Formation of vesicular stomatitis virus nucleocapsid from cytoskeletal framework-bound N protein: possible model for structure assembly.
The pathway of vesicular stomatitis virus N protein from synthesis to assembly into capsids was studied by use of detergent extraction of infected HeLa cells together with protein cross-linking. One half of the newly synthesized N protein was extracted with the soluble cell proteins and, when cross-linked, never formed the N-N dimer characteristic of mature nucleocapsids. In contrast, the cytoskeleton-bound N protein first showed a diffuse spectrum of protein-protein cross-links but, after a lag of 40 min, assumed the cross-link pattern of N protein in nucleocapsids. The efficiency of forming N-N cross-linked dimers is the same for N protein on the skeleton as in nucleocapsids derived from mature virus, suggesting very similar configurations. However, the N protein bound on the skeletal framework formed several additional cross-links that were not found in mature virus and were apparently formed to cellular proteins estimated to be ca. approximately 46,000 and 60,000 in molecular weight.
D002213:Capsid / Q000302:isolation & purification* / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D008970:Molecular Weight; D013997:Time Factors; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014764:Viral Proteins / Q000302:isolation & purification* / Q000378:metabolism
D014764:Viral Proteins