Stability of intracellular influenza virus nucleocapsid protein oligomers
العنوان: | Stability of intracellular influenza virus nucleocapsid protein oligomers |
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المؤلفون: | Prokudina En, N. P. Semenova, Chumakov Vm |
المصدر: | Archives of Virology. 150:833-839 |
بيانات النشر: | Springer Science and Business Media LLC, 2005. |
سنة النشر: | 2005 |
مصطلحات موضوعية: | Protein Conformation, Detergents, Orthomyxoviridae, General Medicine, Hydrogen-Ion Concentration, Biology, medicine.disease_cause, biology.organism_classification, Virology, Oligomer, Hydrophobic effect, chemistry.chemical_compound, Protein structure, chemistry, Influenza A virus, Ionic strength, medicine, RNA, Viral, Thermodynamics, Salts, Chemical stability, Nucleocapsid, Intracellular |
الوصف: | 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. |
تدمد: | 1432-8798 0304-8608 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0817fdf8d26e42231ffb1ac53e69fd3b https://doi.org/10.1007/s00705-004-0425-5 |
حقوق: | CLOSED |
رقم الأكسشن: | edsair.doi.dedup.....0817fdf8d26e42231ffb1ac53e69fd3b |
قاعدة البيانات: | OpenAIRE |
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