[Role of certain factors in intracellular oligomerization of influenza virus nucleoproteins].
Oligomerization of influenza virus nucleoprotein (NP) depends on the virus strain. NP monomers of viruses A/Duck/Ukraine/63 (H3N8) and A/Seal/Massachusets/1/80/ (H7N7) are oligomerized completely. The A/USSR/90/77 virus (H1N1) NP is characterized by just partial oligomerization, similarly as a reassortant containing surface protein genes of virus A/Duck/Ukraine and internal protein genes of A/USSR/90 virus. Hence, it is probable that NP gene controls the type of NP oligomerization. NP oligomerization is shown to depend on the temperature, the optimal t = 37 degrees C, but not on the type of cells or intracellular concentration of total NP. NP oligomers forming in vivo are believed to differ from NP oligomers formed in vitro described previously.
Semenova
N P
NP
Chumakov
V M
VM
Rudneva
I A
IA
Prokudina
E N
EN
D000818:Animals; D001704:Biopolymers; D002460:Cell Line; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D009980:Influenza A virus / Q000378:metabolism*; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000378:metabolism*; D016601:RNA-Binding Proteins; D013552:Swine; D013696:Temperature; D014758:Viral Core Proteins / Q000378:metabolism*
D001704:Biopolymers; C048842:NP protein, Influenza A virus; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins