducted various experiments, including pulse-chase experiments, which involve monitoring changes in molecules over time, use of amino acid analogues, and protease inhibitors.
- The outcomes of these experiments showed no sign that the viral proteins emerged from larger precursors, suggesting they could be primary translation products.
- The research isolated and translated the six polyadenylated RNAs that appear in EAV-infected cells into an mRNA-dependent reticulocyte cell-free system.
Findings and Conclusion
- The outcome of the RNA6 translation resulted in a product with the molecular weight of the nucleocapsid protein (C).
- EAV genomic RNA was translated into proteins of molecular weight 30,000 and 200,000, while RNA1, the intracellular analogue of genomic RNA, only encoded protein p30.
- The study concludes that the absence of large precursor molecules in infected cells and the findings from the in-vitro translation experiments both imply that some proteins are initial translation products.
Cite This Article
APA
van Berlo MF, Rottier PJ, Spaan WJ, Horzinek MC.
(1986).
Equine arteritis virus-induced polypeptide synthesis.
J Gen Virol, 67 ( Pt 8), 1543-1549.
https://doi.org/10.1099/0022-1317-67-8-1543 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Capsid / biosynthesis
- Capsid / genetics
- Cell Line
- Cricetinae
- Equartevirus / genetics
- Equartevirus / metabolism
- Molecular Weight
- Poly A / genetics
- Protein Biosynthesis
- Protein Processing, Post-Translational
- RNA / genetics
- RNA Viruses / metabolism
- RNA, Messenger
- RNA, Viral / genetics
- Viral Core Proteins / biosynthesis
- Viral Core Proteins / genetics
- Viral Proteins / biosynthesis
- Viral Proteins / genetics
Citations
This article has been cited 12 times.- Glaser AL, Chirnside ED, Horzinek MC, de Vries AA. Equine arteritis virus. Theriogenology 1997 Apr 15;47(6):1275-95.
- Wieringa R, De Vries AA, Post SM, Rottier PJ. Intra- and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity. J Virol 2003 Dec;77(24):12996-3004.
- Wieringa R, de Vries AA, Rottier PJ. Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus. J Virol 2003 Jun;77(11):6216-26.
- Wieringa R, de Vries AA, Raamsman MJ, Rottier PJ. Characterization of two new structural glycoproteins, GP(3) and GP(4), of equine arteritis virus. J Virol 2002 Nov;76(21):10829-40.
- Godeny EK, de Vries AA, Wang XC, Smith SL, de Groot RJ. Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: evidence for gene duplication during arterivirus evolution. J Virol 1998 Jan;72(1):862-7.
- Kheyar A, Martin S, St-Laurent G, Timoney PJ, McCollum WH, Archambault D. Expression cloning and humoral immune response to the nucleocapsid and membrane proteins of equine arteritis virus. Clin Diagn Lab Immunol 1997 Nov;4(6):648-52.
- Chirnside ED, Francis PM, Mumford JA. Expression cloning and antigenic analysis of the nucleocapsid protein of equine arteritis virus. Virus Res 1995 Dec;39(2-3):277-88.
- Godeny EK, Zeng L, Smith SL, Brinton MA. Molecular characterization of the 3' terminus of the simian hemorrhagic fever virus genome. J Virol 1995 Apr;69(4):2679-83.
- de Vries AA, Chirnside ED, Bredenbeek PJ, Gravestein LA, Horzinek MC, Spaan WJ. All subgenomic mRNAs of equine arteritis virus contain a common leader sequence. Nucleic Acids Res 1990 Jun 11;18(11):3241-7.
- den Boon JA, Snijder EJ, Chirnside ED, de Vries AA, Horzinek MC, Spaan WJ. Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily. J Virol 1991 Jun;65(6):2910-20.
- de Vries AA, Chirnside ED, Horzinek MC, Rottier PJ. Structural proteins of equine arteritis virus. J Virol 1992 Nov;66(11):6294-303.
- Chirnside ED. Equine arteritis virus: an overview. Br Vet J 1992 May-Jun;148(3):181-97.
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