Cell-free translation of foot-and-mouth disease virus RNA into identifiable non-capsid and capsid proteins
| Autor: | H. L. Bachrach, J. Polatnick, N. K. Chatterjee |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Peptide Biosynthesis
Reticulocytes Picornavirus Immunoprecipitation viruses Virus chemistry.chemical_compound Epitopes Viral Proteins Aphthovirus Capsid Ribonucleases Peptide Initiation Factors Virology Aurintricarboxylic acid Animals Carcinoma Ehrlich Tumor Gel electrophoresis biology Cell-Free System Aurintricarboxylic Acid virus diseases RNA biochemical phenomena metabolism and nutrition biology.organism_classification Molecular biology chemistry Protein Biosynthesis RNA Viral Puromycin Foot-and-mouth disease virus Peptides |
| Zdroj: | The Journal of general virology. 32(3) |
| ISSN: | 0022-1317 |
| Popis: | Foot-and-mouth disease virus (a member of the picornavirus group) RNA could be translated effectively in an S-30 extract from Ehrlich ascites tumour cells. This translation was inhibited by aurintricarboxylic acid, cycloheximide, puromycin and RNase. Cell-free products of translation were identified by disc gel electrophoresis and immunoprecipitation with specific antisera. Gel electrophoresis of the products without prior immunoprecipitation suggested the synthesis of some of the non-capsid proteins and capsid proteins VP1, VP2 and VP3 of the virus. Immunoprecipitations with antisera against whole virus and VP3 indicated the synthesis of VP3 and of at least two additional peptides of 100 000 and 56 000 daltons containing antigenic sites of VP3. Gel electrophoresis after immunoprecipitation with antiserum against virus infection-associated antigen indicated the synthesis of a different 56 000-dalton protein appearing to resemble non-capsid protein NCVP5. The amount of foot-and-mouth disease virus and VP3-specific peptides in the virus RNA-directed products were measured by immunoprecipitation. |
| Databáze: | OpenAIRE |
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