title: [Polymeric forms of the influenza virus nucleoprotein].
abstract: Two high-molecular-weight types of in vivo formed nucleoproteins (NP) capable of reacting with anti-NP monoclonal antibodies were detected in continuous MDCK cells and primary CEFs, along with the monomeric virus NP. High-molecular NP were stable at 37 degrees C, despite the presence of dodecyl sulfate and B-mercaptoethanol, but were converted to monomeric NP at 37 degrees C in the presence of 6 M urea, 1 M NaCl, and at acid pH. Hence, high-molecular-weight NP may be the polymeric forms of NP, which are probably stabilized by noncovalent bonds. The kinetics of NP-polymers formation suggests that NP-monomers are their precursors and NP-polymers are formed rapidly after monomeric NP molecules synthesis. Both forms of NP-polymers are detected in the sedimented and soluble fractions of not only cell lysate, but in the extracellular maintenance medium as well. NP-polymers are resistant to RNAse and are more resistant to protease than NP-monomers.
mesh_terms: D000818:Animals; D001704:Biopolymers; D002478:Cells, Cultured; D004285:Dogs; D009980:Influenza A virus / Q000737:chemistry*; D007700:Kinetics; D008970:Molecular Weight; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000096:biosynthesis / Q000737:chemistry*; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins / Q000096:biosynthesis / Q000737:chemistry*
chemical_list: D001704:Biopolymers; C048842:NP protein, Influenza A virus; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins
vernacular_title: Polimernye formy nukleoproteina virusa grippa.