Stability of intracellular influenza virus nucleocapsid protein oligomers.
Stability of A/Duck/Ukrainae/63 (H3N8) influenza virus intracellular NP oligomers was studied using reducing agents, denaturants, detergents, salts, various pH and a range of temperatures. The results obtained indicate that influenza virus NP oligomers are noncovalently stabilized, and NP subunits are not linked by disulfide bonds. NP oligomers are thermostable and SDS resistant. Urea and high ionic strength also do not dissociate avian influenza virus intracellular NP oligomers. However, NP oligomers are completely dissociated at pH < 5. The data obtained suggest that hydrophobic bonds together with the electrostatic interactions take part in the stabilization of compact conformation of influenza virus NP oligomers. It was also shown that intrachain disulfides revealed in nascent NPs are reduced in NP subunits of NP oligomers, and this probably contributes to the stability and compactness of the oligomers.
Prokudina
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EN
D. I. Ivanovsky Institute of Virology, Moscow, Russia. prokudinaen@mail.ru
Semenova
N P
NP
Chumakov
V M
VM
D003902:Detergents / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus / Q000502:physiology*; D019251:Nucleocapsid / Q000737:chemistry* / Q000187:drug effects / Q000302:isolation & purification; D011487:Protein Conformation; D012367:RNA, Viral / Q000235:genetics; D012492:Salts / Q000494:pharmacology; D013816:Thermodynamics
D003902:Detergents; D012367:RNA, Viral; D012492:Salts