Glycosylation of measles virus haemagglutinin protein in infected cells
スポンサーリンク
概要
- 論文の詳細を見る
Processing of the measles virus haemagglutinin (H) protein was analysed by the pulse-chase method, immunoprecipitation with an anti-H monoclonal antibody and SDS-polyacrylamide gel electrophoresis, combined with the addition of carbonyl cyanide m-chlorophenylhydrazone (CCCP) or monensin (inhibitors of intracellular processing of secretory proteins) to cultures and digestion of the protein with endoglycosidase H or neuraminidase. The apparent M(r) of the H protein was increased from 74K to 78K during the chase period. Addition of either CCCP or monensin to the chase medium inhibited the appearance of the 78K H protein, but not the immunoreactivity of the H protein or dimer formation, suggesting that these two events occur in the rough endoplasmic reticulum. The 74K H protein processed in the presence of CCCP was fully sensitive to endoglycosidase H digestion, whereas the 74K H protein processed in the presence of monensin was partially resistant to endoglycosidase H. In experiments using 3H-labelled sugars, [3H]galactose was incorporated into the 74K H protein in the presence of monensin. Neuraminidase treatment increased the electrophoretic mobility of the 78K H protein to 74K. Only the 78K H protein was detected on the surface of untreated cells, and it was resistant to endoglycosidase H digestion. These data suggest that after galactose addition sialic acid is added to the H protein in the trans-Golgi complex and then the mature 78K H protein is transported to the cell surface.
- Society for General Microbiologyの論文
Society for General Microbiology | 論文
- Detection and assignment of proteins encoded by rice black streaked dwarf fijivirus S7, S8, S9 and S10
- Rice ragged stunt Oryzavirus genome segment 9 encodes a 38 600 Mr structural protein
- Phylogenetic and virulence analysis of tick-borne encephalitis viruses from Japan and far-eastern Russia
- Hypothesis on particle structure and assembly of rice dwarf phytoreovirus: interactions among multiple structural proteins
- The central and C-terminal domains of VPg of Clover yellow vein virus are important for VPg–HCPro and VPg–VPg interactions