Surface Structure and RNA-Protein Interactions of Foot-and-Mouth Disease Virus
| Autor: | F. Brown, E. J. C. Mellor, D. J. Morrell, D. J. Rowlands |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
viruses
Lysine Succinimides Models Biological Virus Viral Proteins Aphthovirus Virology medicine Sulfites Antigens Viral Viral Structural Proteins chemistry.chemical_classification biology RNA biology.organism_classification Trypsin Molecular biology Amino acid Capsid Biochemistry chemistry RNA Viral Foot-and-mouth disease virus medicine.drug |
| Zdroj: | Journal of General Virology. 68:1649-1658 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/0022-1317-68-6-1649 |
| Popis: | Summary The surface structure of foot-and-mouth disease virus (FMDV) and the interaction of the individual capsid proteins with the virus RNA have been examined using modification reagents. By measuring the extent of modification of the lysine residues of intact and disrupted virus particles and the 12S protein subunit with Bolton & Hunter reagent it was found that 54% of the residues of VP1, 15% of the residues of VP2 and 37% of the residues of VP3, equivalent to five, two and four lysine residues respectively, are on the surface of the intact virus particle. Polypeptide VP4 was not modified in intact virus particles, indicating that it has no lysine residues on the surface of the virus. Modification with sodium metabisulphite, which causes a specific transamination reaction between cytidylic acid residues in ssRNA and closely associated basic amino acids, cross-linked all four structural proteins to the virus RNA. Both fragments of VP1, produced by treatment of the virus particle with trypsin, are also cross-linked to the RNA. These observations have been combined with the evidence that the immunogenic activity of VP1 may be contained in two discontinuous sites, at amino acids 141 to 160 and 200 to 213, in proposing a model for the arrangement of this polypeptide in the virus particle. |
| Databáze: | OpenAIRE |
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