Phosphorylation of influenza C virus CM2 protein
| Autor: | Yoko Matsuzaki, Seiji Hongo, Yuichiro Tada, Kanetsu Sugawara, Fumio Kitame, Yasushi Muraki, Kiyoto Nakamura |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
inorganic chemicals
Cancer Research Influenzavirus C Golgi Apparatus Oligosaccharides Chick Embryo macromolecular substances Biology Endoplasmic Reticulum environment and public health Phosphoamino acid analysis Viral Matrix Proteins Serine chemistry.chemical_compound symbols.namesake Virology Tumor Cells Cultured Animals Humans Protein phosphorylation Phosphorylation Endoplasmic reticulum Virion Biological Transport Tunicamycin Brefeldin A Golgi apparatus enzymes and coenzymes (carbohydrates) Infectious Diseases chemistry Biochemistry symbols bacteria Protein Processing Post-Translational |
| Zdroj: | Virus Research. 58:65-72 |
| ISSN: | 0168-1702 |
| Popis: | Labeling of influenza C virus-infected HMV-II cells with [32P]orthophosphate showed that the CM2 protein is posttranslationally modified by phosphorylation. The unglycosylated form of CM2 synthesized in the presence of tunicamycin was found to be highly phosphorylated. This result, together with the finding that digestion of CM2 with peptide-N-glycosidase F failed to remove the 32P label from the glycosylated form of CM2, indicated that phosphorylation occurs in the polypeptide backbone and not in the oligosaccharide chain. Furthermore, phosphoamino acid analysis revealed that phosphorylation occurs exclusively on serine residues. Treatment of infected cells with brefeldin A resulted in a complete inhibition of phosphorylation, showing that phosphorylation of CM2 occurs after its migration from the endoplasmic reticulum to the Golgi apparatus. Phosphorylation of CM2 was also inhibited strongly, although not completely, by monensin treatment, suggesting that CM2 is phosphorylated predominantly after its movement from medial to trans Golgi cisternae. Finally, we found that the CM2 protein incorporated into the progeny virion is phosphorylated, which indicates that there is no strictly selective incorporation of the unphosphorylated form of CM2 into the virion. |
| Databáze: | OpenAIRE |
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