Formation of vesicular stomatitis virus nucleocapsid from cytoskeletal framework-bound N protein: possible model for structure assembly.

AUTOR(ES)

Chatterjee, P K

RESUMO

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.

Documentos Relacionados

• Study of the Assembly of Vesicular Stomatitis Virus N Protein: Role of the P Protein
• Stereo images of vesicular stomatitis virus assembly.
• Heterogeneity of vesicular stomatitis virus particles: implications for virion assembly.
• The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly.
• Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA.