Post-translational modifications of poliovirus proteins.
The post-translational modifications of poliovirus proteins have been investigated by analysis of glycosylation, sulphation, phosphorylation and acylation of the proteins made in the infected HeLa cells. No glycosylation or sulphation of proteins specific for virus-infected cells was apparent. A number of changes in the pattern of phosphorylated proteins took place. The specific myristylation of the structural protein VP4 and its precursors was clearly apparent. Acylation of viral proteins with oleic or palmitic acid was not detected. Myristylation took place in the presence of the protease inhibitor ZnCl2, but not in the presence of inhibitors of translation, such as cycloneximide and anysomycin.
Urzainqui
A
A
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Canto Blanco, Madrid, Spain.
Carrasco
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L
D015180:Electrophoresis, Gel, Two-Dimensional; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D017955:Poliovirus / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D014764:Viral Proteins / Q000235:genetics* / Q000302:isolation & purification
D009227:Myristic Acids; D009829:Oleic Acids; D010169:Palmitic Acids; D010710:Phosphates; D014764:Viral Proteins; D019814:Myristic Acid; D019301:Oleic Acid; D019308:Palmitic Acid