Association of the nucleocapsid protein N of vesicular stomatitis virus with phospholipid vesicles containing the matrix protein M.
The matrix protein M and the nucleocapsid protein N were isolated from vesicular stomatitis virus and reconstituted into artificial phospholipid vesicles. While the M protein could be reconstituted into phospholipid vesicles, the N protein had no affinity for lipid vesicles. The N protein could, however, associate with phospholipid vesicles in the presence of M protein. Identical results were also obtained when an in vitro system synthesizing M and N proteins was used for reconstitution. The results suggest that M protein is involved in virus maturation by interacting with the viral envelope and the N protein of the nucleoprotein core.
D000818:Animals; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007739:L Cells / Q000378:metabolism; D008081:Liposomes; D051379:Mice; D011485:Protein Binding; D014176:Protein Biosynthesis; D012156:Reticulocytes / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D008081:Liposomes; D014763:Viral Matrix Proteins; D014764:Viral Proteins