[Relationship of nuclear import of influenza virus nucleoprotein polymers to their conformational status].
It has been earlier shown that in the cells infected with influenza virus, the molecules of nucleoprotein (NP) are polymers that differ in their conformational maturity and stability. The present investigation has studied the ability of different conformational forms of NP polymers to migrate into the nucleus. Conformationally mature compact NP oligomers are shown to predominantly import into the nucleus. In contrast, unstable, loose, and conformationally immature NP multimers accumulate in the cytoplasm and do not migrate into the nucleus. The present investigation is the first evidence for that that the conformational maturity of influenza virus NPs is essential for their nuclear traffic and, hence, for participation in the transcription and replication of viral genomes.
Semenova
N P
NP
Chumakov
V M
VM
Grigor'eva
T A
TA
Prokudina
E N
EN
D021581:Active Transport, Cell Nucleus; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004285:Dogs; D004372:Ducks / Q000821:virology; D053123:Influenza A Virus, H3N8 Subtype / Q000378:metabolism*; D005585:Influenza in Birds / Q000378:metabolism* / Q000821:virology; D011487:Protein Conformation; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism*
D014758:Viral Core Proteins