title: [Complete oligomerization of the nucleoprotein and various strains of influenza virus].
abstract: Previously we demonstrated that in the course of intracellular reproduction of WSN influenza virus strain, part of monomeric nucleoprotein (NP) undergo polymerization into dimers and trimers, which dissociate into monomers after boiling. Further studies showed that different strains of influenza virus are characterized by different degree of NP-oligomerization. Specifically, Duck/ Ukraine/63 (H3N8) and Seal Massacuhsets 1/80 (H7N7) NP monomers are completely transformed into oligomers. As a result of 40-min chase and of prolonged label exposure only NP-oligomers but not monomers can be detected in unboiled samples of infected cells or in virions. NP monomers of A/Duck/Ukraine strain are detectable in unboiled samples only after a short period of labeling. Influenza virus NP oligomers are more hydrophobic than NP monomers. Oligomers are hypothesized to be the native functionally important form of influenza virus NP.
authors.forename: N P
authors.initials: NP
authors.lastname: Semenova
authors.forename: E N
authors.initials: EN
authors.lastname: Prokudina
authors.forename: V M
authors.initials: VM
authors.lastname: Chumakov
mesh_terms: D000818:Animals; D006801:Humans; D009980:Influenza A virus / Q000737:chemistry*; D008970:Molecular Weight; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000302:isolation & purification*; D011108:Polymers; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins / Q000302:isolation & purification*
chemical_list: C048842:NP protein, Influenza A virus; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D011108:Polymers; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins